ID   HLAA_HUMAN              Reviewed;         365 AA.
AC   P04439; B1PKZ3; O02939; O02954; O02955; O02963; O19509; O19546; O19598;
AC   O19605; O19606; O19619; O19647; O19673; O19687; O19695; O19756; O19794;
AC   O19795; O43906; O43907; O46874; O62921; O62924; O77937; O77938; O77964;
AC   O78073; O78171; O98009; O98010; O98011; O98137; P01891; P01892; P05534;
AC   P06338; P10313; P10314; P10315; P10316; P13746; P16188; P16189; P16190;
AC   P18462; P30443; P30444; P30445; P30446; P30447; P30448; P30449; P30450;
AC   P30451; P30452; P30453; P30454; P30455; P30456; P30457; P30458; P30459;
AC   P30512; P30514; P79505; P79562; P79563; Q09160; Q29680; Q29747; Q29835;
AC   Q29837; Q29838; Q29899; Q29908; Q29909; Q29910; Q30208; Q31623; Q5S3G1;
AC   Q65A82; Q8MHM1; Q8MHN9; Q95352; Q95355; Q95362; Q95377; Q95380; Q95IZ5;
AC   Q9BCN0; Q9BD15; Q9BD19; Q9GJE6; Q9GJE7; Q9GJE8; Q9MW42; Q9MY89; Q9MYA3;
AC   Q9MYA5; Q9MYC4; Q9MYE6; Q9MYE9; Q9MYG4; Q9MYG5; Q9MYI5; Q9TP25; Q9TPQ3;
AC   Q9TPR8; Q9TPX8; Q9TPX9; Q9TPY0; Q9TQ24; Q9TQE8; Q9TQE9; Q9TQF1; Q9TQF5;
AC   Q9TQF8; Q9TQF9; Q9TQG0; Q9TQG5; Q9TQG7; Q9TQH5; Q9TQI3; Q9TQK5; Q9TQM6;
AC   Q9TQN5; Q9TQP5; Q9TQP6; Q9TQP7; Q9UIN1; Q9UIN2; Q9UIP7; Q9UQU3; Q9UQU6;
AC   Q9UQU7;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   12-OCT-2022, entry version 208.
DE   RecName: Full=HLA class I histocompatibility antigen, A alpha chain;
DE   AltName: Full=Human leukocyte antigen A;
DE            Short=HLA-A;
DE   Flags: Precursor;
GN   Name=HLA-A {ECO:0000312|HGNC:HGNC:4931}; Synonyms=HLAA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE OF 25-298 (ALLELE A*32:01).
RX   PubMed=2431040;
RA   Wan A.M., Ennis P., Parham P., Holmes N.;
RT   "The primary structure of HLA-A32 suggests a region involved in formation
RT   of the Bw4/Bw6 epitopes.";
RL   J. Immunol. 137:3671-3674(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:05).
RX   PubMed=3496393;
RA   Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.;
RT   "Multiple genetic mechanisms have contributed to the generation of the HLA-
RT   A2/A28 family of class I MHC molecules.";
RL   J. Immunol. 139:936-941(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:01).
RX   PubMed=2460344; DOI=10.1002/j.1460-2075.1988.tb03131.x;
RA   Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., Klein J.;
RT   "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for
RT   trans-species mode of evolution.";
RL   EMBO J. 7:2765-2774(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*29:01).
RX   PubMed=2461903; DOI=10.1007/bf02341610;
RA   Trapani J.A., Mizuno S., Kang S.H., Yang S.Y., Dupont B.;
RT   "Molecular mapping of a new public HLA class I epitope shared by all HLA-B
RT   and HLA-C antigens and defined by a monoclonal antibody.";
RL   Immunogenetics 29:25-32(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELES A*30:01; A*31:01 AND
RP   A*33:01).
RX   PubMed=2478623;
RA   Kato K., Trapani J.A., Allopenna J., Dupont B., Yang S.Y.;
RT   "Molecular analysis of the serologically defined HLA-Aw19 antigens. A
RT   genetically distinct family of HLA-A antigens comprising A29, A31, A32, and
RT   Aw33, but probably not A30.";
RL   J. Immunol. 143:3371-3378(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE A*01:01).
RX   PubMed=2715640;
RA   Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.;
RT   "Diversity and diversification of HLA-A,B,C alleles.";
RL   J. Immunol. 142:3937-3950(1989).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*02:01 AND A*25:01).
RX   PubMed=2320591; DOI=10.1073/pnas.87.7.2833;
RA   Ennis P.D., Zemmour J., Salter R.D., Parham P.;
RT   "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction:
RT   frequency and nature of errors produced in amplification.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*29:02).
RX   PubMed=1782566;
RA   Tabary T., Prochnicka-Chalufour A., Cornillet P., Lehoang P., Betuel H.,
RA   Cohen H.M.;
RT   "HLA-A29 sub-types and 'Birdshot' choroido-retinopathy susceptibility: a
RT   possible 'resistance motif' in the HLA-A29.1 molecule.";
RL   C. R. Acad. Sci. III, Sci. Vie 313:599-605(1991).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*23:01 AND A*24:02).
RX   PubMed=1729171; DOI=10.1007/bf00216625;
RA   Little A.-M., Madrigal J.A., Parham P.;
RT   "Molecular definition of an elusive third HLA-A9 molecule: HLA-A9.3.";
RL   Immunogenetics 35:41-45(1992).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*34:01; A*36:01; A*43:01; A*66:01 AND
RP   A*74:01).
RX   PubMed=1431115;
RA   Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., Little A.-M.,
RA   Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., Martell R.W.,
RA   du Toit E.D., Parham P.;
RT   "Distinctive HLA-A,B antigens of black populations formed by interallelic
RT   conversion.";
RL   J. Immunol. 149:3411-3415(1992).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*31:01).
RX   PubMed=1317015; DOI=10.1038/357326a0;
RA   Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., Williams R.C.,
RA   Luz R., Petzl-Erler M.L., Parham P.;
RT   "Unusual HLA-B alleles in two tribes of Brazilian Indians.";
RL   Nature 357:326-329(1992).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*26:01).
RX   PubMed=8475492; DOI=10.1111/j.1399-0039.1993.tb01982.x;
RA   Madrigal J.A., Hildebrand W.H., Belich M.P., Benjamin R.J., Little A.-M.,
RA   Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., du Toit E.D.,
RA   Parham P.;
RT   "Structural diversity in the HLA-A10 family of alleles: correlations with
RT   serology.";
RL   Tissue Antigens 41:72-80(1993).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*80:01).
RX   PubMed=8284791; DOI=10.1111/j.1399-0039.1993.tb02186.x;
RA   Domena J.D., Hildebrand W.H., Bias W.B., Parham P.;
RT   "A sixth family of HLA-A alleles defined by HLA-A*8001.";
RL   Tissue Antigens 42:156-159(1993).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*26:01).
RC   TISSUE=Blood;
RX   PubMed=8026990; DOI=10.1016/0198-8859(94)90263-1;
RA   Ishikawa Y., Tokunaga K., Lin L., Imanishi T., Saitou S., Kashiwase K.,
RA   Akaza T., Tadokoro K., Juji T.;
RT   "Sequences of four splits of HLA-A10 group. Implications for serologic
RT   cross-reactivities and their evolution.";
RL   Hum. Immunol. 39:220-224(1994).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*80:01).
RX   PubMed=8188325; DOI=10.1007/bf00176169;
RA   Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.;
RT   "Characterization of a new and highly distinguishable HLA-A allele in a
RT   Spanish family.";
RL   Immunogenetics 39:452-452(1994).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:01).
RX   PubMed=8016845; DOI=10.1111/j.1399-0039.1994.tb02304.x;
RA   Lin L., Tokunaga K., Ishikawa Y., Bannai M., Kashiwase K., Kuwata S.,
RA   Akaza T., Tadokoro K., Shibata Y., Juji T.;
RT   "Sequence analysis of serological HLA-A11 split antigens, A11.1 and
RT   A11.2.";
RL   Tissue Antigens 43:78-82(1994).
RN   [17]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*30:01).
RX   PubMed=7871528; DOI=10.1111/j.1399-0039.1994.tb02393.x;
RA   Olerup O., Daniels T.J., Baxter-Lowe L.;
RT   "Correct sequence of the A*3001 allele obtained by PCR-SSP typing and
RT   automated nucleotide sequencing.";
RL   Tissue Antigens 44:265-267(1994).
RN   [18]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:01) (ISOFORM 2).
RX   PubMed=17092262; DOI=10.1111/j.1399-0039.2006.00687.x;
RA   Sun Y., Liu S., Luo Y., Liang F., Xi Y.;
RT   "Identification and frequency of a novel HLA-A allele, A*110104.";
RL   Tissue Antigens 68:453-454(2006).
RN   [19]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*03:01).
RX   PubMed=6609814; DOI=10.1002/j.1460-2075.1984.tb01901.x;
RA   Strachan T., Sodoyer R., Damotte M., Jordan B.R.;
RT   "Complete nucleotide sequence of a functional class I HLA gene, HLA-A3:
RT   implications for the evolution of HLA genes.";
RL   EMBO J. 3:887-894(1984).
RN   [20]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-297 (ALLELES A*68:01 AND A*69:01).
RX   PubMed=3877632; DOI=10.1002/j.1460-2075.1985.tb04013.x;
RA   Holmes N., Parham P.;
RT   "Exon shuffling in vivo can generate novel HLA class I molecules.";
RL   EMBO J. 4:2849-2854(1985).
RN   [21]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
RX   PubMed=2982951;
RA   Koller B.H., Orr H.T.;
RT   "Cloning and complete sequence of an HLA-A2 gene: analysis of two HLA-A
RT   alleles at the nucleotide level.";
RL   J. Immunol. 134:2727-2733(1985).
RN   [22]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-365 (ALLELE A*11:01).
RX   PubMed=2437024; DOI=10.1007/bf00404694;
RA   Cowan E.P., Jelachich M.L., Biddison W.E., Coligan J.E.;
RT   "DNA sequence of HLA-A11: remarkable homology with HLA-A3 allows
RT   identification of residues involved in epitopes recognized by antibodies
RT   and T cells.";
RL   Immunogenetics 25:241-250(1987).
RN   [23]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01).
RX   PubMed=2251137; DOI=10.1093/nar/18.22.6701;
RA   Girdlestone J.;
RT   "Nucleotide sequence of an HLA-A1 gene.";
RL   Nucleic Acids Res. 18:6701-6701(1990).
RN   [24]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
RC   TISSUE=Blood;
RX   PubMed=7836067; DOI=10.1016/0198-8859(94)90087-6;
RA   Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.;
RT   "HLA class I allele (HLA-A2) expression defect associated with a mutation
RT   in its enhancer B inverted CAT box in two families.";
RL   Hum. Immunol. 41:69-73(1994).
RN   [25]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*31:01).
RX   PubMed=8795145; DOI=10.1111/j.1399-0039.1996.tb02580.x;
RA   Arnett K.L., Adams E.J., Parham P.;
RT   "On the sequence of A*3101.";
RL   Tissue Antigens 47:428-430(1996).
RN   [26]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*24:02).
RX   PubMed=9349616; DOI=10.1111/j.1399-0039.1997.tb02884.x;
RA   Laforet M., Froelich N., Parissiadis A., Bausinger H., Pfeiffer B.,
RA   Tongio M.M.;
RT   "An intronic mutation responsible for a low level of expression of an HLA-
RT   A*24 allele.";
RL   Tissue Antigens 50:340-346(1997).
RN   [27]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01).
RX   PubMed=9349617; DOI=10.1111/j.1399-0039.1997.tb02885.x;
RA   Laforet M., Froelich N., Parissiadis A., Pfeiffer B., Schell A., Faller B.,
RA   Woehl-Jaegle M.L., Cazenave J.-P., Tongio M.M.;
RT   "A nucleotide insertion in exon 4 is responsible for the absence of
RT   expression of an HLA-A*01 allele.";
RL   Tissue Antigens 50:347-350(1997).
RN   [28]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*69:01).
RX   PubMed=19735485; DOI=10.1111/j.1744-313x.2009.00874.x;
RA   Zhu F., He Y., Zhang W., He J., He J., Xu X., Yan L.;
RT   "Analysis of the complete genomic sequence of HLA-A alleles in the Chinese
RT   Han population.";
RL   Int. J. Immunogenet. 36:351-360(2009).
RN   [29]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*32:01).
RA   Domena J.D.;
RL   Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN   [30]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*74:01).
RA   Hurley C.K.;
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN   [31]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*03:01).
RA   Ellexson M.E., Hildebrand W.H.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [32]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*03:01).
RA   Mayor N.P.;
RT   "Full length sequence of an HLA-A*0301 intron 2 variant.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [33]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [34]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [35]
RP   PROTEIN SEQUENCE OF 25-295 (ALLELE A*02:01).
RX   PubMed=92029; DOI=10.1073/pnas.76.9.4395;
RA   Orr H.T., Lopez de Castro J.A., Parham P., Ploegh H.L., Strominger J.L.;
RT   "Comparison of amino acid sequences of two human histocompatibility
RT   antigens, HLA-A2 and HLA-B7: location of putative alloantigenic sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 76:4395-4399(1979).
RN   [36]
RP   PROTEIN SEQUENCE OF 25-294 (ALLELE A*68:01).
RX   PubMed=6179086; DOI=10.1073/pnas.79.12.3813;
RA   Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.;
RT   "Structure of crossreactive human histocompatibility antigens HLA-A28 and
RT   HLA-A2: possible implications for the generation of HLA polymorphism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982).
RN   [37]
RP   FUNCTION (ALLELE A*03:01), AND CHARACTERIZATION OF VARIANT VAL-176.
RX   PubMed=2456340;
RA   Jelachich M.L., Cowan E.P., Turner R.V., Coligan J.E., Biddison W.E.;
RT   "Analysis of the molecular basis of HLA-A3 recognition by cytotoxic T cells
RT   using defined mutants of the HLA-A3 molecule.";
RL   J. Immunol. 141:1108-1113(1988).
RN   [38]
RP   FUNCTION (ALLELES A*02:01 AND A*68:01), INTERACTION WITH CD8A, DOMAIN, AND
RP   CHARACTERIZATION OF VARIANT VAL-269.
RX   PubMed=2784196; DOI=10.1038/338345a0;
RA   Salter R.D., Norment A.M., Chen B.P., Clayberger C., Krensky A.M.,
RA   Littman D.R., Parham P.;
RT   "Polymorphism in the alpha 3 domain of HLA-A molecules affects binding to
RT   CD8.";
RL   Nature 338:345-347(1989).
RN   [39]
RP   FUNCTION (ALLELE A*01:01).
RX   PubMed=1402688; DOI=10.1084/jem.176.5.1453;
RA   Traversari C., van der Bruggen P., Luescher I.F., Lurquin C., Chomez P.,
RA   Van Pel A., De Plaen E., Amar-Costesec A., Boon T.;
RT   "A nonapeptide encoded by human gene MAGE-1 is recognized on HLA-A1 by
RT   cytolytic T lymphocytes directed against tumor antigen MZ2-E.";
RL   J. Exp. Med. 176:1453-1457(1992).
RN   [40]
RP   FUNCTION (ALLELES A*01:01 AND A*03:01), AND INTERACTION WITH B2M AND
RP   PEPTIDE.
RX   PubMed=7504010;
RA   DiBrino M., Tsuchida T., Turner R.V., Parker K.C., Coligan J.E.,
RA   Biddison W.E.;
RT   "HLA-A1 and HLA-A3 T cell epitopes derived from influenza virus proteins
RT   predicted from peptide binding motifs.";
RL   J. Immunol. 151:5930-5935(1993).
RN   [41]
RP   FUNCTION (ALLELE A*03:01), AND INTERACTION WITH B2M AND PEPTIDE.
RX   PubMed=7679507; DOI=10.1073/pnas.90.4.1508;
RA   DiBrino M., Parker K.C., Shiloach J., Knierman M., Lukszo J., Turner R.V.,
RA   Biddison W.E., Coligan J.E.;
RT   "Endogenous peptides bound to HLA-A3 possess a specific combination of
RT   anchor residues that permit identification of potential antigenic
RT   peptides.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:1508-1512(1993).
RN   [42]
RP   FUNCTION (ALLELE A*01:01), AND INTERACTION WITH B2M AND PEPTIDE.
RX   PubMed=7506728;
RA   DiBrino M., Parker K.C., Shiloach J., Turner R.V., Tsuchida T.,
RA   Garfield M., Biddison W.E., Coligan J.E.;
RT   "Endogenous peptides with distinct amino acid anchor residue motifs bind to
RT   HLA-A1 and HLA-B8.";
RL   J. Immunol. 152:620-631(1994).
RN   [43]
RP   FUNCTION (ALLELE A*02:01), MUTAGENESIS OF SER-156 AND THR-158, DOMAIN,
RP   INTERACTION WITH B2M, INTERACTION WITH TAP1-TAP2 COMPLEX, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=8805302; DOI=10.1016/s0960-9822(02)00611-5;
RA   Lewis J.W., Neisig A., Neefjes J., Elliott T.;
RT   "Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally
RT   relevant interaction with TAP.";
RL   Curr. Biol. 6:873-883(1996).
RN   [44]
RP   FUNCTION (ALLELE A*02:01), INTERACTION WITH TAP1-TAP2 COMPLEX, AND
RP   MUTAGENESIS OF THR-158.
RX   PubMed=8630735; DOI=10.1016/s1074-7613(00)80416-1;
RA   Peace-Brewer A.L., Tussey L.G., Matsui M., Li G., Quinn D.G.,
RA   Frelinger J.A.;
RT   "A point mutation in HLA-A*0201 results in failure to bind the TAP complex
RT   and to present virus-derived peptides to CTL.";
RL   Immunity 4:505-514(1996).
RN   [45]
RP   FUNCTION (ALLELE A*29:02).
RX   PubMed=8622959; DOI=10.1073/pnas.93.8.3466;
RA   Boisgerault F., Khalil I., Tieng V., Connan F., Tabary T., Cohen J.H.,
RA   Choppin J., Charron D., Toubert A.;
RT   "Definition of the HLA-A29 peptide ligand motif allows prediction of
RT   potential T-cell epitopes from the retinal soluble antigen, a candidate
RT   autoantigen in birdshot retinopathy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:3466-3470(1996).
RN   [46]
RP   FUNCTION (ALLELE A*24:02).
RX   PubMed=9047241; DOI=10.1016/s1074-7613(00)80426-4;
RA   Ikeda H., Lethe B.G., Lehmann F., van Baren N., Baurain J.-F., de Smet C.,
RA   Chambost H., Vitale M., Moretta A., Boon T., Coulie P.G.;
RT   "Characterization of an antigen that is recognized on a melanoma showing
RT   partial HLA loss by CTL expressing an NK inhibitory receptor.";
RL   Immunity 6:199-208(1997).
RN   [47]
RP   FUNCTION (ALLELE A*03:01).
RX   PubMed=9862734;
RA   Kawakami Y., Robbins P.F., Wang X., Tupesis J.P., Parkhurst M.R., Kang X.,
RA   Sakaguchi K., Appella E., Rosenberg S.A.;
RT   "Identification of new melanoma epitopes on melanosomal proteins recognized
RT   by tumor infiltrating T lymphocytes restricted by HLA-A1, -A2, and -A3
RT   alleles.";
RL   J. Immunol. 161:6985-6992(1998).
