ID   TUSC3_HUMAN             Reviewed;         348 AA.
AC   Q13454; A8MSM0; D3DSP2; Q14911; Q14912; Q96FW0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   12-OCT-2022, entry version 184.
DE   RecName: Full=Tumor suppressor candidate 3;
DE   AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3;
DE            Short=Oligosaccharyl transferase subunit TUSC3;
DE   AltName: Full=Magnesium uptake/transporter TUSC3;
DE   AltName: Full=Protein N33;
DE   Flags: Precursor;
GN   Name=TUSC3; Synonyms=N33;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=8661104; DOI=10.1006/geno.1996.0322;
RA   Macgrogan D., Levy A., Bova G.S., Isaacs W.B., Bookstein R.;
RT   "Structure and methylation-associated silencing of a gene within a
RT   homozygously deleted region of human chromosome band 8p22.";
RL   Genomics 35:55-65(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Skin;
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   [6]
RP   IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=12887896; DOI=10.1016/s1097-2765(03)00243-0;
RA   Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
RT   "Oligosaccharyltransferase isoforms that contain different catalytic STT3
RT   subunits have distinct enzymatic properties.";
RL   Mol. Cell 12:101-111(2003).
RN   [7]
RP   INVOLVEMENT IN MRT7.
RX   PubMed=18455129; DOI=10.1016/j.ajhg.2008.03.021;
RA   Molinari F., Foulquier F., Tarpey P.S., Morelle W., Boissel S., Teague J.,
RA   Edkins S., Futreal P.A., Stratton M.R., Turner G., Matthijs G., Gecz J.,
RA   Munnich A., Colleaux L.;
RT   "Oligosaccharyltransferase-subunit mutations in nonsyndromic mental
RT   retardation.";
RL   Am. J. Hum. Genet. 82:1150-1157(2008).
RN   [8]
RP   INVOLVEMENT IN MRT7.
RX   PubMed=18452889; DOI=10.1016/j.ajhg.2008.03.018;
RA   Garshasbi M., Hadavi V., Habibi H., Kahrizi K., Kariminejad R., Behjati F.,
RA   Tzschach A., Najmabadi H., Ropers H.H., Kuss A.W.;
RT   "A defect in the TUSC3 gene is associated with autosomal recessive mental
RT   retardation.";
RL   Am. J. Hum. Genet. 82:1158-1164(2008).
RN   [9]
RP   FUNCTION IN MAGNESIUM UPTAKE.
RX   PubMed=19717468; DOI=10.1073/pnas.0908332106;
RA   Zhou H., Clapham D.E.;
RT   "Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and
RT   vertebrate embryonic development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15750-15755(2009).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF CYS-99 AND CYS-102.
RX   PubMed=25135935; DOI=10.1083/jcb.201404083;
RA   Cherepanova N.A., Shrimal S., Gilmore R.;
RT   "Oxidoreductase activity is necessary for N-glycosylation of cysteine-
RT   proximal acceptor sites in glycoproteins.";
RL   J. Cell Biol. 206:525-539(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 44-194, DISULFIDE BOND, PROPOSED
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=24685145; DOI=10.1016/j.str.2014.02.013;
RA   Mohorko E., Owen R.L., Malojcic G., Brozzo M.S., Aebi M., Glockshuber R.;
RT   "Structural basis of substrate specificity of human oligosaccharyl
RT   transferase subunit N33/Tusc3 and its role in regulating protein N-
RT   glycosylation.";
RL   Structure 22:590-601(2014).
RN   [12]
RP   VARIANT VAL-247.
RX   PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA   de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA   Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA   del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA   Veltman J.A., Vissers L.E.;
RT   "Diagnostic exome sequencing in persons with severe intellectual
RT   disability.";
RL   N. Engl. J. Med. 367:1921-1929(2012).
CC   -!- FUNCTION: Acts as accessory component of the N-oligosaccharyl
CC       transferase (OST) complex which catalyzes the transfer of a high
CC       mannose oligosaccharide from a lipid-linked oligosaccharide donor to an
CC       asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent
CC       polypeptide chains. Involved in N-glycosylation of STT3B-dependent
CC       substrates. Specifically required for the glycosylation of a subset of
CC       acceptor sites that are near cysteine residues; in this function seems
CC       to act redundantly with MAGT1. In its oxidized form proposed to form
CC       transient mixed disulfides with a glycoprotein substrate to facilitate
CC       access of STT3B to the unmodified acceptor site. Has also
CC       oxidoreductase-independent functions in the STT3B-containing OST
CC       complex possibly involving substrate recognition.
CC       {ECO:0000269|PubMed:25135935, ECO:0000305|PubMed:12887896,
CC       ECO:0000305|PubMed:24685145}.