RN   [48]
RP   FUNCTION (ALLELE A*11:01).
RX   PubMed=10449296; DOI=10.1097/00002030-199907300-00021;
RA   Fukada K., Chujoh Y., Tomiyama H., Miwa K., Kaneko Y., Oka S.,
RA   Takiguchi M.;
RT   "HLA-A*1101-restricted cytotoxic T lymphocyte recognition of HIV-1 Pol
RT   protein.";
RL   AIDS 13:1413-1414(1999).
RN   [49]
RP   INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION).
RX   PubMed=11390610; DOI=10.1128/jvi.75.13.6086-6094.2001;
RA   Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L., Mulloy J.C.,
RA   Jacobson S., Franchini G.;
RT   "Free major histocompatibility complex class I heavy chain is
RT   preferentially targeted for degradation by human T-cell
RT   leukemia/lymphotropic virus type 1 p12(I) protein.";
RL   J. Virol. 75:6086-6094(2001).
RN   [50]
RP   INTERACTION WITH HUMAN HERPESVIRUS 8 MIR1 PROTEIN (MICROBIAL INFECTION),
RP   AND UBIQUITINATION (MICROBIAL INFECTION).
RX   PubMed=12006494; DOI=10.1093/emboj/21.10.2418;
RA   Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G., Lehner P.J.;
RT   "Ubiquitylation of MHC class I by the K3 viral protein signals
RT   internalization and TSG101-dependent degradation.";
RL   EMBO J. 21:2418-2429(2002).
RN   [51]
RP   FUNCTION (ALLELE A*02:01).
RX   PubMed=12138174; DOI=10.1073/pnas.112331099;
RA   Nagata Y., Ono S., Matsuo M., Gnjatic S., Valmori D., Ritter G.,
RA   Garrett W., Old L.J., Mellman I.;
RT   "Differential presentation of a soluble exogenous tumor antigen, NY-ESO-1,
RT   by distinct human dendritic cell populations.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10629-10634(2002).
RN   [52]
RP   FUNCTION (ALLELE A*24:02).
RX   PubMed=12393434; DOI=10.1182/blood-2002-04-1240;
RA   Kuzushima K., Hayashi N., Kudoh A., Akatsuka Y., Tsujimura K.,
RA   Morishima Y., Tsurumi T.;
RT   "Tetramer-assisted identification and characterization of epitopes
RT   recognized by HLA A*2402-restricted Epstein-Barr virus-specific CD8+ T
RT   cells.";
RL   Blood 101:1460-1468(2003).
RN   [53]
RP   FUNCTION (ALLELE A*26:01).
RX   PubMed=15893615; DOI=10.1016/j.vaccine.2005.02.022;
RA   Satoh M., Takamiya Y., Oka S., Tokunaga K., Takiguchi M.;
RT   "Identification and characterization of HIV-1-specific CD8+ T cell epitopes
RT   presented by HLA-A*2601.";
RL   Vaccine 23:3783-3790(2005).
RN   [54]
RP   FUNCTION (ALLELE A*01:01).
RX   PubMed=17189421; DOI=10.1158/1078-0432.ccr-06-1337;
RA   Asemissen A.M., Keilholz U., Tenzer S., Mueller M., Walter S.,
RA   Stevanovic S., Schild H., Letsch A., Thiel E., Rammensee H.G.,
RA   Scheibenbogen C.;
RT   "Identification of a highly immunogenic HLA-A*01-binding T cell epitope of
RT   WT1.";
RL   Clin. Cancer Res. 12:7476-7482(2006).
RN   [55]
RP   FUNCTION (ALLELES A*23:01; A*24:02 AND A*32:01), AND INTERACTION WITH
RP   KIR3DL1.
RX   PubMed=17182537; DOI=10.4049/jimmunol.178.1.33;
RA   Thananchai H., Gillespie G., Martin M.P., Bashirova A., Yawata N.,
RA   Yawata M., Easterbrook P., McVicar D.W., Maenaka K., Parham P.,
RA   Carrington M., Dong T., Rowland-Jones S.;
RT   "Cutting Edge: Allele-specific and peptide-dependent interactions between
RT   KIR3DL1 and HLA-A and HLA-B.";
RL   J. Immunol. 178:33-37(2007).
RN   [56]
RP   FUNCTION (ALLELE A*02:01).
RX   PubMed=17079320; DOI=10.1128/jvi.01779-06;
RA   Robek M.D., Garcia M.L., Boyd B.S., Chisari F.V.;
RT   "Role of immunoproteasome catalytic subunits in the immune response to
RT   hepatitis B virus.";
RL   J. Virol. 81:483-491(2007).
RN   [57]
RP   FUNCTION (ALLELE A*24:02), AND INTERACTION WITH KIR3DL1.
RX   PubMed=18502829; DOI=10.1182/blood-2008-02-137521;
RA   Stern M., Ruggeri L., Capanni M., Mancusi A., Velardi A.;
RT   "Human leukocyte antigens A23, A24, and A32 but not A25 are ligands for
RT   KIR3DL1.";
RL   Blood 112:708-710(2008).
RN   [58]
RP   FUNCTION (ALLELE A*01:01).
RX   PubMed=18779413; DOI=10.1182/blood-2008-06-162883;
RA   Brennan R.M., Burrows S.R.;
RT   "A mechanism for the HLA-A*01-associated risk for EBV+ Hodgkin lymphoma and
RT   infectious mononucleosis.";
RL   Blood 112:2589-2590(2008).
RN   [59]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [60]
RP   FUNCTION (ALLELE A*03:01).
RX   PubMed=19543285; DOI=10.1038/nmeth.1345;
RA   Hadrup S.R., Bakker A.H., Shu C.J., Andersen R.S., van Veluw J.,
RA   Hombrink P., Castermans E., Thor Straten P., Blank C., Haanen J.B.,
RA   Heemskerk M.H., Schumacher T.N.;
RT   "Parallel detection of antigen-specific T-cell responses by
RT   multidimensional encoding of MHC multimers.";
RL   Nat. Methods 6:520-526(2009).
RN   [61]
RP   FUNCTION (ALLELE A*01:01).
RX   PubMed=20364150; DOI=10.1038/ni.1862;
RA   Parmentier N., Stroobant V., Colau D., de Diesbach P., Morel S.,
RA   Chapiro J., van Endert P., Van den Eynde B.J.;
RT   "Production of an antigenic peptide by insulin-degrading enzyme.";
RL   Nat. Immunol. 11:449-454(2010).
RN   [62]
RP   NOMENCLATURE.
RX   PubMed=20356336; DOI=10.1111/j.1399-0039.2010.01466.x;
RA   Marsh S.G., Albert E.D., Bodmer W.F., Bontrop R.E., Dupont B., Erlich H.A.,
RA   Fernandez-Vina M., Geraghty D.E., Holdsworth R., Hurley C.K., Lau M.,
RA   Lee K.W., Mach B., Maiers M., Mayr W.R., Mueller C.R., Parham P.,
RA   Petersdorf E.W., Sasazuki T., Strominger J.L., Svejgaard A., Terasaki P.I.,
RA   Tiercy J.M., Trowsdale J.;
RT   "Nomenclature for factors of the HLA system, 2010.";
RL   Tissue Antigens 75:291-455(2010).
RN   [63]
RP   INDUCTION BY IFNG, GLYCOSYLATION AT ASN-110, MUTAGENESIS OF ASN-110,
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH TAPBP.
RX   PubMed=21263072; DOI=10.4049/jimmunol.1002959;
RA   Rizvi S.M., Del Cid N., Lybarger L., Raghavan M.;
RT   "Distinct functions for the glycans of tapasin and heavy chains in the
RT   assembly of MHC class I molecules.";
RL   J. Immunol. 186:2309-2320(2011).
RN   [64]
RP   FUNCTION (ALLELE A*74:01).
RX   PubMed=21498667; DOI=10.4049/jimmunol.1003711;
RA   Matthews P.C., Adland E., Listgarten J., Leslie A., Mkhwanazi N.,
RA   Carlson J.M., Harndahl M., Stryhn A., Payne R.P., Ogwu A., Huang K.H.,
RA   Frater J., Paioni P., Kloverpris H., Jooste P., Goedhals D., van Vuuren C.,
RA   Steyn D., Riddell L., Chen F., Luzzi G., Balachandran T., Ndung'u T.,
RA   Buus S., Carrington M., Shapiro R., Heckerman D., Goulder P.J.;
RT   "HLA-A*7401-mediated control of HIV viremia is independent of its linkage
RT   disequilibrium with HLA-B*5703.";
RL   J. Immunol. 186:5675-5686(2011).
RN   [65]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [66]
RP   FUNCTION (ALLELE A*24:02).
RX   PubMed=24192765; DOI=10.1038/srep03097;
RA   Shimizu A., Kawana-Tachikawa A., Yamagata A., Han C., Zhu D., Sato Y.,
RA   Nakamura H., Koibuchi T., Carlson J., Martin E., Brumme C.J., Shi Y.,
RA   Gao G.F., Brumme Z.L., Fukai S., Iwamoto A.;
RT   "Structure of TCR and antigen complexes at an immunodominant CTL epitope in
RT   HIV-1 infection.";
RL   Sci. Rep. 3:3097-3097(2013).
RN   [67]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; TYR-344; SER-349;
RP   SER-350; SER-352; SER-356 AND SER-359, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [68]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [69]
RP   FUNCTION (ALLELE A*01:01), AND SUBCELLULAR LOCATION.
RX   PubMed=25880248; DOI=10.1111/tan.12565;
RA   Giam K., Ayala-Perez R., Illing P.T., Schittenhelm R.B., Croft N.P.,
RA   Purcell A.W., Dudek N.L.;
RT   "A comprehensive analysis of peptides presented by HLA-A1.";
RL   Tissue Antigens 85:492-496(2015).
RN   [70]
RP   INTERACTION WITH TAPBPL.
RX   PubMed=26869717; DOI=10.1073/pnas.1519894113;
RA   Morozov G.I., Zhao H., Mage M.G., Boyd L.F., Jiang J., Dolan M.A.,
RA   Venna R., Norcross M.A., McMurtrey C.P., Hildebrand W., Schuck P.,
RA   Natarajan K., Margulies D.H.;
RT   "Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes
RT   peptide editing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:E1006-E1015(2016).
RN   [71]
RP   FUNCTION (ALLELE A*02:01).
RX   PubMed=26929325; DOI=10.1073/pnas.1521812113;
RA   Tripathi S.C., Peters H.L., Taguchi A., Katayama H., Wang H., Momin A.,
RA   Jolly M.K., Celiktas M., Rodriguez-Canales J., Liu H., Behrens C.,
RA   Wistuba I.I., Ben-Jacob E., Levine H., Molldrem J.J., Hanash S.M.,
RA   Ostrin E.J.;
RT   "Immunoproteasome deficiency is a feature of non-small cell lung cancer
RT   with a mesenchymal phenotype and is associated with a poor outcome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:E1555-E1564(2016).
RN   [72]
RP   FUNCTION (ALLELE A*03:01).
RX   PubMed=27049119; DOI=10.1038/srep24032;
RA   Ebstein F., Textoris-Taube K., Keller C., Golnik R., Vigneron N.,
RA   Van den Eynde B.J., Schuler-Thurner B., Schadendorf D., Lorenz F.K.,
RA   Uckert W., Urban S., Lehmann A., Albrecht-Koepke N., Janek K., Henklein P.,
RA   Niewienda A., Kloetzel P.M., Mishto M.;
RT   "Proteasomes generate spliced epitopes by two different mechanisms and as
RT   efficiently as non-spliced epitopes.";
RL   Sci. Rep. 6:24032-24032(2016).
RN   [73]
RP   FUNCTION (ALLELE A*01:01).
RX   PubMed=30530481; DOI=10.4049/jimmunol.1801003;
RA   Keib A., Mei Y.F., Cicin-Sain L., Busch D.H., Dennehy K.M.;
RT   "Measuring Antiviral Capacity of T Cell Responses to Adenovirus.";
RL   J. Immunol. 202:618-624(2019).
RN   [74]
RP   FUNCTION (ALLELES A*01:01; A*03:01 AND A*11:01).
RX   PubMed=32887977; DOI=10.1038/s41590-020-0782-6;
RG   Oxford Immunology Network Covid-19 Response T cell Consortium;
RG   ISARIC4C Investigators;
RA   Peng Y., Mentzer A.J., Liu G., Yao X., Yin Z., Dong D., Dejnirattisai W.,
RA   Rostron T., Supasa P., Liu C., Lopez-Camacho C., Slon-Campos J., Zhao Y.,
RA   Stuart D.I., Paesen G.C., Grimes J.M., Antson A.A., Bayfield O.W.,
RA   Hawkins D.E.D.P., Ker D.S., Wang B., Turtle L., Subramaniam K., Thomson P.,
RA   Zhang P., Dold C., Ratcliff J., Simmonds P., de Silva T., Sopp P.,
RA   Wellington D., Rajapaksa U., Chen Y.L., Salio M., Napolitani G., Paes W.,
RA   Borrow P., Kessler B.M., Fry J.W., Schwabe N.F., Semple M.G., Baillie J.K.,
RA   Moore S.C., Openshaw P.J.M., Ansari M.A., Dunachie S., Barnes E.,
RA   Frater J., Kerr G., Goulder P., Lockett T., Levin R., Zhang Y., Jing R.,
RA   Ho L.P., Cornall R.J., Conlon C.P., Klenerman P., Screaton G.R.,
RA   Mongkolsapaya J., McMichael A., Knight J.C., Ogg G., Dong T.;
RT   "Broad and strong memory CD4+ and CD8+ T cells induced by SARS-CoV-2 in UK
RT   convalescent individuals following COVID-19.";
RL   Nat. Immunol. 21:1336-1345(2020).
RN   [75]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (ALLELE A*68:01), AND
RP   FUNCTION (ALLELE A*68:01).
RX   PubMed=1448153; DOI=10.1038/360364a0;
RA   Guo H.-C., Jardetzky T.S., Garrett T.P.J., Lane W.S., Strominger J.L.,
RA   Wiley D.C.;
RT   "Different length peptides bind to HLA-Aw68 similarly at their ends but
RT   bulge out in the middle.";
RL   Nature 360:364-366(1992).
RN   [76]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (ALLELE A*68:01), AND
RP   FUNCTION (ALLELE A*68:01).
RX   PubMed=1448154; DOI=10.1038/360367a0;
RA   Silver M.L., Guo H.-C., Strominger J.L., Wiley D.C.;
RT   "Atomic structure of a human MHC molecule presenting an influenza virus
RT   peptide.";
RL   Nature 360:367-369(1992).
RN   [77]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), DISULFIDE BOND,
RP   AND DOMAIN.
RX   PubMed=7694806; DOI=10.1016/0092-8674(93)90490-h;
RA   Madden D.R., Garboczi D.N., Wiley D.C.;
RT   "The antigenic identity of peptide-MHC complexes: a comparison of the
RT   conformations of five viral peptides presented by HLA-A2.";
RL   Cell 75:693-708(1993).
RN   [78]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, AND FUNCTION (ALLELE A*02:01).
RX   PubMed=7935798; DOI=10.1038/371626a0;
RA   Collins E.J., Garboczi D.N., Wiley D.C.;
RT   "Three-dimensional structure of a peptide extending from one end of a class
RT   I MHC binding site.";
RL   Nature 371:626-629(1994).
RN   [79]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), AND DOMAIN.
RX   PubMed=8906788; DOI=10.1038/384134a0;
RA   Garboczi D.N., Ghosh P., Utz U., Fan Q.R., Biddison W.E., Wiley D.C.;
RT   "Structure of the complex between human T-cell receptor, viral peptide and
RT   HLA-A2.";
RL   Nature 384:134-141(1996).
RN   [80]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-300 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH CD8A, AND FUNCTION (ALLELE
RP   A*02:01).
RX   PubMed=9177355; DOI=10.1038/42523;
RA   Gao G.F., Tormo J., Gerth U.C., Wyer J.R., McMichael A.J., Stuart D.I.,
RA   Bell J.I., Jones E.Y., Jakobsen B.K.;
RT   "Crystal structure of the complex between human CD8alpha(alpha) and HLA-
RT   A2.";
RL   Nature 387:630-634(1997).
RN   [81]
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, AND FUNCTION (ALLELE A*02:01).
RX   PubMed=11502003; DOI=10.1006/jmbi.2001.4816;
RA   Hillig R.C., Coulie P.G., Stroobant V., Saenger W., Ziegler A.,
RA   Hulsmeyer M.;
RT   "High-resolution structure of HLA-A*0201 in complex with a tumour-specific
RT   antigenic peptide encoded by the MAGE-A4 gene.";
RL   J. Mol. Biol. 310:1167-1176(2001).
RN   [82]
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 25-300 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH TCR, AND FUNCTION (ALLELE
RP   A*02:01).
RX   PubMed=12796775; DOI=10.1038/ni942;
RA   Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I., Jones E.Y.;
RT   "A structural basis for immunodominant human T cell receptor recognition.";
RL   Nat. Immunol. 4:657-663(2003).
RN   [83]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 25-299 (ALLELE A*11:01) IN
RP   COMPLEX WITH SARS NUCLEOCAPSID PEPTIDE, AND DISULFIDE BONDS.
RX   PubMed=16041067; DOI=10.1107/s0907444905013090;
RA   Blicher T., Kastrup J.S., Buus S., Gajhede M.;
RT   "High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid
RT   peptide.";
RL   Acta Crystallogr. D 61:1031-1040(2005).
RN   [84]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-300 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH TCR, AND FUNCTION (ALLELE
RP   A*02:01).
RX   PubMed=18275829; DOI=10.1016/j.immuni.2007.12.018;
RA   Ishizuka J., Stewart-Jones G.B., van der Merwe A., Bell J.I.,
RA   McMichael A.J., Jones E.Y.;
RT   "The structural dynamics and energetics of an immunodominant T cell
RT   receptor are programmed by its Vbeta domain.";
RL   Immunity 28:171-182(2008).
RN   [85]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-298 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), AND DOMAIN.
RX   PubMed=19542454; DOI=10.4049/jimmunol.0900556;
RA   Gras S., Saulquin X., Reiser J.B., Debeaupuis E., Echasserieau K.,
RA   Kissenpfennig A., Legoux F., Chouquet A., Le Gorrec M., Machillot P.,
RA   Neveu B., Thielens N., Malissen B., Bonneville M., Housset D.;
RT   "Structural bases for the affinity-driven selection of a public TCR against
RT   a dominant human cytomegalovirus epitope.";
RL   J. Immunol. 183:430-437(2009).
RN   [86]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-298 (ALLELE A*01:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*01:01), DOMAIN, AND
RP   DISULFIDE BOND.
RX   PubMed=19177349; DOI=10.1002/pro.4;
RA   Kumar P., Vahedi-Faridi A., Saenger W., Ziegler A., Uchanska-Ziegler B.;
RT   "Conformational changes within the HLA-A1:MAGE-A1 complex induced by
RT   binding of a recombinant antibody fragment with TCR-like specificity.";
RL   Protein Sci. 18:37-49(2009).
RN   [87]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-298 (ALLELE A*24:02) IN COMPLEX
RP   WITH B2M AND WITH SARS NUCLEOCAPSID PEPTIDE, DISULFIDE BONDS, FUNCTION
RP   (ALLELE A*24:02), AND DOMAIN.
RX   PubMed=20844028; DOI=10.1128/jvi.01464-10;
RA   Liu J., Wu P., Gao F., Qi J., Kawana-Tachikawa A., Xie J., Vavricka C.J.,
RA   Iwamoto A., Li T., Gao G.F.;
RT   "Novel immunodominant peptide presentation strategy: a featured HLA-A*2402-
RT   restricted cytotoxic T-lymphocyte epitope stabilized by intrachain hydrogen
RT   bonds from severe acute respiratory syndrome coronavirus nucleocapsid
RT   protein.";
RL   J. Virol. 84:11849-11857(2010).
RN   [88]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), AND DOMAIN.
RX   PubMed=20619457; DOI=10.1016/j.molimm.2010.06.005;
RA   Borbulevych O.Y., Do P., Baker B.M.;
RT   "Structures of native and affinity-enhanced WT1 epitopes bound to HLA-
RT   A*0201: implications for WT1-based cancer therapeutics.";
RL   Mol. Immunol. 47:2519-2524(2010).
RN   [89]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-298 (ALLELE A*03:01) IN COMPLEX
RP   WITH B2M AND PLP1 ANTIGENIC PEPTIDE, DISULFIDE BONDS, AND DOMAIN.
RX   PubMed=21543847; DOI=10.1107/s0907444911007888;
RA   McMahon R.M., Friis L., Siebold C., Friese M.A., Fugger L., Jones E.Y.;
RT   "Structure of HLA-A*0301 in complex with a peptide of proteolipid protein:
RT   insights into the role of HLA-A alleles in susceptibility to multiple
RT   sclerosis.";
RL   Acta Crystallogr. D 67:447-454(2011).
RN   [90]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-298 (ALLELE A*03:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, DISULFIDE BOND, DOMAIN, AND FUNCTION (ALLELE
RP   A*03:01).
RX   PubMed=21943705; DOI=10.1016/j.molimm.2011.08.015;
RA   Zhang S., Liu J., Cheng H., Tan S., Qi J., Yan J., Gao G.F.;
RT   "Structural basis of cross-allele presentation by HLA-A*0301 and HLA-A*1101
RT   revealed by two HIV-derived peptide complexes.";
RL   Mol. Immunol. 49:395-401(2011).
RN   [91]
RP   X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 25-300 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH TCR, FUNCTION (ALLELE
RP   A*02:01), DOMAIN, INDUCTION BY CYTOKINES, AND INVOLVEMENT IN IDDM (ALLELE
RP   A*02:01).
RX   PubMed=22245737; DOI=10.1038/ni.2206;
RA   Bulek A.M., Cole D.K., Skowera A., Dolton G., Gras S., Madura F.,
RA   Fuller A., Miles J.J., Gostick E., Price D.A., Drijfhout J.W., Knight R.R.,
RA   Huang G.C., Lissin N., Molloy P.E., Wooldridge L., Jakobsen B.K.,
RA   Rossjohn J., Peakman M., Rizkallah P.J., Sewell A.K.;
RT   "Structural basis for the killing of human beta cells by CD8(+) T cells in
RT   type 1 diabetes.";
RL   Nat. Immunol. 13:283-289(2012).
RN   [92]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-308 (ALLELE A*01:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*01:01), AND DOMAIN.
RX   PubMed=24395804; DOI=10.1073/pnas.1322229111;
RA   Quinones-Parra S., Grant E., Loh L., Nguyen T.H., Campbell K.A., Tong S.Y.,
RA   Miller A., Doherty P.C., Vijaykrishna D., Rossjohn J., Gras S.,
RA   Kedzierska K.;
RT   "Preexisting CD8+ T-cell immunity to the H7N9 influenza A virus varies
RT   across ethnicities.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:1049-1054(2014).
RN   [93]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 25-298 (ALLELE A*01:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*01:01), DOMAIN, AND
RP   DISULFIDE BOND.
RX   PubMed=26758806; DOI=10.1038/srep18851;
RA   Raman M.C., Rizkallah P.J., Simmons R., Donnellan Z., Dukes J., Bossi G.,
RA   Le Provost G.S., Todorov P., Baston E., Hickman E., Mahon T., Hassan N.,
RA   Vuidepot A., Sami M., Cole D.K., Jakobsen B.K.;
RT   "Direct molecular mimicry enables off-target cardiovascular toxicity by an
RT   enhanced affinity TCR designed for cancer immunotherapy.";
RL   Sci. Rep. 6:18851-18851(2016).
RN   [94]
RP   X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN
RP   COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), DOMAIN, AND
RP   DISULFIDE BOND.
RX   PubMed=28250417; DOI=10.1038/nsmb.3383;
RA   Song I., Gil A., Mishra R., Ghersi D., Selin L.K., Stern L.J.;
RT   "Broad TCR repertoire and diverse structural solutions for recognition of
RT   an immunodominant CD8+ T cell epitope.";
RL   Nat. Struct. Mol. Biol. 24:395-406(2017).
RN   [95]
RP   ASSOCIATION OF ALLELE A*29:02 WITH BIRDSHOT CHORIORETINOPATHY.
RX   PubMed=1728143; DOI=10.1016/s0002-9394(14)75749-6;
RA   LeHoang P., Ozdemir N., Benhamou A., Tabary T., Edelson C., Betuel H.,
RA   Semiglia R., Cohen J.H.;
RT   "HLA-A29.2 subtype associated with birdshot retinochoroidopathy.";
RL   Am. J. Ophthalmol. 113:33-35(1992).
RN   [96]
RP   ASSOCIATION OF ALLELE A*03:01 WITH MULTIPLE SCLEROSIS.
RX   PubMed=10746785; DOI=10.1034/j.1399-0039.2000.550205.x;
RA   Fogdell-Hahn A., Ligers A., Groenning M., Hillert J., Olerup O.;
RT   "Multiple sclerosis: a modifying influence of HLA class I genes in an HLA
RT   class II associated autoimmune disease.";
RL   Tissue Antigens 55:140-148(2000).
RN   [97]
RP   ASSOCIATION OF ALLELE A*24:02 WITH IDDM.
RX   PubMed=16731854; DOI=10.2337/db05-1049;
RA   Nakanishi K., Inoko H.;
RT   "Combination of HLA-A24, -DQA1*03, and -DR9 contributes to acute-onset and
RT   early complete beta-cell destruction in type 1 diabetes: longitudinal study
RT   of residual beta-cell function.";
RL   Diabetes 55:1862-1868(2006).
RN   [98]
RP   ASSOCIATION OF ALLELE A*02:01 WITH IDDM.
RX   PubMed=18802479; DOI=10.1172/jci35449;
RA   Skowera A., Ellis R.J., Varela-Calvino R., Arif S., Huang G.C.,
RA   Van-Krinks C., Zaremba A., Rackham C., Allen J.S., Tree T.I., Zhao M.,
RA   Dayan C.M., Sewell A.K., Unger W.W., Unger W., Drijfhout J.W.,
RA   Ossendorp F., Roep B.O., Peakman M.;
RT   "CTLs are targeted to kill beta cells in patients with type 1 diabetes
RT   through recognition of a glucose-regulated preproinsulin epitope.";
RL   J. Clin. Invest. 118:3390-3402(2008).
RN   [99]
RP   ASSOCIATION OF ALLELE A*03:01 WITH MULTIPLE SCLEROSIS.
RX   PubMed=18953350; DOI=10.1038/nm.1881;
RA   Friese M.A., Jakobsen K.B., Friis L., Etzensperger R., Craner M.J.,
RA   McMahon R.M., Jensen L.T., Huygelen V., Jones E.Y., Bell J.I., Fugger L.;
RT   "Opposing effects of HLA class I molecules in tuning autoreactive CD8+ T
RT   cells in multiple sclerosis.";
RL   Nat. Med. 14:1227-1235(2008).
RN   [100]
RP   ASSOCIATION OF ALLELE A*24:02 WITH IDDM.
RX   PubMed=22522618; DOI=10.2337/db11-1520;
RA   Kronenberg D., Knight R.R., Estorninho M., Ellis R.J., Kester M.G.,
RA   de Ru A., Eichmann M., Huang G.C., Powrie J., Dayan C.M., Skowera A.,
RA   van Veelen P.A., Peakman M.;
RT   "Circulating preproinsulin signal peptide-specific CD8 T cells restricted
RT   by the susceptibility molecule HLA-A24 are expanded at onset of type 1
RT   diabetes and kill beta-cells.";
RL   Diabetes 61:1752-1759(2012).
RN   [101]
RP   ASSOCIATION OF ALLELE A*31:01 WITH CARBAMAZEPINE-INDUCED HYPERSENSITIVITY
RP   REACTIONS.
RX   PubMed=21428769; DOI=10.1056/nejmoa1013297;
RA   McCormack M., Alfirevic A., Bourgeois S., Farrell J.J., Kasperaviciute D.,
RA   Carrington M., Sills G.J., Marson T., Jia X., de Bakker P.I.,
RA   Chinthapalli K., Molokhia M., Johnson M.R., O'Connor G.D., Chaila E.,
RA   Alhusaini S., Shianna K.V., Radtke R.A., Heinzen E.L., Walley N.,
RA   Pandolfo M., Pichler W., Park B.K., Depondt C., Sisodiya S.M.,
RA   Goldstein D.B., Deloukas P., Delanty N., Cavalleri G.L., Pirmohamed M.;
RT   "HLA-A*3101 and carbamazepine-induced hypersensitivity reactions in
RT   Europeans.";
RL   N. Engl. J. Med. 364:1134-1143(2011).
RN   [102]
RP   ASSOCIATION OF ALLELE A*26:01 WITH BEHCET DISEASE.
RX   PubMed=30872678; DOI=10.1038/s41598-019-40824-y;
RA   Nakamura J., Meguro A., Ishii G., Mihara T., Takeuchi M., Mizuki Y.,
RA   Yuda K., Yamane T., Kawagoe T., Ota M., Mizuki N.;
RT   "The association analysis between HLA-A*26 and Behcet's disease.";
RL   Sci. Rep. 9:4426-4426(2019).
RN   [103]
RP   POLYMORPHISM.
RX   PubMed=28650991; DOI=10.1371/journal.pgen.1006862;
RA   Robinson J., Guethlein L.A., Cereb N., Yang S.Y., Norman P.J.,
RA   Marsh S.G.E., Parham P.;
RT   "Distinguishing functional polymorphism from random variation in the
RT   sequences of >10,000 HLA-A, -B and -C alleles.";
RL   PLoS Genet. 13:E1006862-E1006862(2017).
CC   -!- FUNCTION: Antigen-presenting major histocompatibility complex class I
CC       (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays
CC       primarily viral and tumor-derived peptides on antigen-presenting cells
CC       for recognition by alpha-beta T cell receptor (TCR) on HLA-A-restricted
CC       CD8-positive T cells, guiding antigen-specific T cell immune response
CC       to eliminate infected or transformed cells (PubMed:2456340,
CC       PubMed:2784196, PubMed:1402688, PubMed:7504010, PubMed:9862734,
CC       PubMed:10449296, PubMed:12138174, PubMed:12393434, PubMed:15893615,
CC       PubMed:17189421, PubMed:19543285, PubMed:21498667, PubMed:24192765,
CC       PubMed:7694806, PubMed:24395804, PubMed:28250417). May also present
CC       self-peptides derived from the signal sequence of secreted or membrane
CC       proteins, although T cells specific for these peptides are usually
CC       inactivated to prevent autoreactivity (PubMed:25880248, PubMed:7506728,
CC       PubMed:7679507). Both the peptide and the MHC molecule are recognized
CC       by TCR, the peptide is responsible for the fine specificity of antigen
CC       recognition and MHC residues account for the MHC restriction of T cells
CC       (PubMed:12796775, PubMed:18275829, PubMed:19542454, PubMed:28250417).
CC       Typically presents intracellular peptide antigens of 8 to 13 amino
CC       acids that arise from cytosolic proteolysis via IFNG-induced
CC       immunoproteasome or via endopeptidase IDE/insulin-degrading enzyme
CC       (PubMed:17189421, PubMed:20364150, PubMed:17079320, PubMed:26929325,
CC       PubMed:27049119). Can bind different peptides containing allele-
CC       specific binding motifs, which are mainly defined by anchor residues at
CC       position 2 and 9 (PubMed:7504010, PubMed:9862734).
CC       {ECO:0000269|PubMed:10449296, ECO:0000269|PubMed:12138174,
CC       ECO:0000269|PubMed:12393434, ECO:0000269|PubMed:12796775,
CC       ECO:0000269|PubMed:1402688, ECO:0000269|PubMed:15893615,
CC       ECO:0000269|PubMed:17079320, ECO:0000269|PubMed:17189421,
CC       ECO:0000269|PubMed:18275829, ECO:0000269|PubMed:19542454,
CC       ECO:0000269|PubMed:19543285, ECO:0000269|PubMed:20364150,
CC       ECO:0000269|PubMed:21498667, ECO:0000269|PubMed:24192765,
CC       ECO:0000269|PubMed:24395804, ECO:0000269|PubMed:2456340,
CC       ECO:0000269|PubMed:25880248, ECO:0000269|PubMed:26929325,
CC       ECO:0000269|PubMed:27049119, ECO:0000269|PubMed:2784196,
CC       ECO:0000269|PubMed:28250417, ECO:0000269|PubMed:7504010,
CC       ECO:0000269|PubMed:7506728, ECO:0000269|PubMed:7679507,
CC       ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:9862734}.
CC   -!- FUNCTION: Allele A*01:01: Presents a restricted peptide repertoire
CC       including viral epitopes derived from IAV NP/nucleoprotein (CTELKLSDY),
CC       IAV PB1/polymerase basic protein 1 (VSDGGPNLY), HAdV-11 capsid L3/hexon
CC       protein (LTDLGQNLLY), SARS-CoV-2 3a/ORF3a (FTSDYYQLY) as well as tumor
CC       peptide antigens including MAGE1 (EADPTGHSY), MAGEA3 (EVDPIGHLY) and
CC       WT1 (TSEKRPFMCAY), all having in common a canonical motif with a
CC       negatively charged Asp or Glu residue at position 3 and a Tyr anchor
CC       residue at the C-terminus (PubMed:1402688, PubMed:7504010,
CC       PubMed:17189421, PubMed:20364150, PubMed:25880248, PubMed:30530481,
CC       PubMed:19177349, PubMed:24395804, PubMed:26758806, PubMed:32887977). A
CC       number of HLA-A*01:01-restricted peptides carry a post-translational
CC       modification with oxidation and N-terminal acetylation being the most
CC       frequent (PubMed:25880248). Fails to present highly immunogenic
CC       peptides from the EBV latent antigens (PubMed:18779413).
CC       {ECO:0000269|PubMed:1402688, ECO:0000269|PubMed:17189421,
CC       ECO:0000269|PubMed:18779413, ECO:0000269|PubMed:19177349,
CC       ECO:0000269|PubMed:20364150, ECO:0000269|PubMed:24395804,
CC       ECO:0000269|PubMed:25880248, ECO:0000269|PubMed:26758806,
CC       ECO:0000269|PubMed:30530481, ECO:0000269|PubMed:7504010}.
CC   -!- FUNCTION: Allele A*02:01: A major allele in human populations, presents
CC       immunodominant viral epitopes derived from IAV M/matrix protein 1
CC       (GILGFVFTL), HIV-1 env (TLTSCNTSV), HIV-1 gag-pol (ILKEPVHGV), HTLV-1
CC       Tax (LLFGYPVYV), HBV C/core antigen (FLPSDFFPS), HCMV UL83/pp65
CC       (NLVPMVATV) as well as tumor peptide antigens including MAGEA4
CC       (GVYDGREHTV), WT1 (RMFPNAPYL) and CTAG1A/NY-ESO-1 (SLLMWITQC), all
CC       having in common hydrophobic amino acids at position 2 and at the C-
CC       terminal anchors. {ECO:0000269|PubMed:11502003,
CC       ECO:0000269|PubMed:12138174, ECO:0000269|PubMed:12796775,
CC       ECO:0000269|PubMed:17079320, ECO:0000269|PubMed:18275829,
CC       ECO:0000269|PubMed:19542454, ECO:0000269|PubMed:20619457,
CC       ECO:0000269|PubMed:22245737, ECO:0000269|PubMed:26929325,
CC       ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417,
CC       ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:7935798,
CC       ECO:0000269|PubMed:8630735, ECO:0000269|PubMed:8805302,
CC       ECO:0000269|PubMed:8906788, ECO:0000269|PubMed:9177355}.
CC   -!- FUNCTION: Allele A*03:01: Presents viral epitopes derived from IAV NP
CC       (ILRGSVAHK), HIV-1 nef (QVPLRPMTYK), HIV-1 gag-pol (AIFQSSMTK), SARS-
CC       CoV-2 N/nucleoprotein (KTFPPTEPK) as well as tumor peptide antigens
CC       including PMEL (LIYRRRLMK), NODAL (HAYIQSLLK), TRP-2 (RMYNMVPFF), all
CC       having in common hydrophobic amino acids at position 2 and Lys or Arg
CC       anchor residues at the C-terminus (PubMed:7504010, PubMed:7679507,
CC       PubMed:9862734, PubMed:19543285, PubMed:21943705, PubMed:2456340,
CC       PubMed:32887977). May also display spliced peptides resulting from the
CC       ligation of two separate proteasomal cleavage products that are not
CC       contiguous in the parental protein (PubMed:27049119).
CC       {ECO:0000269|PubMed:19543285, ECO:0000269|PubMed:21943705,
CC       ECO:0000269|PubMed:2456340, ECO:0000269|PubMed:27049119,
CC       ECO:0000269|PubMed:7504010, ECO:0000269|PubMed:7679507,
CC       ECO:0000269|PubMed:9862734}.
CC   -!- FUNCTION: Allele A*11:01: Presents several immunodominant epitopes
CC       derived from HIV-1 gag-pol and HHV-4 EBNA4, containing the peptide
CC       motif with Val, Ile, Thr, Leu, Tyr or Phe at position 2 and Lys anchor
CC       residue at the C-terminus. Important in the control of HIV-1, EBV and
CC       HBV infections (PubMed:10449296). Presents an immunodominant epitope
CC       derived from SARS-CoV-2 N/nucleoprotein (KTFPPTEPK) (PubMed:32887977).
CC       {ECO:0000269|PubMed:10449296, ECO:0000269|PubMed:32887977}.
CC   -!- FUNCTION: Allele A*23:01: Interacts with natural killer (NK) cell
CC       receptor KIR3DL1 and may contribute to functional maturation of NK
CC       cells and self-nonself discrimination during innate immune response.
CC       {ECO:0000269|PubMed:17182537}.