CC   -!- FUNCTION: Magnesium transporter. {ECO:0000269|PubMed:19717468}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Accessory component of the STT3B-containing form of the
CC       oligosaccharyltransferase (OST) complex. OST exists in two different
CC       complex forms which contain common core subunits RPN1, RPN2, OST48,
CC       OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits,
CC       and form-specific accessory subunits. OST can form stable complexes
CC       with the Sec61 complex or with both the Sec61 and TRAP complexes. The
CC       association of TUSC3 or MAGT1 with the STT3B-containing complex seems
CC       to be mutually exclusvice. {ECO:0000305|PubMed:12887896,
CC       ECO:0000305|PubMed:24685145}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q13454-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13454-2; Sequence=VSP_003776;
CC   -!- TISSUE SPECIFICITY: Expressed in most non-lymphoid cells and tissues
CC       examined, including prostate, lung, liver, colon, heart, kidney and
CC       pancreas. {ECO:0000269|PubMed:12887896}.
CC   -!- DISEASE: Intellectual developmental disorder, autosomal recessive 7
CC       (MRT7) [MIM:611093]: A disorder characterized by significantly below
CC       average general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period.
CC       {ECO:0000269|PubMed:18452889, ECO:0000269|PubMed:18455129}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U42349; AAB18374.1; -; mRNA.
DR   EMBL; U42359; AAB18375.1; -; Genomic_DNA.
DR   EMBL; U42350; AAB18375.1; JOINED; Genomic_DNA.
DR   EMBL; U42351; AAB18375.1; JOINED; Genomic_DNA.
DR   EMBL; U42352; AAB18375.1; JOINED; Genomic_DNA.
DR   EMBL; U42354; AAB18375.1; JOINED; Genomic_DNA.
DR   EMBL; U42355; AAB18375.1; JOINED; Genomic_DNA.
DR   EMBL; U42356; AAB18375.1; JOINED; Genomic_DNA.
DR   EMBL; U42357; AAB18375.1; JOINED; Genomic_DNA.
DR   EMBL; U42358; AAB18375.1; JOINED; Genomic_DNA.
DR   EMBL; U42360; AAB18376.1; -; Genomic_DNA.
DR   EMBL; U42350; AAB18376.1; JOINED; Genomic_DNA.
DR   EMBL; U42351; AAB18376.1; JOINED; Genomic_DNA.
DR   EMBL; U42352; AAB18376.1; JOINED; Genomic_DNA.
DR   EMBL; U42354; AAB18376.1; JOINED; Genomic_DNA.
DR   EMBL; U42355; AAB18376.1; JOINED; Genomic_DNA.
DR   EMBL; U42356; AAB18376.1; JOINED; Genomic_DNA.
DR   EMBL; U42357; AAB18376.1; JOINED; Genomic_DNA.
DR   EMBL; U42358; AAB18376.1; JOINED; Genomic_DNA.
DR   EMBL; BT020002; AAV38805.1; -; mRNA.
DR   EMBL; AC010656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC019292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC091559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC100850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471080; EAW63837.1; -; Genomic_DNA.
DR   EMBL; CH471080; EAW63839.1; -; Genomic_DNA.
DR   EMBL; BC010370; AAH10370.1; -; mRNA.
DR   CCDS; CCDS5993.1; -. [Q13454-2]
DR   CCDS; CCDS5994.1; -. [Q13454-1]
DR   PIR; G02297; G02297.
DR   RefSeq; NP_006756.2; NM_006765.3. [Q13454-1]
DR   RefSeq; NP_839952.1; NM_178234.2. [Q13454-2]
DR   PDB; 4M8G; X-ray; 2.00 A; A/B=44-194.
DR   PDB; 4M90; X-ray; 1.60 A; A=44-194.
DR   PDB; 4M91; X-ray; 1.10 A; A=44-194.
DR   PDB; 4M92; X-ray; 1.60 A; A=44-194.
DR   PDBsum; 4M8G; -.
DR   PDBsum; 4M90; -.
DR   PDBsum; 4M91; -.
DR   PDBsum; 4M92; -.
DR   AlphaFoldDB; Q13454; -.
DR   SMR; Q13454; -.
DR   BioGRID; 113701; 64.
DR   CORUM; Q13454; -.
DR   IntAct; Q13454; 21.
DR   MINT; Q13454; -.
DR   STRING; 9606.ENSP00000424544; -.
DR   TCDB; 1.A.76.1.2; the magnesium transporter1 (magt1) family.
DR   TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR   iPTMnet; Q13454; -.
DR   PhosphoSitePlus; Q13454; -.
DR   BioMuta; TUSC3; -.
DR   DMDM; 6166601; -.
DR   EPD; Q13454; -.
DR   jPOST; Q13454; -.
DR   MassIVE; Q13454; -.
DR   MaxQB; Q13454; -.
DR   PaxDb; Q13454; -.
DR   PeptideAtlas; Q13454; -.
DR   PRIDE; Q13454; -.
DR   ProteomicsDB; 59456; -. [Q13454-1]
DR   ProteomicsDB; 59457; -. [Q13454-2]
DR   Antibodypedia; 22197; 183 antibodies from 28 providers.
DR   DNASU; 7991; -.