CC   -!- FUNCTION: Allele A*24:02: Presents viral epitopes derived from HIV-1
CC       nef (RYPLTFGWCF), EBV lytic- and latent-cycle antigens BRLF1
CC       (TYPVLEEMF), BMLF1 (DYNFVKQLF) and LMP2 (IYVLVMLVL), SARS-CoV
CC       nucleocapsid/N (QFKDNVILL), as well as tumor peptide antigens including
CC       PRAME (LYVDSLFFL), all sharing a common signature motif, namely an
CC       aromatic residue Tyr or Phe at position 2 and a nonhydrophobic anchor
CC       residue Phe, Leu or Iso at the C-terminus (PubMed:9047241,
CC       PubMed:12393434, PubMed:24192765, PubMed:20844028). Interacts with
CC       natural killer (NK) cell receptor KIR3DL1 and may contribute to
CC       functional maturation of NK cells and self-nonself discrimination
CC       during innate immune response (PubMed:17182537, PubMed:18502829).
CC       {ECO:0000269|PubMed:12393434, ECO:0000269|PubMed:17182537,
CC       ECO:0000269|PubMed:18502829, ECO:0000269|PubMed:20844028,
CC       ECO:0000269|PubMed:24192765, ECO:0000269|PubMed:9047241}.
CC   -!- FUNCTION: Allele A*26:01: Presents several epitopes derived from HIV-1
CC       gag-pol (EVIPMFSAL, ETKLGKAGY) and env (LVSDGGPNLY), carrying as anchor
CC       residues preferentially Glu at position 1, Val or Thr at position 2 and
CC       Tyr at the C-terminus. {ECO:0000269|PubMed:15893615}.
CC   -!- FUNCTION: Allele A*29:02: Presents peptides having a common motif,
CC       namely a Glu residue at position 2 and Tyr or Leu anchor residues at
CC       the C-terminus. {ECO:0000269|PubMed:8622959}.
CC   -!- FUNCTION: Allele A*32:01: Interacts with natural killer (NK) cell
CC       receptor KIR3DL1 and may contribute to functional maturation of NK
CC       cells and self-nonself discrimination during innate immune response.
CC       {ECO:0000269|PubMed:17182537}.
CC   -!- FUNCTION: Allele A*68:01: Presents viral epitopes derived from IAV NP
CC       (KTGGPIYKR) and HIV-1 tat (ITKGLGISYGR), having a common signature
CC       motif namely, Val or Thr at position 2 and positively charged residues
CC       Arg or Lys at the C-terminal anchor. {ECO:0000269|PubMed:1448153,
CC       ECO:0000269|PubMed:1448154, ECO:0000269|PubMed:2784196}.
CC   -!- FUNCTION: Allele A*74:01: Presents immunodominant HIV-1 epitopes
CC       derived from gag-pol (GQMVHQAISPR, QIYPGIKVR) and rev (RQIHSISER),
CC       carrying an aliphatic residue at position 2 and Arg anchor residue at
CC       the C-terminus. May contribute to viral load control in chronic HIV-1
CC       infection. {ECO:0000269|PubMed:21498667}.
CC   -!- SUBUNIT: Heterotrimer that consists of an alpha chain HLA-A, a beta
CC       chain B2M and a peptide (peptide-HLA-A-B2M) (PubMed:7504010,
CC       PubMed:7679507, PubMed:21943705, PubMed:19177349, PubMed:24395804,
CC       PubMed:26758806, PubMed:7504010, PubMed:7506728, PubMed:8805302,
CC       PubMed:7694806, PubMed:7935798, PubMed:9177355, PubMed:18275829,
CC       PubMed:22245737, PubMed:28250417, PubMed:11502003, PubMed:8906788,
CC       PubMed:19542454). Early in biogenesis, HLA-A-B2M dimer interacts with
CC       the components of the peptide-loading complex composed of TAPBP, TAP1-
CC       TAP2, TAPBPL, PDIA3/ERP57 and CALR (PubMed:21263072). Interacts with
CC       TAP1-TAP2 transporter via TAPBP; this interaction is obligatory for the
CC       loading of peptide epitopes delivered to the ER by TAP1-TAP2
CC       transporter (PubMed:8805302, PubMed:8630735, PubMed:21263072).
CC       Interacts with TAPBPL; TAPBPL binds peptide-free HLA-A-B2M complexes or
CC       those loaded with low affinity peptides, likely facilitating peptide
CC       exchange for higher affinity peptides (PubMed:26869717). Only optimally
CC       assembled peptide-HLA-B2M trimer translocates to the surface of
CC       antigen-presenting cells, where it interacts with TCR and CD8
CC       coreceptor on the surface of T cells. HLA-A (via polymorphic alpha-1
CC       and alpha-2 domains) interacts with antigen-specific TCR (via CDR3
CC       domains) (PubMed:22245737, PubMed:12796775, PubMed:18275829). One HLA-A
CC       molecule (mainly via nonpolymorphic alpha-3 domain) interacts with one
CC       CD8A homodimer (via CDR-like loop); this interaction insures peptide-
CC       HLA-A-B2M recognition by CD8-positive T cells only (PubMed:9177355,
CC       PubMed:2784196). Alleles A*23:01; A*24:02 and A*32:01 interact (via Bw4
CC       motif) with KIR3DL1 on NK cells; this interaction is direct.
CC       {ECO:0000269|PubMed:11502003, ECO:0000269|PubMed:12796775,
CC       ECO:0000269|PubMed:17182537, ECO:0000269|PubMed:18275829,
CC       ECO:0000269|PubMed:18502829, ECO:0000269|PubMed:19177349,
CC       ECO:0000269|PubMed:21263072, ECO:0000269|PubMed:21943705,
CC       ECO:0000269|PubMed:22245737, ECO:0000269|PubMed:24395804,
CC       ECO:0000269|PubMed:26758806, ECO:0000269|PubMed:26869717,
CC       ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417,
CC       ECO:0000269|PubMed:7504010, ECO:0000269|PubMed:7506728,
CC       ECO:0000269|PubMed:7679507, ECO:0000269|PubMed:7694806,
CC       ECO:0000269|PubMed:7935798, ECO:0000269|PubMed:8630735,
CC       ECO:0000269|PubMed:8805302, ECO:0000269|PubMed:9177355}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HHV-8 MIR1 protein.
CC       {ECO:0000269|PubMed:12006494}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory protein
CC       p12I. {ECO:0000269|PubMed:11390610}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21263072,
CC       ECO:0000269|PubMed:25880248, ECO:0000269|PubMed:8805302}; Single-pass
CC       type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:8805302}; Single-pass type I membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P04439-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P04439-2; Sequence=VSP_060391, VSP_060392;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000305}.
CC   -!- INDUCTION: Up-regulated by IFNG, and pro-inflammatory cytokines IL1B
CC       and TNF. {ECO:0000269|PubMed:21263072, ECO:0000269|PubMed:22245737}.
CC   -!- DOMAIN: The alpha-1 domain is a structural part of the peptide-binding
CC       cleft. {ECO:0000269|PubMed:19177349, ECO:0000269|PubMed:19542454,
CC       ECO:0000269|PubMed:20619457, ECO:0000269|PubMed:20844028,
CC       ECO:0000269|PubMed:21943705, ECO:0000269|PubMed:22245737,
CC       ECO:0000269|PubMed:24395804, ECO:0000269|PubMed:26758806,
CC       ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:7694806,
CC       ECO:0000269|PubMed:8906788}.
CC   -!- DOMAIN: The alpha-2 domain is a structural part of the peptide-binding
CC       cleft (PubMed:21543847, PubMed:21943705, PubMed:19177349,
CC       PubMed:26758806, PubMed:24395804, PubMed:7694806, PubMed:8906788,
CC       PubMed:2784196, PubMed:28250417, PubMed:22245737, PubMed:19542454,
CC       PubMed:20619457, PubMed:20844028). Mediates the interaction with TAP1-
CC       TAP2 complex (PubMed:8805302). {ECO:0000269|PubMed:19177349,
CC       ECO:0000269|PubMed:19542454, ECO:0000269|PubMed:20619457,
CC       ECO:0000269|PubMed:20844028, ECO:0000269|PubMed:21543847,
CC       ECO:0000269|PubMed:21943705, ECO:0000269|PubMed:22245737,
CC       ECO:0000269|PubMed:24395804, ECO:0000269|PubMed:26758806,
CC       ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417,
CC       ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:8805302,
CC       ECO:0000269|PubMed:8906788}.
CC   -!- DOMAIN: The alpha-3 Ig-like domain mediates the interaction with CD8
CC       coreceptor. {ECO:0000269|PubMed:2784196}.
CC   -!- PTM: (Microbial infection) Polyubiquitinated in a post ER compartment
CC       by interaction with human herpesvirus 8 MIR1 protein. This targets the
CC       protein for rapid degradation via the ubiquitin system.
CC       {ECO:0000269|PubMed:12006494}.
CC   -!- PTM: N-linked glycosylation at Asn-110. {ECO:0000269|PubMed:19159218,
CC       ECO:0000269|PubMed:21263072}.
CC   -!- POLYMORPHISM: Highly polymorphic. Polymorphic residues encode for
CC       alpha-1 and alpha-2 domains of the peptide-binding cleft, where they
CC       contribute to variations in peptide binding and TCR recognition among
CC       different alleles. The human population is estimated to have millions
CC       of HLA-A alleles. But only 11 common HLA-A alleles are considered core
CC       alleles, representing all functionally significant variation
CC       (polymorphism) in alpha-1 and alpha-2 domains. These are: A*01:01;
CC       A*02:01; A*02:05; A*03:01; A*11:01; A*24:02; A*26:01; A*29:02; A*30:01;
CC       A*74:01 and A*80:01. Among these, A*02:01; A*11:01; A*24:02 and
CC       A*26:01, were likely passed by introgression from archaic to modern
CC       humans. Functional alleles of more recent origin (non-core) were
CC       derived by recombination (PubMed:28650991). The sequence shown is that
CC       of A*03:01. The sequences of core alleles and common representative
CC       alleles of serologically distinct allele groups are described as
CC       variants of A*03:01 (PubMed:28650991). Allele A*31:01 is associated
CC       with carbamazepine-induced hypersensitivity reactions among subjects of
CC       Northern European ancestry [MIM:608579] (PubMed:21428769).
CC       {ECO:0000269|PubMed:21428769, ECO:0000269|PubMed:28650991}.
CC   -!- DISEASE: Note=Alleles A*02:01 and A*24:02 are associated with increased
CC       susceptibility to diabetes mellitus, insulin-dependent (IDDM)
CC       (PubMed:22245737, PubMed:18802479, PubMed:16731854, PubMed:22522618).
CC       In a glucose-dependent way, allele A*02:01 may aberrantly present the
CC       signal peptide of preproinsulin (ALWGPDPAAA) on the surface of
CC       pancreatic beta cells to autoreactive CD8-positive T cells, potentially
CC       driving T-cell mediated cytotoxicity in pancreatic islets
CC       (PubMed:22245737, PubMed:18802479). Allele A*24:02 may present the
CC       signal peptide of preproinsulin (LWMRLLPLL) and contribute to acute
CC       pancreatic beta-cell destruction and early onset of IDDM
CC       (PubMed:16731854, PubMed:22522618). {ECO:0000269|PubMed:16731854,
CC       ECO:0000269|PubMed:18802479, ECO:0000269|PubMed:22245737,
CC       ECO:0000269|PubMed:22522618}.
CC   -!- DISEASE: Note=Allele A*03:01 is associated with increased
CC       susceptibility to multiple sclerosis (MS), an autoimmune disease of the
CC       central nervous system (PubMed:10746785). May contribute to the
CC       initiation phase of the disease by presenting myelin PLP1 self-peptide
CC       (KLIETYFSK) to autoreactive CD8-positive T cells capable of initiating
CC       the first autoimmune attacks (PubMed:18953350).
CC       {ECO:0000269|PubMed:10746785, ECO:0000269|PubMed:18953350}.
CC   -!- DISEASE: Note=Allele A*26:01 is associated with increased
CC       susceptibility to Behcet disease (BD) in the Northeast Asian
CC       population. Especially in the HLA-B*51-negative BD populations, HLA-
CC       A*26 is significantly associated with the onset of BD.
CC       {ECO:0000269|PubMed:30872678}.
CC   -!- DISEASE: Note=Allele A*29:02 is associated with increased
CC       susceptibility to birdshot chorioretinopathy (BSCR). May aberrantly
CC       present retinal autoantigens and induce autoimmune uveitis.
CC       {ECO:0000269|PubMed:1728143}.
CC   -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA25162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305|PubMed:6609814};
CC   ---------------------------------------------------------------------------
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DR   EMBL; U03862; AAA03603.1; -; mRNA.
DR   EMBL; X13111; CAA31503.1; -; mRNA.
DR   EMBL; M23739; AAB47873.1; -; mRNA.
DR   EMBL; U83415; AAB53373.1; -; mRNA.
DR   EMBL; U83416; AAB53374.1; -; mRNA.
DR   EMBL; M30576; AAA59612.1; -; Genomic_DNA.
DR   EMBL; M30580; AAB47870.1; -; Genomic_DNA.
DR   EMBL; M24043; AAA59652.1; -; Genomic_DNA.
DR   EMBL; M84379; AAA59606.1; -; mRNA.
DR   EMBL; M32321; AAA36234.1; -; mRNA.
DR   EMBL; X60108; CAA42702.1; -; mRNA.
DR   EMBL; M64740; AAA59600.1; -; mRNA.
DR   EMBL; M64742; AAA03662.1; -; mRNA.
DR   EMBL; X61700; CAA43869.1; -; mRNA.
DR   EMBL; X61701; CAA43870.1; -; mRNA.
DR   EMBL; X61703; CAA43872.1; -; mRNA.
DR   EMBL; X61704; CAA43873.1; -; mRNA.
DR   EMBL; X61711; CAA43880.1; -; mRNA.
DR   EMBL; M84375; AAA59599.1; -; mRNA.
DR   EMBL; U03697; AAA03720.1; -; mRNA.
DR   EMBL; L18898; AAA17012.1; -; mRNA.
DR   EMBL; D14350; BAA03279.1; -; mRNA.
DR   EMBL; U03754; AAC04322.1; -; mRNA.
DR   EMBL; D16841; BAA04117.1; -; mRNA.
DR   EMBL; U07234; AAA70162.1; -; mRNA.
DR   EMBL; AY786587; AAV53345.1; -; mRNA.
DR   EMBL; X00492; CAA25162.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X03070; CAB56605.1; -; Genomic_DNA.
DR   EMBL; X03071; CAB56606.1; -; Genomic_DNA.
DR   EMBL; X03158; CAB56607.1; -; Genomic_DNA.
DR   EMBL; X03159; CAB56608.1; -; Genomic_DNA.
DR   EMBL; K02883; AAA98727.1; -; Genomic_DNA.
DR   EMBL; AH003070; AAA65449.1; -; Genomic_DNA.
DR   EMBL; X55710; CAA39243.1; -; Genomic_DNA.
DR   EMBL; U02935; AAA76608.2; -; Genomic_DNA.
DR   EMBL; L78918; AAB05976.1; -; Genomic_DNA.
DR   EMBL; Z72422; CAA96532.1; -; Genomic_DNA.
DR   EMBL; Z93949; CAB07989.1; -; Genomic_DNA.
DR   EMBL; EU445484; ACA35004.1; -; Genomic_DNA.
DR   EMBL; U03907; AAA03605.1; -; mRNA.
DR   EMBL; U17569; AAA56779.1; -; mRNA.
DR   EMBL; U17570; AAA56780.1; -; mRNA.
DR   EMBL; U32184; AAB63980.1; -; mRNA.
DR   EMBL; AJ748743; CAG38621.1; -; Genomic_DNA.
DR   EMBL; BC003069; AAH03069.1; -; mRNA.
DR   EMBL; BC008611; AAH08611.1; -; mRNA.
DR   EMBL; AL671277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS34373.1; -. [P04439-1]
DR   RefSeq; NP_001229687.1; NM_001242758.1.
DR   RefSeq; NP_002107.3; NM_002116.7. [P04439-1]
DR   PDB; 1AKJ; X-ray; 2.65 A; A=25-300.
DR   PDB; 1AO7; X-ray; 2.60 A; A=25-299.
DR   PDB; 1AQD; X-ray; 2.45 A; C/F/I/L=127-141.
DR   PDB; 1B0G; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 1B0R; X-ray; 2.90 A; A=25-299.
DR   PDB; 1BD2; X-ray; 2.50 A; A=25-299.
DR   PDB; 1DUY; X-ray; 2.15 A; A/D=25-299.
DR   PDB; 1DUZ; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 1EEY; X-ray; 2.25 A; A/D=25-299.
DR   PDB; 1EEZ; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 1HHG; X-ray; 2.60 A; A/D=25-299.
DR   PDB; 1HHH; X-ray; 3.00 A; A=25-299.
DR   PDB; 1HHI; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 1HHJ; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 1HHK; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 1HLA; X-ray; 3.50 A; A=25-294.
DR   PDB; 1HSB; X-ray; 1.90 A; A=25-294.
DR   PDB; 1I1F; X-ray; 2.80 A; A/D=25-299.
DR   PDB; 1I1Y; X-ray; 2.20 A; A/D=25-299.
DR   PDB; 1I4F; X-ray; 1.40 A; A=25-299.
DR   PDB; 1I7R; X-ray; 2.20 A; A/D=25-299.
DR   PDB; 1I7T; X-ray; 2.80 A; A/D=25-299.
DR   PDB; 1I7U; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 1IM3; X-ray; 2.20 A; A/E/I/M=25-299.
DR   PDB; 1JF1; X-ray; 1.85 A; A=25-299.
DR   PDB; 1JHT; X-ray; 2.15 A; A=25-299.
DR   PDB; 1LP9; X-ray; 2.00 A; A/H=25-299.
DR   PDB; 1OGA; X-ray; 1.40 A; A=25-300.
DR   PDB; 1P7Q; X-ray; 3.40 A; A=25-300.
DR   PDB; 1Q94; X-ray; 2.40 A; A/D=25-299.
DR   PDB; 1QEW; X-ray; 2.20 A; A=25-299.
DR   PDB; 1QR1; X-ray; 2.40 A; A/D=25-299.
DR   PDB; 1QRN; X-ray; 2.80 A; A=25-298.
DR   PDB; 1QSE; X-ray; 2.80 A; A=25-298.
DR   PDB; 1QSF; X-ray; 2.80 A; A=25-298.
DR   PDB; 1QVO; X-ray; 2.22 A; A/D=25-299.
DR   PDB; 1S8D; X-ray; 2.20 A; A=25-299.
DR   PDB; 1S9W; X-ray; 2.20 A; A=25-298.
DR   PDB; 1S9X; X-ray; 2.50 A; A=25-298.
DR   PDB; 1S9Y; X-ray; 2.30 A; A=25-298.
DR   PDB; 1T1W; X-ray; 2.20 A; A=25-299.
DR   PDB; 1T1X; X-ray; 2.20 A; A=25-299.
DR   PDB; 1T1Y; X-ray; 2.00 A; A=25-299.
DR   PDB; 1T1Z; X-ray; 1.90 A; A=25-299.
DR   PDB; 1T20; X-ray; 2.20 A; A=25-299.
DR   PDB; 1T21; X-ray; 2.19 A; A=25-299.
DR   PDB; 1T22; X-ray; 2.20 A; A=25-299.
DR   PDB; 1TMC; X-ray; 2.30 A; A=25-199.
DR   PDB; 1TVB; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 1TVH; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 1W72; X-ray; 2.15 A; A/D=25-298.
DR   PDB; 1X7Q; X-ray; 1.45 A; A=25-299.
DR   PDB; 2AV1; X-ray; 1.95 A; A/D=25-299.
DR   PDB; 2AV7; X-ray; 2.05 A; A/D=25-299.
DR   PDB; 2BCK; X-ray; 2.80 A; A/D=25-300.
DR   PDB; 2BNQ; X-ray; 1.70 A; A=25-300.
DR   PDB; 2BNR; X-ray; 1.90 A; A=25-300.
DR   PDB; 2C7U; X-ray; 2.38 A; A/D=25-300.
DR   PDB; 2CLR; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 2F53; X-ray; 2.10 A; A=25-299.
DR   PDB; 2F54; X-ray; 2.70 A; A/F=25-298.
DR   PDB; 2GIT; X-ray; 1.70 A; A/D=25-299.
DR   PDB; 2GJ6; X-ray; 2.56 A; A=25-299.
DR   PDB; 2GT9; X-ray; 1.75 A; A/D=25-299.
DR   PDB; 2GTW; X-ray; 1.55 A; A/D=25-299.
DR   PDB; 2GTZ; X-ray; 1.70 A; A/D=25-299.
DR   PDB; 2GUO; X-ray; 1.90 A; A/D=25-299.
DR   PDB; 2HLA; X-ray; 2.60 A; A=25-294.
DR   PDB; 2HN7; X-ray; 1.60 A; A=25-299.
DR   PDB; 2J8U; X-ray; 2.88 A; A/H=25-299.
DR   PDB; 2JCC; X-ray; 2.50 A; A/H=25-299.
DR   PDB; 2P5E; X-ray; 1.89 A; A=25-300.
DR   PDB; 2P5W; X-ray; 2.20 A; A=25-300.
DR   PDB; 2PYE; X-ray; 2.30 A; A=25-300.
DR   PDB; 2UWE; X-ray; 2.40 A; A/H=25-299.
DR   PDB; 2V2W; X-ray; 1.60 A; A/D=25-300.
DR   PDB; 2V2X; X-ray; 1.60 A; A/D=25-300.
DR   PDB; 2VLJ; X-ray; 2.40 A; A=25-300.
DR   PDB; 2VLK; X-ray; 2.50 A; A=25-300.
DR   PDB; 2VLL; X-ray; 1.60 A; A/D=25-300.
DR   PDB; 2VLR; X-ray; 2.30 A; A/F=25-300.
DR   PDB; 2X4N; X-ray; 2.34 A; A/D=25-299.
DR   PDB; 2X4O; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 2X4P; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 2X4Q; X-ray; 1.90 A; A/D=25-299.
DR   PDB; 2X4R; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 2X4S; X-ray; 2.55 A; A/D=25-299.
DR   PDB; 2X4T; X-ray; 2.30 A; A/D=25-299.
DR   PDB; 2X4U; X-ray; 2.10 A; A/D=25-299.
DR   PDB; 2X70; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 2XPG; X-ray; 2.60 A; A=25-298.
DR   PDB; 3BGM; X-ray; 1.60 A; A=25-298.
DR   PDB; 3BH8; X-ray; 1.65 A; A=25-298.
DR   PDB; 3BH9; X-ray; 1.70 A; A=25-299.
DR   PDB; 3BHB; X-ray; 2.20 A; A=25-298.
DR   PDB; 3BO8; X-ray; 1.80 A; A=25-298.
DR   PDB; 3D25; X-ray; 1.30 A; A=25-298.
DR   PDB; 3D39; X-ray; 2.81 A; A=25-299.
DR   PDB; 3D3V; X-ray; 2.80 A; A=25-299.
DR   PDB; 3FQN; X-ray; 1.65 A; A=25-299.
DR   PDB; 3FQR; X-ray; 1.70 A; A=25-299.
DR   PDB; 3FQT; X-ray; 1.80 A; A=25-299.
DR   PDB; 3FQU; X-ray; 1.80 A; A=25-299.
DR   PDB; 3FQW; X-ray; 1.93 A; A=25-299.
DR   PDB; 3FQX; X-ray; 1.70 A; A=25-299.
DR   PDB; 3FT2; X-ray; 1.80 A; A=25-299.
DR   PDB; 3FT3; X-ray; 1.95 A; A=25-299.
DR   PDB; 3FT4; X-ray; 1.90 A; A=25-299.
DR   PDB; 3GIV; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 3GJF; X-ray; 1.90 A; A/D=25-300.
DR   PDB; 3GSN; X-ray; 2.80 A; H=25-298.
DR   PDB; 3GSO; X-ray; 1.60 A; A=25-298.
DR   PDB; 3GSQ; X-ray; 2.12 A; A=25-298.
DR   PDB; 3GSR; X-ray; 1.95 A; A=25-298.
DR   PDB; 3GSU; X-ray; 1.80 A; A=25-299.
DR   PDB; 3GSV; X-ray; 1.90 A; A=25-299.
DR   PDB; 3GSW; X-ray; 1.81 A; A=25-298.
DR   PDB; 3GSX; X-ray; 2.10 A; A=25-298.
DR   PDB; 3H7B; X-ray; 1.88 A; A/D=25-299.
DR   PDB; 3H9H; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 3H9S; X-ray; 2.70 A; A=25-299.
DR   PDB; 3HAE; X-ray; 2.90 A; A/D/J/P=25-300.
DR   PDB; 3HLA; X-ray; 2.60 A; A=25-294.
DR   PDB; 3HPJ; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 3I6G; X-ray; 2.20 A; A/D=25-299.
DR   PDB; 3I6K; X-ray; 2.80 A; A/E=25-299.
DR   PDB; 3I6L; X-ray; 2.40 A; D=25-298.
DR   PDB; 3IXA; X-ray; 2.10 A; A/D=25-299.
DR   PDB; 3KLA; X-ray; 1.65 A; A/D=25-299.
DR   PDB; 3MGO; X-ray; 2.30 A; A/D/G/J=25-299.
DR   PDB; 3MGT; X-ray; 2.20 A; A/D/G/J=25-299.
DR   PDB; 3MR9; X-ray; 1.93 A; A=25-300.
DR   PDB; 3MRB; X-ray; 1.40 A; A=25-300.
DR   PDB; 3MRC; X-ray; 1.80 A; A=25-300.
DR   PDB; 3MRD; X-ray; 1.70 A; A=25-300.
DR   PDB; 3MRE; X-ray; 1.10 A; A=25-300.
DR   PDB; 3MRF; X-ray; 2.30 A; A=25-300.
DR   PDB; 3MRG; X-ray; 1.30 A; A=25-300.
DR   PDB; 3MRH; X-ray; 2.40 A; A=25-300.
DR   PDB; 3MRI; X-ray; 2.10 A; A=25-300.
DR   PDB; 3MRJ; X-ray; 1.87 A; A=25-300.
DR   PDB; 3MRK; X-ray; 1.40 A; A=25-300.
DR   PDB; 3MRL; X-ray; 2.41 A; A=25-300.
DR   PDB; 3MRM; X-ray; 1.90 A; A=25-300.
DR   PDB; 3MRN; X-ray; 2.30 A; A=25-300.
DR   PDB; 3MRO; X-ray; 2.35 A; A=25-300.
DR   PDB; 3MRP; X-ray; 2.10 A; A=25-300.
DR   PDB; 3MRQ; X-ray; 2.20 A; A=25-300.
DR   PDB; 3MRR; X-ray; 1.60 A; A=25-300.
DR   PDB; 3MYJ; X-ray; 1.89 A; A/D=25-299.
DR   PDB; 3NFN; X-ray; 2.39 A; A=25-298.
DR   PDB; 3O3A; X-ray; 1.80 A; A/D=25-299.
DR   PDB; 3O3B; X-ray; 1.90 A; A/D=25-299.
DR   PDB; 3O3D; X-ray; 1.70 A; A/D=25-299.
DR   PDB; 3O3E; X-ray; 1.85 A; A/D=25-299.
DR   PDB; 3O4L; X-ray; 2.54 A; A=25-300.
DR   PDB; 3PWJ; X-ray; 1.70 A; A/D=25-299.
DR   PDB; 3PWL; X-ray; 1.65 A; A/D=25-299.
DR   PDB; 3PWN; X-ray; 1.60 A; A/D=25-299.
DR   PDB; 3PWP; X-ray; 2.69 A; A=25-299.
DR   PDB; 3QDG; X-ray; 2.69 A; A=25-299.
DR   PDB; 3QDJ; X-ray; 2.30 A; A=25-299.
DR   PDB; 3QDM; X-ray; 2.80 A; A=25-299.
DR   PDB; 3QEQ; X-ray; 2.59 A; A=25-299.
DR   PDB; 3QFD; X-ray; 1.68 A; A/D=25-299.
DR   PDB; 3QFJ; X-ray; 2.29 A; A=25-299.
DR   PDB; 3QZW; X-ray; 2.80 A; A/D=25-298.
DR   PDB; 3REW; X-ray; 1.90 A; A/D=25-299.
DR   PDB; 3RL1; X-ray; 2.00 A; A=25-298.
DR   PDB; 3RL2; X-ray; 2.39 A; A=25-298.
DR   PDB; 3TO2; X-ray; 2.60 A; A=25-299.
DR   PDB; 3UTQ; X-ray; 1.67 A; A=25-300.
DR   PDB; 3UTS; X-ray; 2.71 A; A/F=25-300.
DR   PDB; 3UTT; X-ray; 2.60 A; A/F=25-299.
DR   PDB; 3V5D; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 3V5H; X-ray; 1.63 A; A/D=25-299.
DR   PDB; 3V5K; X-ray; 2.31 A; A/D=25-299.
DR   PDB; 3VXM; X-ray; 2.50 A; A=25-298.
DR   PDB; 3VXN; X-ray; 1.95 A; A=25-298.
DR   PDB; 3VXO; X-ray; 2.61 A; A/D=25-298.
DR   PDB; 3VXP; X-ray; 2.50 A; A/D=25-298.
DR   PDB; 3VXR; X-ray; 2.40 A; A=25-298.
DR   PDB; 3VXS; X-ray; 1.80 A; A=25-298.
DR   PDB; 3VXU; X-ray; 2.70 A; A/F=25-298.
DR   PDB; 3W0W; X-ray; 2.60 A; A=25-298.
DR   PDB; 3WL9; X-ray; 1.66 A; A=25-298.
DR   PDB; 3WLB; X-ray; 2.00 A; A=25-298.
DR   PDB; 4E5X; X-ray; 1.95 A; A/D=25-299.
DR   PDB; 4EMZ; X-ray; 2.90 A; D/E=338-365.
DR   PDB; 4EN2; X-ray; 2.58 A; D/E=338-365.
DR   PDB; 4EUP; X-ray; 2.88 A; A/D=25-299.
DR   PDB; 4F7M; X-ray; 2.40 A; A/D=25-298.
DR   PDB; 4F7P; X-ray; 1.90 A; A=25-298.
DR   PDB; 4F7T; X-ray; 1.70 A; A/D=25-298.
DR   PDB; 4FTV; X-ray; 2.74 A; A=25-299.
DR   PDB; 4GKN; X-ray; 2.75 A; A/D=25-300.
DR   PDB; 4GKS; X-ray; 2.35 A; A/D=25-300.
DR   PDB; 4HWZ; X-ray; 2.40 A; A=25-298.
DR   PDB; 4HX1; X-ray; 1.80 A; A=25-296.
DR   PDB; 4I48; X-ray; 2.80 A; A=25-296.
DR   PDB; 4I4W; X-ray; 1.77 A; A=25-300.
DR   PDB; 4JFD; X-ray; 2.46 A; A=25-300.
DR   PDB; 4JFE; X-ray; 2.70 A; A=25-300.
DR   PDB; 4JFF; X-ray; 2.43 A; A=25-300.
DR   PDB; 4JFO; X-ray; 2.11 A; A/D=25-299.
DR   PDB; 4JFP; X-ray; 1.91 A; A/D=25-300.
DR   PDB; 4JFQ; X-ray; 1.90 A; A/D=25-300.
DR   PDB; 4K7F; X-ray; 2.00 A; A/D=25-299.
DR   PDB; 4L29; X-ray; 3.09 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300.
DR   PDB; 4L3C; X-ray; 2.64 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300.
DR   PDB; 4L3E; X-ray; 2.56 A; A=25-299.
DR   PDB; 4MJ5; X-ray; 2.40 A; A=25-298.
DR   PDB; 4MJ6; X-ray; 2.57 A; A=25-298.
DR   PDB; 4MNQ; X-ray; 2.74 A; A=25-300.
DR   PDB; 4N8V; X-ray; 2.50 A; A/D=25-298.
DR   PDB; 4NNX; X-ray; 2.10 A; A=25-298.
DR   PDB; 4NNY; X-ray; 1.90 A; A=25-298.
DR   PDB; 4NO0; X-ray; 2.70 A; A=25-300.
DR   PDB; 4NO2; X-ray; 2.00 A; A=25-298.
DR   PDB; 4NO3; X-ray; 1.70 A; A=25-298.
DR   PDB; 4NO5; X-ray; 2.10 A; A=25-299.
DR   PDB; 4NQV; X-ray; 2.39 A; A/C/E/G/I/K=25-298.
DR   PDB; 4NQX; X-ray; 2.00 A; A/C/E/G/I/K=25-308.
DR   PDB; 4OV5; X-ray; 2.20 A; C/F/I/L/O/R=128-141.
DR   PDB; 4QOK; X-ray; 3.00 A; A=25-300.
DR   PDB; 4U6X; X-ray; 1.68 A; A=25-300.
DR   PDB; 4U6Y; X-ray; 1.47 A; A=25-300.
DR   PDB; 4UQ2; X-ray; 2.43 A; A/C=25-299.
DR   PDB; 4UQ3; X-ray; 2.10 A; A/C=25-299.
DR   PDB; 4WJ5; X-ray; 1.65 A; A/D=25-299.
DR   PDB; 4WU5; X-ray; 2.40 A; A/D=25-298.
DR   PDB; 4WU7; X-ray; 2.30 A; A/D=25-298.
DR   PDB; 4WUU; X-ray; 3.05 A; A=25-300.
DR   PDB; 5BRZ; X-ray; 2.62 A; A=25-298.
DR   PDB; 5BS0; X-ray; 2.40 A; A=25-298.
DR   PDB; 5C07; X-ray; 2.11 A; A/F=25-300.
DR   PDB; 5C08; X-ray; 2.33 A; A/F=25-300.
DR   PDB; 5C09; X-ray; 2.48 A; A/F=25-300.
DR   PDB; 5C0A; X-ray; 2.46 A; A/F=25-300.
DR   PDB; 5C0B; X-ray; 2.03 A; A/F=25-299.
DR   PDB; 5C0C; X-ray; 1.97 A; A/F=25-300.
DR   PDB; 5C0D; X-ray; 1.68 A; A=25-300.
DR   PDB; 5C0E; X-ray; 1.49 A; A=25-300.
DR   PDB; 5C0F; X-ray; 1.46 A; A=25-300.
DR   PDB; 5C0G; X-ray; 1.37 A; A=25-300.
DR   PDB; 5C0I; X-ray; 1.53 A; A=25-300.
DR   PDB; 5C0J; X-ray; 1.64 A; A=25-300.
DR   PDB; 5D2L; X-ray; 3.51 A; A/C/G/M=25-299.
DR   PDB; 5D2N; X-ray; 2.10 A; A/H=25-299.
DR   PDB; 5D9S; X-ray; 1.87 A; A=25-298.
DR   PDB; 5DDH; X-ray; 1.50 A; A=25-298.
DR   PDB; 5E00; X-ray; 1.70 A; A=25-299.
DR   PDB; 5E6I; X-ray; 4.00 A; C/I/M/R=25-299.
DR   PDB; 5E9D; X-ray; 2.51 A; A/F=25-299.
DR   PDB; 5ENW; X-ray; 1.85 A; A=25-298.
DR   PDB; 5EOT; X-ray; 2.10 A; A=26-298.
DR   PDB; 5EU3; X-ray; 1.97 A; A=25-300.
DR   PDB; 5EU4; X-ray; 2.12 A; A/D=25-300.
DR   PDB; 5EU5; X-ray; 1.54 A; A=25-300.
DR   PDB; 5EU6; X-ray; 2.02 A; A=25-300.
DR   PDB; 5EUO; X-ray; 2.10 A; A/C=25-299.
DR   PDB; 5F7D; X-ray; 2.30 A; A=26-298.
DR   PDB; 5F9J; X-ray; 2.51 A; A=25-298.
DR   PDB; 5FA3; X-ray; 1.86 A; A=26-298.
DR   PDB; 5FA4; X-ray; 2.40 A; A=25-298.
DR   PDB; 5FDW; X-ray; 2.70 A; A=25-298.
DR   PDB; 5GRD; X-ray; 1.80 A; A=25-299.
DR   PDB; 5GRG; X-ray; 1.94 A; A=25-299.
DR   PDB; 5GSD; X-ray; 2.30 A; A=25-299.
DR   PDB; 5HGA; X-ray; 2.20 A; A/D=25-298.
DR   PDB; 5HGB; X-ray; 2.40 A; A/D/G/J=25-298.
DR   PDB; 5HGD; X-ray; 2.07 A; A/D=25-298.
DR   PDB; 5HGH; X-ray; 2.39 A; A=25-298.
DR   PDB; 5HHM; X-ray; 2.50 A; A/F=25-300.
DR   PDB; 5HHN; X-ray; 2.03 A; A=25-298.
DR   PDB; 5HHO; X-ray; 2.95 A; A=25-300.
DR   PDB; 5HHP; X-ray; 1.90 A; A=25-298.
DR   PDB; 5HHQ; X-ray; 2.10 A; A=25-298.
DR   PDB; 5HYJ; X-ray; 3.06 A; A/F=25-300.
DR   PDB; 5IRO; X-ray; 2.64 A; A/E/I/M/Q/U=25-299.
DR   PDB; 5ISZ; X-ray; 2.06 A; A=25-299.
DR   PDB; 5JHD; X-ray; 2.46 A; A/F=25-299.
DR   PDB; 5JZI; X-ray; 2.50 A; A/F=25-299.
DR   PDB; 5MEN; X-ray; 2.81 A; A=25-300.
DR   PDB; 5MEO; X-ray; 1.77 A; A=25-300.
DR   PDB; 5MEP; X-ray; 2.71 A; A/D=25-300.
DR   PDB; 5MEQ; X-ray; 2.27 A; A=25-300.
DR   PDB; 5MER; X-ray; 1.88 A; A/D=25-300.
DR   PDB; 5N1Y; X-ray; 1.39 A; A=25-300.
DR   PDB; 5N6B; X-ray; 1.71 A; A/D=25-300.
DR   PDB; 5NHT; X-ray; 3.20 A; H=25-300.
DR   PDB; 5NME; X-ray; 2.94 A; A/F=25-300.
DR   PDB; 5NMF; X-ray; 2.89 A; A/F=25-300.
DR   PDB; 5NMG; X-ray; 2.75 A; A/F=25-300.
DR   PDB; 5NMH; X-ray; 1.55 A; A=25-300.
DR   PDB; 5NMK; X-ray; 1.66 A; A=25-300.