DR   Ensembl; ENST00000382020.8; ENSP00000371450.4; ENSG00000104723.21. [Q13454-2]
DR   Ensembl; ENST00000503731.6; ENSP00000424544.1; ENSG00000104723.21. [Q13454-1]
DR   GeneID; 7991; -.
DR   KEGG; hsa:7991; -.
DR   MANE-Select; ENST00000503731.6; ENSP00000424544.1; NM_006765.4; NP_006756.2.
DR   UCSC; uc003wwt.4; human. [Q13454-1]
DR   CTD; 7991; -.
DR   DisGeNET; 7991; -.
DR   GeneCards; TUSC3; -.
DR   GeneReviews; TUSC3; -.
DR   HGNC; HGNC:30242; TUSC3.
DR   HPA; ENSG00000104723; Low tissue specificity.
DR   MalaCards; TUSC3; -.
DR   MIM; 601385; gene.
DR   MIM; 611093; phenotype.
DR   neXtProt; NX_Q13454; -.
DR   OpenTargets; ENSG00000104723; -.
DR   Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR   PharmGKB; PA128394537; -.
DR   VEuPathDB; HostDB:ENSG00000104723; -.
DR   eggNOG; KOG2603; Eukaryota.
DR   GeneTree; ENSGT00390000012030; -.
DR   InParanoid; Q13454; -.
DR   OMA; NLWAAVS; -.
DR   OrthoDB; 1460433at2759; -.
DR   PhylomeDB; Q13454; -.
DR   TreeFam; TF314850; -.
DR   PathwayCommons; Q13454; -.
DR   Reactome; R-HSA-446203; Asparagine N-linked glycosylation.
DR   Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR   Reactome; R-HSA-9694548; Maturation of spike protein.
DR   SignaLink; Q13454; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 7991; 106 hits in 1077 CRISPR screens.
DR   ChiTaRS; TUSC3; human.
DR   GeneWiki; TUSC3; -.
DR   GenomeRNAi; 7991; -.
DR   Pharos; Q13454; Tbio.
DR   PRO; PR:Q13454; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q13454; protein.
DR   Bgee; ENSG00000104723; Expressed in type B pancreatic cell and 185 other tissues.
DR   ExpressionAtlas; Q13454; baseline and differential.
DR   Genevisible; Q13454; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:HGNC-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR   GO; GO:0015693; P:magnesium ion transport; IMP:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; NAS:UniProtKB.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12692; PTHR12692; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disulfide bond; Endoplasmic reticulum;
KW   Intellectual disability; Magnesium; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..348
FT                   /note="Tumor suppressor candidate 3"
FT                   /id="PRO_0000215300"
FT   TOPO_DOM        42..196
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..276
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..312
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..348
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          59..187
FT                   /note="Thioredoxin"
FT   DISULFID        99..102
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000269|PubMed:24685145,
FT                   ECO:0007744|PDB:4M8G, ECO:0007744|PDB:4M90"
FT   VAR_SEQ         344..348
FT                   /note="DLDFE -> FLIK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:8661104"
FT                   /id="VSP_003776"
FT   VARIANT         65
FT                   /note="I -> V (in dbSNP:rs11545035)"
FT                   /id="VAR_045836"
FT   VARIANT         247
FT                   /note="M -> V"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069369"
FT   MUTAGEN         99
FT                   /note="C->S: Reduces N-glycosylation of cysteine-proximal
FT                   acceptor sites; when associated with S-102."
FT                   /evidence="ECO:0000269|PubMed:25135935"
FT   MUTAGEN         102
FT                   /note="C->S: Reduces N-glycosylation of cysteine-proximal
FT                   acceptor sites; when associated with S-99."
FT                   /evidence="ECO:0000269|PubMed:25135935"
FT   HELIX           44..62
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   HELIX           70..76
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   STRAND          84..91
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   HELIX           100..118
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   HELIX           137..142
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:4M91"
FT   HELIX           175..186
FT                   /evidence="ECO:0007829|PDB:4M91"
SQ   SEQUENCE   348 AA;  39676 MW;  16D97CB1E00C5190 CRC64;
     MGARGAPSRR RQAGRRLRYL PTGSFPFLLL LLLLCIQLGG GQKKKENLLA EKVEQLMEWS
     SRRSIFRMNG DKFRKFIKAP PRNYSMIVMF TALQPQRQCS VCRQANEEYQ ILANSWRYSS
     AFCNKLFFSM VDYDEGTDVF QQLNMNSAPT FMHFPPKGRP KRADTFDLQR IGFAAEQLAK
     WIADRTDVHI RVFRPPNYSG TIALALLVSL VGGLLYLRRN NLEFIYNKTG WAMVSLCIVF
     AMTSGQMWNH IRGPPYAHKN PHNGQVSYIH GSSQAQFVAE SHIILVLNAA ITMGMVLLNE
     AATSKGDVGK RRIICLVGLG LVVFFFSFLL SIFRSKYHGY PYSDLDFE
//