DR   PDB; 5NQK; X-ray; 3.25 A; H=25-300.
DR   PDB; 5SWQ; X-ray; 2.00 A; A=25-300.
DR   PDB; 5TEZ; X-ray; 1.70 A; A=25-299.
DR   PDB; 5W1W; X-ray; 3.10 A; C/H/M/R=3-11.
DR   PDB; 5WJL; X-ray; 3.15 A; A/D/G=25-298.
DR   PDB; 5WJN; X-ray; 2.85 A; A/D/G=25-298.
DR   PDB; 5WKF; X-ray; 2.95 A; A/F=25-298.
DR   PDB; 5WKH; X-ray; 3.20 A; A/F=25-298.
DR   PDB; 5WSH; X-ray; 2.00 A; A=25-299.
DR   PDB; 5WWI; X-ray; 3.19 A; A=25-298.
DR   PDB; 5WWJ; X-ray; 2.29 A; A/C=25-298.
DR   PDB; 5WWU; X-ray; 2.79 A; A=25-298.
DR   PDB; 5WXC; X-ray; 2.29 A; A/C=25-298.
DR   PDB; 5WXD; X-ray; 3.29 A; A=25-298.
DR   PDB; 5XOV; X-ray; 2.68 A; A/D=25-298.
DR   PDB; 5YXN; X-ray; 2.03 A; C=25-299.
DR   PDB; 5YXU; X-ray; 2.70 A; C/E=25-299.
DR   PDB; 6AM5; X-ray; 2.39 A; A=25-299.
DR   PDB; 6AMT; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 6AMU; X-ray; 2.15 A; A=26-298.
DR   PDB; 6APN; X-ray; 2.22 A; A/B=26-301.
DR   PDB; 6AT9; X-ray; 2.95 A; A=25-304.
DR   PDB; 6D78; X-ray; 2.35 A; A=25-299.
DR   PDB; 6D7G; X-ray; 2.75 A; A=25-299.
DR   PDB; 6DKP; X-ray; 2.97 A; A=25-299.
DR   PDB; 6EI2; X-ray; 1.61 A; A=25-299.
DR   PDB; 6ENY; EM; 5.80 A; F=25-365.
DR   PDB; 6EQA; X-ray; 3.16 A; A=25-300.
DR   PDB; 6EQB; X-ray; 2.81 A; A=25-300.
DR   PDB; 6EWA; X-ray; 2.39 A; A/E=25-300.
DR   PDB; 6EWC; X-ray; 3.20 A; A/E=25-300.
DR   PDB; 6EWO; X-ray; 2.30 A; A/E=25-300.
DR   PDB; 6G3J; X-ray; 2.45 A; A/D=25-300.
DR   PDB; 6G3K; X-ray; 2.90 A; A/D=25-300.
DR   PDB; 6ID4; X-ray; 2.40 A; A/E=25-299.
DR   PDB; 6J1W; X-ray; 1.50 A; A=25-298.
DR   PDB; 6J29; X-ray; 1.60 A; A=25-298.
DR   PDB; 6J2A; X-ray; 1.40 A; A=25-298.
DR   PDB; 6JOZ; X-ray; 1.35 A; A=25-299.
DR   PDB; 6JP3; X-ray; 1.66 A; A=25-299.
DR   PDB; 6MPP; NMR; -; A=25-303.
DR   PDB; 6NCA; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=25-299.
DR   PDB; 6O9B; X-ray; 2.20 A; A=25-304.
DR   PDB; 6O9C; X-ray; 2.45 A; A=25-304.
DR   PDB; 6OPD; X-ray; 1.79 A; A=25-299.
DR   PDB; 6PBH; X-ray; 1.89 A; A=25-302.
DR   PDB; 6PTB; X-ray; 2.15 A; A/D=25-299.
DR   PDB; 6PTE; X-ray; 1.90 A; A/E/H/K=25-299.
DR   PDB; 6Q3K; X-ray; 1.50 A; A=24-299.
DR   PDB; 6Q3S; X-ray; 2.50 A; A=25-300.
DR   PDB; 6R2L; X-ray; 2.30 A; A=25-299.
DR   PDB; 6RP9; X-ray; 3.12 A; A/F=25-299.
DR   PDB; 6RPA; X-ray; 2.56 A; A=25-299.
DR   PDB; 6RPB; X-ray; 2.50 A; A/F/K/P=25-299.
DR   PDB; 6RSY; X-ray; 2.95 A; A/F=25-299.
DR   PDB; 6SS7; X-ray; 2.50 A; A/D=25-299.
DR   PDB; 6SS8; X-ray; 2.24 A; A/D=25-299.
DR   PDB; 6SS9; X-ray; 2.70 A; A/D=25-299.
DR   PDB; 6SSA; X-ray; 2.11 A; A/D/G/J=25-299.
DR   PDB; 7L1B; X-ray; 2.04 A; A=25-298.
DR   PDB; 7L1C; X-ray; 1.96 A; A=25-298.
DR   PDB; 7L1D; X-ray; 3.11 A; A=25-298.
DR   PDB; 7MLE; X-ray; 2.20 A; A=25-301.
DR   PDB; 7RM4; X-ray; 3.33 A; A/F/K/P=25-299.
DR   PDB; 7RRG; X-ray; 2.12 A; A=25-298.
DR   PDBsum; 1AKJ; -.
DR   PDBsum; 1AO7; -.
DR   PDBsum; 1AQD; -.
DR   PDBsum; 1B0G; -.
DR   PDBsum; 1B0R; -.
DR   PDBsum; 1BD2; -.
DR   PDBsum; 1DUY; -.
DR   PDBsum; 1DUZ; -.
DR   PDBsum; 1EEY; -.
DR   PDBsum; 1EEZ; -.
DR   PDBsum; 1HHG; -.
DR   PDBsum; 1HHH; -.
DR   PDBsum; 1HHI; -.
DR   PDBsum; 1HHJ; -.
DR   PDBsum; 1HHK; -.
DR   PDBsum; 1HLA; -.
DR   PDBsum; 1HSB; -.
DR   PDBsum; 1I1F; -.
DR   PDBsum; 1I1Y; -.
DR   PDBsum; 1I4F; -.
DR   PDBsum; 1I7R; -.
DR   PDBsum; 1I7T; -.
DR   PDBsum; 1I7U; -.
DR   PDBsum; 1IM3; -.
DR   PDBsum; 1JF1; -.
DR   PDBsum; 1JHT; -.
DR   PDBsum; 1LP9; -.
DR   PDBsum; 1OGA; -.
DR   PDBsum; 1P7Q; -.
DR   PDBsum; 1Q94; -.
DR   PDBsum; 1QEW; -.
DR   PDBsum; 1QR1; -.
DR   PDBsum; 1QRN; -.
DR   PDBsum; 1QSE; -.
DR   PDBsum; 1QSF; -.
DR   PDBsum; 1QVO; -.
DR   PDBsum; 1S8D; -.
DR   PDBsum; 1S9W; -.
DR   PDBsum; 1S9X; -.
DR   PDBsum; 1S9Y; -.
DR   PDBsum; 1T1W; -.
DR   PDBsum; 1T1X; -.
DR   PDBsum; 1T1Y; -.
DR   PDBsum; 1T1Z; -.
DR   PDBsum; 1T20; -.
DR   PDBsum; 1T21; -.
DR   PDBsum; 1T22; -.
DR   PDBsum; 1TMC; -.
DR   PDBsum; 1TVB; -.
DR   PDBsum; 1TVH; -.
DR   PDBsum; 1W72; -.
DR   PDBsum; 1X7Q; -.
DR   PDBsum; 2AV1; -.
DR   PDBsum; 2AV7; -.
DR   PDBsum; 2BCK; -.
DR   PDBsum; 2BNQ; -.
DR   PDBsum; 2BNR; -.
DR   PDBsum; 2C7U; -.
DR   PDBsum; 2CLR; -.
DR   PDBsum; 2F53; -.
DR   PDBsum; 2F54; -.
DR   PDBsum; 2GIT; -.
DR   PDBsum; 2GJ6; -.
DR   PDBsum; 2GT9; -.
DR   PDBsum; 2GTW; -.
DR   PDBsum; 2GTZ; -.
DR   PDBsum; 2GUO; -.
DR   PDBsum; 2HLA; -.
DR   PDBsum; 2HN7; -.
DR   PDBsum; 2J8U; -.
DR   PDBsum; 2JCC; -.
DR   PDBsum; 2P5E; -.
DR   PDBsum; 2P5W; -.
DR   PDBsum; 2PYE; -.
DR   PDBsum; 2UWE; -.
DR   PDBsum; 2V2W; -.
DR   PDBsum; 2V2X; -.
DR   PDBsum; 2VLJ; -.
DR   PDBsum; 2VLK; -.
DR   PDBsum; 2VLL; -.
DR   PDBsum; 2VLR; -.
DR   PDBsum; 2X4N; -.
DR   PDBsum; 2X4O; -.
DR   PDBsum; 2X4P; -.
DR   PDBsum; 2X4Q; -.
DR   PDBsum; 2X4R; -.
DR   PDBsum; 2X4S; -.
DR   PDBsum; 2X4T; -.
DR   PDBsum; 2X4U; -.
DR   PDBsum; 2X70; -.
DR   PDBsum; 2XPG; -.
DR   PDBsum; 3BGM; -.
DR   PDBsum; 3BH8; -.
DR   PDBsum; 3BH9; -.
DR   PDBsum; 3BHB; -.
DR   PDBsum; 3BO8; -.
DR   PDBsum; 3D25; -.
DR   PDBsum; 3D39; -.
DR   PDBsum; 3D3V; -.
DR   PDBsum; 3FQN; -.
DR   PDBsum; 3FQR; -.
DR   PDBsum; 3FQT; -.
DR   PDBsum; 3FQU; -.
DR   PDBsum; 3FQW; -.
DR   PDBsum; 3FQX; -.
DR   PDBsum; 3FT2; -.
DR   PDBsum; 3FT3; -.
DR   PDBsum; 3FT4; -.
DR   PDBsum; 3GIV; -.
DR   PDBsum; 3GJF; -.
DR   PDBsum; 3GSN; -.
DR   PDBsum; 3GSO; -.
DR   PDBsum; 3GSQ; -.
DR   PDBsum; 3GSR; -.
DR   PDBsum; 3GSU; -.
DR   PDBsum; 3GSV; -.
DR   PDBsum; 3GSW; -.
DR   PDBsum; 3GSX; -.
DR   PDBsum; 3H7B; -.
DR   PDBsum; 3H9H; -.
DR   PDBsum; 3H9S; -.
DR   PDBsum; 3HAE; -.
DR   PDBsum; 3HLA; -.
DR   PDBsum; 3HPJ; -.
DR   PDBsum; 3I6G; -.
DR   PDBsum; 3I6K; -.
DR   PDBsum; 3I6L; -.
DR   PDBsum; 3IXA; -.
DR   PDBsum; 3KLA; -.
DR   PDBsum; 3MGO; -.
DR   PDBsum; 3MGT; -.
DR   PDBsum; 3MR9; -.
DR   PDBsum; 3MRB; -.
DR   PDBsum; 3MRC; -.
DR   PDBsum; 3MRD; -.
DR   PDBsum; 3MRE; -.
DR   PDBsum; 3MRF; -.
DR   PDBsum; 3MRG; -.
DR   PDBsum; 3MRH; -.
DR   PDBsum; 3MRI; -.
DR   PDBsum; 3MRJ; -.
DR   PDBsum; 3MRK; -.
DR   PDBsum; 3MRL; -.
DR   PDBsum; 3MRM; -.
DR   PDBsum; 3MRN; -.
DR   PDBsum; 3MRO; -.
DR   PDBsum; 3MRP; -.
DR   PDBsum; 3MRQ; -.
DR   PDBsum; 3MRR; -.
DR   PDBsum; 3MYJ; -.
DR   PDBsum; 3NFN; -.
DR   PDBsum; 3O3A; -.
DR   PDBsum; 3O3B; -.
DR   PDBsum; 3O3D; -.
DR   PDBsum; 3O3E; -.
DR   PDBsum; 3O4L; -.
DR   PDBsum; 3PWJ; -.
DR   PDBsum; 3PWL; -.
DR   PDBsum; 3PWN; -.
DR   PDBsum; 3PWP; -.
DR   PDBsum; 3QDG; -.
DR   PDBsum; 3QDJ; -.
DR   PDBsum; 3QDM; -.
DR   PDBsum; 3QEQ; -.
DR   PDBsum; 3QFD; -.
DR   PDBsum; 3QFJ; -.
DR   PDBsum; 3QZW; -.
DR   PDBsum; 3REW; -.
DR   PDBsum; 3RL1; -.
DR   PDBsum; 3RL2; -.
DR   PDBsum; 3TO2; -.
DR   PDBsum; 3UTQ; -.
DR   PDBsum; 3UTS; -.
DR   PDBsum; 3UTT; -.
DR   PDBsum; 3V5D; -.
DR   PDBsum; 3V5H; -.
DR   PDBsum; 3V5K; -.
DR   PDBsum; 3VXM; -.
DR   PDBsum; 3VXN; -.
DR   PDBsum; 3VXO; -.
DR   PDBsum; 3VXP; -.
DR   PDBsum; 3VXR; -.
DR   PDBsum; 3VXS; -.
DR   PDBsum; 3VXU; -.
DR   PDBsum; 3W0W; -.
DR   PDBsum; 3WL9; -.
DR   PDBsum; 3WLB; -.
DR   PDBsum; 4E5X; -.
DR   PDBsum; 4EMZ; -.
DR   PDBsum; 4EN2; -.
DR   PDBsum; 4EUP; -.
DR   PDBsum; 4F7M; -.
DR   PDBsum; 4F7P; -.
DR   PDBsum; 4F7T; -.
DR   PDBsum; 4FTV; -.
DR   PDBsum; 4GKN; -.
DR   PDBsum; 4GKS; -.
DR   PDBsum; 4HWZ; -.
DR   PDBsum; 4HX1; -.
DR   PDBsum; 4I48; -.
DR   PDBsum; 4I4W; -.
DR   PDBsum; 4JFD; -.
DR   PDBsum; 4JFE; -.
DR   PDBsum; 4JFF; -.
DR   PDBsum; 4JFO; -.
DR   PDBsum; 4JFP; -.
DR   PDBsum; 4JFQ; -.
DR   PDBsum; 4K7F; -.
DR   PDBsum; 4L29; -.
DR   PDBsum; 4L3C; -.
DR   PDBsum; 4L3E; -.
DR   PDBsum; 4MJ5; -.
DR   PDBsum; 4MJ6; -.
DR   PDBsum; 4MNQ; -.
DR   PDBsum; 4N8V; -.
DR   PDBsum; 4NNX; -.
DR   PDBsum; 4NNY; -.
DR   PDBsum; 4NO0; -.
DR   PDBsum; 4NO2; -.
DR   PDBsum; 4NO3; -.
DR   PDBsum; 4NO5; -.
DR   PDBsum; 4NQV; -.
DR   PDBsum; 4NQX; -.
DR   PDBsum; 4OV5; -.
DR   PDBsum; 4QOK; -.
DR   PDBsum; 4U6X; -.
DR   PDBsum; 4U6Y; -.
DR   PDBsum; 4UQ2; -.
DR   PDBsum; 4UQ3; -.
DR   PDBsum; 4WJ5; -.
DR   PDBsum; 4WU5; -.
DR   PDBsum; 4WU7; -.
DR   PDBsum; 4WUU; -.
DR   PDBsum; 5BRZ; -.
DR   PDBsum; 5BS0; -.
DR   PDBsum; 5C07; -.
DR   PDBsum; 5C08; -.
DR   PDBsum; 5C09; -.
DR   PDBsum; 5C0A; -.
DR   PDBsum; 5C0B; -.
DR   PDBsum; 5C0C; -.
DR   PDBsum; 5C0D; -.
DR   PDBsum; 5C0E; -.
DR   PDBsum; 5C0F; -.
DR   PDBsum; 5C0G; -.
DR   PDBsum; 5C0I; -.
DR   PDBsum; 5C0J; -.
DR   PDBsum; 5D2L; -.
DR   PDBsum; 5D2N; -.
DR   PDBsum; 5D9S; -.
DR   PDBsum; 5DDH; -.
DR   PDBsum; 5E00; -.
DR   PDBsum; 5E6I; -.
DR   PDBsum; 5E9D; -.
DR   PDBsum; 5ENW; -.
DR   PDBsum; 5EOT; -.
DR   PDBsum; 5EU3; -.
DR   PDBsum; 5EU4; -.
DR   PDBsum; 5EU5; -.
DR   PDBsum; 5EU6; -.
DR   PDBsum; 5EUO; -.
DR   PDBsum; 5F7D; -.
DR   PDBsum; 5F9J; -.
DR   PDBsum; 5FA3; -.
DR   PDBsum; 5FA4; -.
DR   PDBsum; 5FDW; -.
DR   PDBsum; 5GRD; -.
DR   PDBsum; 5GRG; -.
DR   PDBsum; 5GSD; -.
DR   PDBsum; 5HGA; -.
DR   PDBsum; 5HGB; -.
DR   PDBsum; 5HGD; -.
DR   PDBsum; 5HGH; -.
DR   PDBsum; 5HHM; -.
DR   PDBsum; 5HHN; -.
DR   PDBsum; 5HHO; -.
DR   PDBsum; 5HHP; -.
DR   PDBsum; 5HHQ; -.
DR   PDBsum; 5HYJ; -.
DR   PDBsum; 5IRO; -.
DR   PDBsum; 5ISZ; -.
DR   PDBsum; 5JHD; -.
DR   PDBsum; 5JZI; -.
DR   PDBsum; 5MEN; -.
DR   PDBsum; 5MEO; -.
DR   PDBsum; 5MEP; -.
DR   PDBsum; 5MEQ; -.
DR   PDBsum; 5MER; -.
DR   PDBsum; 5N1Y; -.
DR   PDBsum; 5N6B; -.
DR   PDBsum; 5NHT; -.
DR   PDBsum; 5NME; -.
DR   PDBsum; 5NMF; -.
DR   PDBsum; 5NMG; -.
DR   PDBsum; 5NMH; -.
DR   PDBsum; 5NMK; -.
DR   PDBsum; 5NQK; -.
DR   PDBsum; 5SWQ; -.
DR   PDBsum; 5TEZ; -.
DR   PDBsum; 5W1W; -.
DR   PDBsum; 5WJL; -.
DR   PDBsum; 5WJN; -.
DR   PDBsum; 5WKF; -.
DR   PDBsum; 5WKH; -.
DR   PDBsum; 5WSH; -.
DR   PDBsum; 5WWI; -.
DR   PDBsum; 5WWJ; -.
DR   PDBsum; 5WWU; -.
DR   PDBsum; 5WXC; -.
DR   PDBsum; 5WXD; -.
DR   PDBsum; 5XOV; -.
DR   PDBsum; 5YXN; -.
DR   PDBsum; 5YXU; -.
DR   PDBsum; 6AM5; -.
DR   PDBsum; 6AMT; -.
DR   PDBsum; 6AMU; -.
DR   PDBsum; 6APN; -.
DR   PDBsum; 6AT9; -.
DR   PDBsum; 6D78; -.
DR   PDBsum; 6D7G; -.
DR   PDBsum; 6DKP; -.
DR   PDBsum; 6EI2; -.
DR   PDBsum; 6ENY; -.
DR   PDBsum; 6EQA; -.
DR   PDBsum; 6EQB; -.
DR   PDBsum; 6EWA; -.
DR   PDBsum; 6EWC; -.
DR   PDBsum; 6EWO; -.
DR   PDBsum; 6G3J; -.
DR   PDBsum; 6G3K; -.
DR   PDBsum; 6ID4; -.
DR   PDBsum; 6J1W; -.
DR   PDBsum; 6J29; -.
DR   PDBsum; 6J2A; -.
DR   PDBsum; 6JOZ; -.
DR   PDBsum; 6JP3; -.
DR   PDBsum; 6MPP; -.
DR   PDBsum; 6NCA; -.
DR   PDBsum; 6O9B; -.
DR   PDBsum; 6O9C; -.
DR   PDBsum; 6OPD; -.
DR   PDBsum; 6PBH; -.
DR   PDBsum; 6PTB; -.
DR   PDBsum; 6PTE; -.
DR   PDBsum; 6Q3K; -.
DR   PDBsum; 6Q3S; -.
DR   PDBsum; 6R2L; -.
DR   PDBsum; 6RP9; -.
DR   PDBsum; 6RPA; -.
DR   PDBsum; 6RPB; -.
DR   PDBsum; 6RSY; -.
DR   PDBsum; 6SS7; -.
DR   PDBsum; 6SS8; -.
DR   PDBsum; 6SS9; -.
DR   PDBsum; 6SSA; -.
DR   PDBsum; 7L1B; -.
DR   PDBsum; 7L1C; -.
DR   PDBsum; 7L1D; -.
DR   PDBsum; 7MLE; -.
DR   PDBsum; 7RM4; -.
DR   PDBsum; 7RRG; -.
DR   AlphaFoldDB; P04439; -.
DR   SMR; P04439; -.
DR   BioGRID; 109350; 351.
DR   IntAct; P04439; 115.
DR   MINT; P04439; -.
DR   STRING; 9606.ENSP00000379873; -.
DR   BindingDB; P04439; -.
DR   ChEMBL; CHEMBL2632; -.
DR   DrugBank; DB02740; 3-Indolebutyric Acid.
DR   DrugBank; DB11294; Coccidioides immitis spherule.
DR   DrugBank; DB06226; Nelipepimut-S.
DR   TCDB; 9.A.75.1.2; the mhc ii receptor (mhc2r) family.
DR   GlyConnect; 1315; 3 N-Linked glycans (1 site).
DR   GlyConnect; 1316; 3 N-Linked glycans (1 site).
DR   GlyConnect; 1317; 4 N-Linked glycans (1 site).
DR   GlyConnect; 1318; 1 N-Linked glycan (1 site).
DR   GlyConnect; 1319; 3 N-Linked glycans (1 site).
DR   GlyConnect; 1320; 3 N-Linked glycans (1 site).
DR   GlyConnect; 1321; 1 N-Linked glycan (1 site).
DR   GlyConnect; 1322; 1 N-Linked glycan (1 site).
DR   GlyConnect; 1323; 4 N-Linked glycans (1 site).
DR   GlyConnect; 1324; 3 N-Linked glycans (1 site).
DR   GlyConnect; 1325; 4 N-Linked glycans (1 site).
DR   GlyConnect; 1326; 4 N-Linked glycans (1 site).
DR   GlyConnect; 1327; 1 N-Linked glycan (1 site).
DR   GlyConnect; 1328; 3 N-Linked glycans (1 site).
DR   GlyConnect; 1329; 1 N-Linked glycan (1 site).
DR   GlyGen; P04439; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P04439; -.
DR   PhosphoSitePlus; P04439; -.
DR   SwissPalm; P04439; -.
DR   BioMuta; HLA-A; -.
DR   DMDM; 13124681; -.
DR   EPD; P04439; -.
DR   jPOST; P04439; -.
DR   MassIVE; P04439; -.
DR   MaxQB; P04439; -.
DR   PaxDb; P04439; -.
DR   PeptideAtlas; P04439; -.
DR   PRIDE; P04439; -.
DR   ProteomicsDB; 51505; -.
DR   ProteomicsDB; 51506; -.
DR   ProteomicsDB; 51714; -.
DR   ProteomicsDB; 51843; -.
DR   ProteomicsDB; 52596; -.
DR   ProteomicsDB; 52597; -.
DR   ProteomicsDB; 52979; -.
DR   ProteomicsDB; 52980; -.
DR   ProteomicsDB; 53320; -.
DR   ProteomicsDB; 53321; -.
DR   ProteomicsDB; 53322; -.
DR   ProteomicsDB; 53564; -.
DR   ProteomicsDB; 54669; -.
DR   ProteomicsDB; 54670; -.
DR   ProteomicsDB; 54671; -.
DR   ProteomicsDB; 54672; -.
DR   ProteomicsDB; 54673; -.
DR   ProteomicsDB; 54674; -.
DR   ProteomicsDB; 54675; -.
DR   ProteomicsDB; 54676; -.
DR   ProteomicsDB; 54707; -.
DR   ProteomicsDB; 58716; -.
DR   ABCD; P04439; 62 sequenced antibodies.
DR   Antibodypedia; 26136; 1336 antibodies from 31 providers.
DR   CPTC; P04439; 1 antibody.
DR   DNASU; 3105; -.
DR   Ensembl; ENST00000376809.10; ENSP00000366005.5; ENSG00000206503.13. [P04439-1]
DR   Ensembl; ENST00000396634.5; ENSP00000379873.1; ENSG00000206503.13. [P04439-1]
DR   GeneID; 3105; -.
DR   KEGG; hsa:3105; -.
DR   MANE-Select; ENST00000376809.10; ENSP00000366005.5; NM_002116.8; NP_002107.3.
DR   UCSC; uc021zos.2; human.
DR   CTD; 3105; -.
DR   DisGeNET; 3105; -.
DR   GeneCards; HLA-A; -.
DR   HGNC; HGNC:4931; HLA-A.
DR   HPA; ENSG00000206503; Low tissue specificity.
DR   MalaCards; HLA-A; -.
DR   MIM; 126200; phenotype.
DR   MIM; 142800; gene.
DR   MIM; 222100; phenotype.
DR   neXtProt; NX_P04439; -.
DR   OpenTargets; ENSG00000206503; -.
DR   Orphanet; 179; Birdshot chorioretinopathy.
DR   Orphanet; 414750; Prediction of phenytoin or carbamazepine toxicity.
DR   Orphanet; 619246; Selection of immunotherapy in solid cancer.
DR   PharmGKB; PA35055; -.
DR   VEuPathDB; HostDB:ENSG00000206503; -.
DR   eggNOG; ENOG502RQEK; Eukaryota.
DR   GeneTree; ENSGT00980000198488; -.
DR   OMA; TPPKTHM; -.
DR   OrthoDB; 1390181at2759; -.
DR   PhylomeDB; P04439; -.
DR   TreeFam; TF336617; -.
DR   PathwayCommons; P04439; -.
DR   Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR   Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
DR   Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR   Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR   Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR   SignaLink; P04439; -.
DR   BioGRID-ORCS; 3105; 27 hits in 1003 CRISPR screens.
DR   ChiTaRS; HLA-A; human.
DR   GeneWiki; HLA-A; -.
DR   GenomeRNAi; 3105; -.
DR   Pharos; P04439; Tbio.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000206503; Expressed in blood and 102 other tissues.
DR   ExpressionAtlas; P04439; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0042824; C:MHC class I peptide loading complex; IDA:UniProtKB.
DR   GO; GO:0042612; C:MHC class I protein complex; IDA:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
DR   GO; GO:0030881; F:beta-2-microglobulin binding; IDA:UniProtKB.
DR   GO; GO:0042610; F:CD8 receptor binding; IDA:UniProtKB.
DR   GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR   GO; GO:0042608; F:T cell receptor binding; IDA:UniProtKB.
DR   GO; GO:0046977; F:TAP binding; IDA:UniProtKB.
DR   GO; GO:0062061; F:TAP complex binding; IDA:UniProtKB.
DR   GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR   GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IDA:UniProtKB.
DR   GO; GO:0002485; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent; IMP:UniProtKB.
DR   GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IDA:UniProtKB.
DR   GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IDA:UniProtKB.
DR   GO; GO:0036037; P:CD8-positive, alpha-beta T cell activation; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB.
DR   GO; GO:0006955; P:immune response; IMP:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:2001187; P:positive regulation of CD8-positive, alpha-beta T cell activation; IDA:BHF-UCL.
DR   GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; IDA:UniProtKB.
DR   GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
DR   GO; GO:2000568; P:positive regulation of memory T cell activation; IDA:UniProtKB.
DR   GO; GO:0002726; P:positive regulation of T cell cytokine production; IDA:BHF-UCL.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:UniProtKB.
DR   GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR   GO; GO:0001913; P:T cell mediated cytotoxicity; IDA:UniProtKB.
DR   GO; GO:0002419; P:T cell mediated cytotoxicity directed against tumor cell target; IDA:UniProtKB.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.500.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR011161; MHC_I-like_Ag-recog.
DR   InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   InterPro; IPR001039; MHC_I_a_a1/a2.
DR   InterPro; IPR010579; MHC_I_a_C.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00129; MHC_I; 1.
DR   Pfam; PF06623; MHC_I_C; 1.
DR   PRINTS; PR01638; MHCCLASSI.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF54452; SSF54452; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Host-virus interaction; Immunity; Immunoglobulin domain;
KW   Innate immunity; Membrane; MHC I; Phosphoprotein; Reference proteome;
KW   Signal; Sulfation; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:92029"
FT   CHAIN           25..365
FT                   /note="HLA class I histocompatibility antigen, A alpha
FT                   chain"
FT                   /id="PRO_0000018815"
FT   TOPO_DOM        25..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          209..295
FT                   /note="Ig-like C1-type"
FT                   /evidence="ECO:0000255"
FT   REGION          25..114
FT                   /note="Alpha-1"
FT                   /evidence="ECO:0000255"
FT   REGION          115..206
FT                   /note="Alpha-2"
FT                   /evidence="ECO:0000255"
FT   REGION          207..298
FT                   /note="Alpha-3"
FT                   /evidence="ECO:0000255"
FT   REGION          299..308
FT                   /note="Connecting peptide"
FT                   /evidence="ECO:0000255"
FT   REGION          339..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         31
FT                   /ligand="a peptide antigen"
FT                   /ligand_id="ChEBI:CHEBI:166823"
FT                   /ligand_label="1"
FT                   /ligand_note="pathogen-derived peptide antigen"
FT                   /evidence="ECO:0000269|PubMed:21943705"
FT   BINDING         97
FT                   /ligand="a peptide antigen"
FT                   /ligand_id="ChEBI:CHEBI:166823"
FT                   /ligand_label="1"
FT                   /ligand_note="pathogen-derived peptide antigen"
FT                   /evidence="ECO:0000269|PubMed:21943705"
FT   BINDING         108
FT                   /ligand="a peptide antigen"
FT                   /ligand_id="ChEBI:CHEBI:166823"
FT                   /ligand_label="1"
FT                   /ligand_note="pathogen-derived peptide antigen"
FT                   /evidence="ECO:0000269|PubMed:21943705"
FT   BINDING         140
FT                   /ligand="a peptide antigen"
FT                   /ligand_id="ChEBI:CHEBI:166823"
FT                   /ligand_label="2"
FT                   /ligand_note="self-peptide antigen"
FT                   /evidence="ECO:0000269|PubMed:21543847"
FT   BINDING         167
FT                   /ligand="a peptide antigen"
FT                   /ligand_id="ChEBI:CHEBI:166823"
FT                   /ligand_label="1"
FT                   /ligand_note="pathogen-derived peptide antigen"
FT                   /evidence="ECO:0000269|PubMed:21943705"
FT   BINDING         170
FT                   /ligand="a peptide antigen"
FT                   /ligand_id="ChEBI:CHEBI:166823"
FT                   /ligand_label="1"
FT                   /ligand_note="pathogen-derived peptide antigen"
FT                   /evidence="ECO:0000269|PubMed:21943705"
FT   BINDING         183
FT                   /ligand="a peptide antigen"
FT                   /ligand_id="ChEBI:CHEBI:166823"
FT                   /ligand_label="1"
FT                   /ligand_note="pathogen-derived peptide antigen"
FT                   /evidence="ECO:0000269|PubMed:21943705"
FT   BINDING         183
FT                   /ligand="a peptide antigen"
FT                   /ligand_id="ChEBI:CHEBI:166823"
FT                   /ligand_label="2"
FT                   /ligand_note="self-peptide antigen"
FT                   /evidence="ECO:0000269|PubMed:21543847"
FT   BINDING         195
FT                   /ligand="a peptide antigen"
FT                   /ligand_id="ChEBI:CHEBI:166823"
FT                   /ligand_label="1"
FT                   /ligand_note="pathogen-derived peptide antigen"
FT                   /evidence="ECO:0000269|PubMed:21943705"
FT   MOD_RES         83
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         344
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   DISULFID        125..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:16041067, ECO:0000269|PubMed:19177349,
FT                   ECO:0000269|PubMed:20844028, ECO:0000269|PubMed:21543847,
FT                   ECO:0000269|PubMed:21943705, ECO:0000269|PubMed:26758806,
FT                   ECO:0000269|PubMed:28250417, ECO:0000269|PubMed:7694806"
FT   DISULFID        227..283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:16041067, ECO:0000269|PubMed:19177349,
FT                   ECO:0000269|PubMed:20844028, ECO:0000269|PubMed:21543847,
FT                   ECO:0000269|PubMed:21943705, ECO:0000269|PubMed:26758806,
FT                   ECO:0000269|PubMed:28250417, ECO:0000269|PubMed:7694806"
FT   VAR_SEQ         176..187
FT                   /note="EAEQLRAYLDGT -> AAEQQRAYLEGR (in isoform 2)"
FT                   /id="VSP_060391"
FT   VAR_SEQ         337
FT                   /note="S -> SGGEGVK (in isoform 2)"
FT                   /id="VSP_060392"
FT   VARIANT         3
FT                   /note="V -> I (in allele A*34:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115"
FT                   /id="VAR_082315"
FT   VARIANT         5
FT                   /note="A -> P (in allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082316"
FT   VARIANT         10
FT                   /note="L -> V (in allele A*02:01, allele A*02:05, allele
FT                   A*23:01, allele A*24:02, allele A*25:01, allele A*26:01,
FT                   allele A*34:01, allele A*43:01, allele A*66:01, allele
FT                   A*68:01 and allele A*69:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:1729171, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082317"
FT   VARIANT         14
FT                   /note="S -> L (in allele A*29:02, allele A*31:01, allele
FT                   A*32:01, allele A*33:01 and allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|Ref.29"
FT                   /id="VAR_082318"
FT   VARIANT         23
FT                   /note="W -> R (in allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115"
FT                   /id="VAR_082319"
FT   VARIANT         33
FT                   /note="F -> S (in allele A*23:01, allele A*24:02 and allele
FT                   A*30:01; dbSNP:rs2075684)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:7871528,
FT                   ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082320"
FT   VARIANT         33
FT                   /note="F -> T (in allele A*29:02, allele A*31:01 and allele
FT                   A*33:01; requires 2 nucleotide substitutions)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:8795145"
FT                   /id="VAR_082321"
FT   VARIANT         33
FT                   /note="F -> Y (in allele A*02:05, allele A*11:01, allele
FT                   A*25:01, allele A*26:01, allele A*34:01, allele A*43:01,
FT                   allele A*66:01, allele A*68:01 and allele A*69:01;
FT                   dbSNP:rs2075684)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2437024,
FT                   ECO:0000269|PubMed:2460344, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:8016845,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8475492"
FT                   /id="VAR_082322"
FT   VARIANT         41
FT                   /note="R -> S (in allele A*30:01; dbSNP:rs1059423)"
FT                   /evidence="ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:7871528"
FT                   /id="VAR_082323"
FT   VARIANT         55
FT                   /note="T -> S (in allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082324"
FT   VARIANT         59
FT                   /note="R -> Q (in allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082325"
FT   VARIANT         67
FT                   /note="Q -> R (in allele A*02:05; dbSNP:rs41559117)"
FT                   /evidence="ECO:0000269|PubMed:3496393"
FT                   /id="VAR_082326"
FT   VARIANT         68
FT                   /note="R -> K (in alleles A*01:01 and allele A*36:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082327"
FT   VARIANT         80
FT                   /note="G -> E (in allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082328"
FT   VARIANT         80
FT                   /note="G -> R (in allele A*30:01 and allele A*31:01;
FT                   dbSNP:rs1059449)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:7871528,
FT                   ECO:0000269|PubMed:8795145"
FT                   /id="VAR_082329"
FT   VARIANT         86
FT                   /note="Q -> E (in allele A*23:01, allele 24:02 and allele
FT                   A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791,
FT                   ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082330"
FT   VARIANT         86
FT                   /note="Q -> G (in allele A*02:01 and allele A*02:05;
FT                   requires 2 nucleotide substitutions)"
FT                   /evidence="ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:7836067"
FT                   /id="VAR_082331"
FT   VARIANT         86
FT                   /note="Q -> L (in alleles A*29:02 and allele A*43:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:1782566"
FT                   /id="VAR_082332"
FT   VARIANT         86
FT                   /note="Q -> R (in allele A*25:01, allele A*26:01, allele
FT                   A*33:01, allele A*34:01, allele A*66:01, allele A*68:01 and
FT                   allele A*69:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492"
FT                   /id="VAR_082333"
FT   VARIANT         87
FT                   /note="E -> N (in alleles A*25:01, allele A*26:01, allele
FT                   A*33:01, allele A*34:01, allele A*66:01, allele A*68:01 and
FT                   allele A*69:01; requires 2 nucleotide substitutions)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492"
FT                   /id="VAR_082334"
FT   VARIANT         87
FT                   /note="E -> Q (in allele A*29:02 and allele A*43:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:1782566"
FT                   /id="VAR_082335"
FT   VARIANT         89
FT                   /note="R -> G (in allele A*23:01 and allele 24:02;
FT                   dbSNP:rs199474430)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082336"
FT   VARIANT         90
FT                   /note="N -> K (in allele A*02:01, allele A*02:05, allele
FT                   A*23:01, allele 24:02 and allele A*34:01;
FT                   dbSNP:rs199474436)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:1729171, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082337"
FT   VARIANT         91
FT                   /note="V -> M (in allele A*01:01 and allele A*36:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082338"
FT   VARIANT         94
FT                   /note="Q -> H (in allele A*01:01, allele A*02:01, allele
FT                   A*02:05, allele A*23:01, allele 24:02, allele A*25:01,
FT                   allele A*26:01, allele A*31:01, allele A*32:01, allele
FT                   A*33:01, allele A*36:01, allele A*43:01, allele A*74:01 and
FT                   allele A*80:01; dbSNP:rs78306866)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:7836067,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616,
FT                   ECO:0000269|PubMed:9349617, ECO:0000269|Ref.29"
FT                   /id="VAR_082339"
FT   VARIANT         97
FT                   /note="T -> I (in allele A*31:01 and allele A*33:01;
FT                   dbSNP:rs199474457)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:8795145"
FT                   /id="VAR_082340"
FT   VARIANT         98
FT                   /note="D -> H (in allele A*02:01 and allele A*02:05)"
FT                   /evidence="ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:7836067"
FT                   /id="VAR_082341"
FT   VARIANT         98
FT                   /note="D -> N (in allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082342"
FT   VARIANT         100
FT                   /note="V -> A (in allele A*01:01, allele A*26:01, allele
FT                   A*29:02, allele A*36:01, allele A*43:01 and allele
FT                   A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2251137,
FT                   ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082343"
FT   VARIANT         100
FT                   /note="V -> E (in allele A*23:01, allele A*24:02, allele
FT                   A*25:01 and allele A*32:01; dbSNP:rs1071742)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:9349616, ECO:0000269|Ref.29"
FT                   /id="VAR_082344"
FT   VARIANT         101
FT                   /note="D -> N (allele A*01:01, allele A*23:01, allele
FT                   A*24:02, allele A*26:01, allele A*29:02, allele A*36:01,
FT                   allele A*43:01 and allele A*80:01; dbSNP:rs1136688)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:1729171, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|PubMed:9349616, ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082345"
FT   VARIANT         101
FT                   /note="D -> S (in allele A*25:01 and allele A*32:01;
FT                   requires 2 nucleotide substitutions)"
FT                   /evidence="ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|Ref.29"
FT                   /id="VAR_082346"
FT   VARIANT         103..107
FT                   /note="GTLRG -> RIALR (in allele A*23:01, allele A*24:02,
FT                   allele A*25:01 and allele A*32:01; Bw4 motif RIALR is
FT                   involved in the recognition of NK cell inhibitory receptor
FT                   KIR3DL1)"
FT                   /evidence="ECO:0000269|PubMed:17182537,
FT                   ECO:0000269|PubMed:1729171, ECO:0000269|PubMed:18502829,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:9349616, ECO:0000269|Ref.29"
FT                   /id="VAR_082347"
FT   VARIANT         114
FT                   /note="A -> D (in allele A*01:01, allele A*11:01, allele
FT                   A*25:01, allele A*26:01, allele A*34:01, allele A*36:01,
FT                   allele A*43:01, allele A*66:01 and allele A*80:01;
FT                   dbSNP:rs1136692)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2437024, ECO:0000269|PubMed:2460344,
FT                   ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:8016845,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082348"
FT   VARIANT         119
FT                   /note="I -> L (in allele A*02:05, allele A*23:01 and allele
FT                   24:02; dbSNP:rs1071743)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082349"
FT   VARIANT         119
FT                   /note="I -> V (in allele A*02:01 and allele A*69:01)"
FT                   /evidence="ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067"
FT                   /id="VAR_082350"
FT   VARIANT         121
FT                   /note="I -> M (in allele A*23:01, allele 24:02, allele
FT                   A*29:02, allele A*31:01, allele A*32:01, allele A*33:01,
FT                   allele A*68:01 and allele A*74:01; dbSNP:rs1136695)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082351"
FT   VARIANT         121
FT                   /note="I -> R (in allele A*02:01, allele A*02:05, allele
FT                   A*25:01, allele A*26:01, allele A*34:01, allele A*43:01,
FT                   allele A*66:01 and allele A*69:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492"
FT                   /id="VAR_082352"
FT   VARIANT         123
FT                   /note="Y -> F (in allele A*23:01, allele 24:02;
FT                   dbSNP:rs1136697)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082353"
FT   VARIANT         129
FT                   /note="S -> P (in allele A*01:01, allele A*11:01, allele
FT                   A*25:01, allele A*26:01, allele A*32:01, allele A*34:01,
FT                   allele A*36:01, allele A*43:01, allele A*66:01 and allele
FT                   A*74:01; dbSNP:rs1136700)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2437024,
FT                   ECO:0000269|PubMed:2460344, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:8016845, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:9349617,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082354"
FT   VARIANT         131
FT                   /note="G -> W (in allele A*02:01, allele A*02:05 and allele
FT                   A*69:01; dbSNP:rs1136702)"
FT                   /evidence="ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067"
FT                   /id="VAR_082355"
FT   VARIANT         133
FT                   /note="F -> L (in allele A*32:01 and allele A*74:01;
FT                   dbSNP:rs1059488)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|Ref.29"
FT                   /id="VAR_082356"
FT   VARIANT         138
FT                   /note="R -> E (in allele A*30:01; requires 2 nucleotide
FT                   substitutions)"
FT                   /evidence="ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:7871528"
FT                   /id="VAR_082357"
FT   VARIANT         138
FT                   /note="R -> H (in allele A*02:01, allele A*02:05, allele
FT                   A*23:01, allele A*24:02, allele A*69:01)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082358"
FT   VARIANT         138
FT                   /note="R -> Q (in allele A*25:01, allele A*26:01, allele
FT                   A*31:01, allele A*32:01, allele A*33:01, allele A*34:01,
FT                   allele A*43:01, allele A*66:01, allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|Ref.29"
FT                   /id="VAR_082359"
FT   VARIANT         140
FT                   /note="D -> H (in allele A*30:01)"
FT                   /evidence="ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:7871528"
FT                   /id="VAR_082360"
FT   VARIANT         140
FT                   /note="D -> Y (in allele A*02:01, allele A*02:05, allele
FT                   A*23:01, allele A*24:02 and allele A*69:01)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082361"
FT   VARIANT         151
FT                   /note="N -> K (in allele A*02:01, allele A*02:05, allele
FT                   A*23:01, allele A*24:02, allele A*68:01 and allele A*69:01;
FT                   dbSNP:rs1059509)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082362"
FT   VARIANT         166
FT                   /note="I -> T (in allele A*02:01, allele A*02:05, allele
FT                   A*68:01 and allele A*69:01; dbSNP:rs1059516)"
FT                   /evidence="ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067"
FT                   /id="VAR_082363"
FT   VARIANT         168
FT                   /note="K -> Q (in allele A*23:01, allele A*25:01, allele
FT                   A*26:01, allele A*29:02, allele A*30:01, allele A*31:01,
FT                   allele A*32:01, allele A*33:01, allele A*34:01, allele
FT                   A*43:01, allele A*66:01 and allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:7871528, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082364"
FT   VARIANT         169
FT                   /note="R -> H (in allele A*02:01, allele A*02:05, allele
FT                   A*68:01 and allele A*69:01; dbSNP:rs1059520)"
FT                   /evidence="ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067"
FT                   /id="VAR_082365"
FT   VARIANT         173
FT                   /note="A -> T (in allele A*25:01, allele A*26:01, allele
FT                   A*34:01, allele A*43:01 and allele A*66:01;
FT                   dbSNP:rs1059526)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492"
FT                   /id="VAR_082366"
FT   VARIANT         174
FT                   /note="A -> V (in allele A*01:01 and allele A*36:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082367"
FT   VARIANT         175
FT                   /note="H -> R (in allele A*23:01, allele A*29:02, allele
FT                   A*30:01, allele A*31:01, allele A*32:01, allele A*33:01,
FT                   allele A*74:01 and allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:7871528,
FT                   ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|Ref.29"
FT                   /id="VAR_082368"
FT   VARIANT         176
FT                   /note="E -> A (in allele A*01:01, allele A*11:01 and allele
FT                   A*36:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2437024,
FT                   ECO:0000269|PubMed:2460344, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:8016845, ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082369"
FT   VARIANT         176
FT                   /note="E -> R (in allele A*80:01; requires 2 nucleotide
FT                   substitutions)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082370"
FT   VARIANT         176
FT                   /note="E -> V (in allele A*02:01, allele A*02:05, allele
FT                   A*23:01, allele A*24:02, allele A*29:02, allele A*31:01,
FT                   allele A*32:01, allele A*33:01, allele A*68:01, allele
FT                   A*69:01 and allele A*74:01; results in inefficient T cell
FT                   recognition of epitopes derived from influenza A virus.;
FT                   dbSNP:rs9256983)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2456340,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8795145,
FT                   ECO:0000269|PubMed:9349616, ECO:0000269|Ref.29"
FT                   /id="VAR_082371"
FT   VARIANT         176
FT                   /note="E -> W (in allele A*30:01; requires 2 nucleotide
FT                   substitutions)"
FT                   /evidence="ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:7871528"
FT                   /id="VAR_082372"
FT   VARIANT         180
FT                   /note="L -> Q (in allele A*11:01 and allele A*24:02)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:2437024, ECO:0000269|PubMed:2460344,
FT                   ECO:0000269|PubMed:8016845, ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082373"
FT   VARIANT         180
FT                   /note="L -> R (in allele A*01:01 and allele A*36:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082374"
FT   VARIANT         180
FT                   /note="L -> W (in allele A*02:05, allele A*25:01, allele
FT                   A*26:01, allele A*34:01, allele A*43:01, allele A*66:01,
FT                   allele A*68:01; dbSNP:rs9260156)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492"
FT                   /id="VAR_082375"
FT   VARIANT         182
FT                   /note="A -> V (in allele A*01:01 and allele A*36:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082376"
FT   VARIANT         185
FT                   /note="D -> E (in allele A*01:01, allele A*02:01, allele
FT                   A*02:05, allele A*11:01, allele A*23:01, allele A*24:02,
FT                   allele A*25:01, allele A*26:01, allele A*29:02, allele
FT                   A*30:01, allele A*31:01, allele A*32:01, allele A*33:01,
FT                   allele A*34:01, allele A*36:01, allele A*43:01, allele
FT                   A*66:01, allele A*68:01, allele A*69:01, allele A*74:01 and
FT                   allele A*80:01; dbSNP:rs1059542)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2251137,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2437024, ECO:0000269|PubMed:2460344,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067,
FT                   ECO:0000269|PubMed:7871528, ECO:0000269|PubMed:8016845,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616,
FT                   ECO:0000269|PubMed:9349617, ECO:0000269|Ref.29"
FT                   /id="VAR_082377"
FT   VARIANT         187
FT                   /note="T -> E (in allele A*80:01; requires 2 nucleotide
FT                   substitutions)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082378"
FT   VARIANT         187
FT                   /note="T -> R (in allele A*01:01, allele A*11:01, allele
FT                   A*25:01, allele A*26:01, allele A*43:01 and allele
FT                   A*66:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2437024, ECO:0000269|PubMed:2460344,
FT                   ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:8016845,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082379"
FT   VARIANT         190
FT                   /note="E -> D (in allele A*01:01, allele A*23:01, allele
FT                   A*24:02 and allele A*80:01; dbSNP:rs879577815)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791,
FT                   ECO:0000269|PubMed:9349616, ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082380"
FT   VARIANT         191
FT                   /note="W -> G (in allele A*01:01, allele A*23:01, allele
FT                   A*24:02 and allele A*80:01; dbSNP:rs3098019)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640,
FT                   ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791,
FT                   ECO:0000269|PubMed:9349616, ECO:0000269|PubMed:9349617"
FT                   /id="VAR_082381"
FT   VARIANT         195
FT                   /note="Y -> H (in allele A*33:01)"
FT                   /evidence="ECO:0000269|PubMed:2478623"
FT                   /id="VAR_082382"
FT   VARIANT         208
FT                   /note="P -> A (in allele A*02:01, allele A*02:05, allele
FT                   A*25:01, allele A*26:01, allele A*29:02, allele A*32:01,
FT                   allele A*34:01, allele A*43:01, allele A*66:01, allele
FT                   A*68:01, allele A*69:01 and allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|Ref.29"
FT                   /id="VAR_082383"
FT   VARIANT         210
FT                   /note="K -> R (in allele A*33:01)"
FT                   /evidence="ECO:0000269|PubMed:2478623"
FT                   /id="VAR_082384"
FT   VARIANT         217
FT                   /note="P -> A (in allele A*02:01, allele A*02:05, allele
FT                   A*25:01, allele A*26:01, allele A*29:02, allele A*31:01,
FT                   allele A*32:01, allele A*33:01, allele A*34:01, allele
FT                   A*43:01, allele A*66:01, allele A*68:01, allele A*69:01,
FT                   allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082385"
FT   VARIANT         218
FT                   /note="I -> V (in allele A*02:01, allele A*02:05, allele
FT                   A*25:01, allele A*26:01, allele A*29:02, allele A*31:01,
FT                   allele A*32:01, allele A*33:01, allele A*34:01, allele
FT                   A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and
FT                   allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082386"
FT   VARIANT         231
FT                   /note="G -> S (in allele A*02:01, allele A*02:05, allele
FT                   A*25:01, allele A*26:01, allele A*29:02, allele A*31:01,
FT                   allele A*32:01, allele A*33:01, allele A*34:01, allele
FT                   A*43:01, allele A*66:01, allele A*68:01, allele A*69:01,
FT                   allele A*74:01 and allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082387"
FT   VARIANT         269
FT                   /note="A -> V (in allele A*68:01; impairs binding to CD8A
FT                   and reduces recognition by antigen-specific CD8-positive T
FT                   cells)"
FT                   /evidence="ECO:0000269|PubMed:2784196,
FT                   ECO:0000269|PubMed:3877632"
FT                   /id="VAR_082388"
FT   VARIANT         270
FT                   /note="A -> S (in allele A*25:01, allele A*26:01, allele
FT                   A*29:02, allele A*31:01, allele A*32:01, allele A*33:01,
FT                   allele A*34:01, allele A*43:01, allele A*66:01 and allele
FT                   A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082389"
FT   VARIANT         277
FT                   /note="E -> K (in allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082390"
FT   VARIANT         277
FT                   /note="E -> Q (in allele A*02:01, allele A*02:05, allele
FT                   A*25:01, allele A*26:01, allele A*29:02, allele A*31:01,
FT                   allele A*32:01, allele A*33:01, allele A*34:01, allele
FT                   A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and
FT                   allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082391"
FT   VARIANT         279
FT                   /note="Q -> K (in allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082392"
FT   VARIANT         292
FT                   /note="K -> E (in allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082393"
FT   VARIANT         300
FT                   /note="L -> P (in allele A*02:01, allele A*02:05, allele
FT                   A*23:01, allele A*24:02, allele A*25:01, allele A*26:01,
FT                   allele A*29:02, allele A*31:01, allele A*32:01, allele
FT                   A*33:01, allele A*34:01, allele A*43:01, allele A*66:01,
FT                   allele A*68:01, allele A*69:01, allele A*74:01 and allele
FT                   A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082394"
FT   VARIANT         306
FT                   /note="I -> V (in allele A*23:01 and allele A*24:02)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082395"
FT   VARIANT         307
FT                   /note="P -> H (in allele A*23:01)"
FT                   /evidence="ECO:0000269|PubMed:1729171"
FT                   /id="VAR_082396"
FT   VARIANT         312
FT                   /note="I -> L (in allele A*34:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115"
FT                   /id="VAR_082397"
FT   VARIANT         318
FT                   /note="L -> F (in allele A*02:01, allele A*02:05, allele
FT                   A*25:01, allele A*26:01, allele A*29:02, allele A*31:01,
FT                   allele A*32:01, allele A*33:01, allele A*34:01, allele
FT                   A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and
FT                   allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951,
FT                   ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632,
FT                   ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082398"
FT   VARIANT         321
FT                   /note="V -> M (in allele A*32:01 and allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1431115,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|Ref.29"
FT                   /id="VAR_082399"
FT   VARIANT         322
FT                   /note="I -> F (in allele A*29:02, allele A*31:01, allele
FT                   A*32:01, allele A*33:01 and allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|Ref.29"
FT                   /id="VAR_082400"
FT   VARIANT         323
FT                   /note="T -> A (in allele A*25:01, allele A*26:01, allele
FT                   A*29:02, allele A*31:01, allele A*32:01, allele A*33:01,
FT                   allele A*34:01, allele A*43:01, allele A*66:01, allele
FT                   A*74:01 and allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082401"
FT   VARIANT         331
FT                   /note="M -> R (in allele A*29:02, allele A*31:01, allele
FT                   A*32:01, allele A*33:01 and allele A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|Ref.29"
FT                   /id="VAR_082402"
FT   VARIANT         334
FT                   /note="R -> K (allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082403"
FT   VARIANT         335
FT                   /note="K -> N (in allele A*23:01 and allele A*24:02)"
FT                   /evidence="ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:9349616"
FT                   /id="VAR_082404"
FT   VARIANT         338
FT                   /note="D -> V (allele A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791"
FT                   /id="VAR_082405"
FT   VARIANT         345
FT                   /note="T -> S (in allele A*02:01, allele A*02:05, allele
FT                   A*23:01, allele A*24:02, allele A*25:01, allele A*26:01,
FT                   allele A*29:02, allele A*31:01, allele A*32:01, allele
FT                   A*33:01, allele A*34:01, allele A*43:01, allele A*66:01,
FT                   allele A*68:01 allele A*69:01, allele A*74:01 and allele
FT                   A*80:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171,
FT                   ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591,
FT                   ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623,
FT                   ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393,
FT                   ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067,
FT                   ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325,
FT                   ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492,
FT                   ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082406"
FT   VARIANT         358
FT                   /note="V -> M (in allele A*25:01, allele A*26:01, allele
FT                   A*29:02, allele A*31:01, allele A*32:01, allele A*33:01,
FT                   allele A*34:01, allele A*43:01, allele A*66:01 and allele
FT                   A*74:01)"
FT                   /evidence="ECO:0000269|PubMed:1317015,
FT                   ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566,
FT                   ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040,
FT                   ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:8026990,
FT                   ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145,
FT                   ECO:0000269|Ref.29"
FT                   /id="VAR_082407"
FT   MUTAGEN         110
FT                   /note="N->Q: Impairs the recruitment of HLA-A*02 in the
FT                   peptide-loading complex."
FT                   /evidence="ECO:0000269|PubMed:21263072"
FT   MUTAGEN         156
FT                   /note="S->C: Impairs the maturation of a peptide-receptive
FT                   HLA-A*02-B2M complex."
FT                   /evidence="ECO:0000269|PubMed:8805302"
FT   MUTAGEN         158
FT                   /note="T->K: Impairs binding to TAP1-TAP2 transporter,
FT                   resulting in impaired presentation of intracellular
FT                   peptides."
FT                   /evidence="ECO:0000269|PubMed:8630735,
FT                   ECO:0000269|PubMed:8805302"
FT   STRAND          27..36
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          45..52
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:4F7T"
FT   HELIX           74..78
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   HELIX           81..108
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:3D25"
FT   STRAND          118..127
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          131..142
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          145..150
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:6EWA"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   HELIX           162..173
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   HELIX           176..184
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   HELIX           187..198
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          210..235
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          238..243
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          246..248
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   HELIX           249..251
FT                   /evidence="ECO:0007829|PDB:2GTW"
FT   STRAND          252..254
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          265..274
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:4JFD"
FT   HELIX           278..280
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          281..286
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          290..292
FT                   /evidence="ECO:0007829|PDB:2V2X"
FT   STRAND          294..297
FT                   /evidence="ECO:0007829|PDB:3MRE"
FT   STRAND          348..350
FT                   /evidence="ECO:0007829|PDB:4EN2"
SQ   SEQUENCE   365 AA;  40841 MW;  DEDFCEC4450E0580 CRC64;
     MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF
     DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ
     IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHEAEQL
     RAYLDGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT
     WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL
     SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL
     TACKV
//
