ID   CLD1_HUMAN              Reviewed;         211 AA.
AC   O95832;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   12-OCT-2022, entry version 186.
DE   RecName: Full=Claudin-1;
DE   AltName: Full=Senescence-associated epithelial membrane protein;
GN   Name=CLDN1; Synonyms=CLD1, SEMP1; ORFNames=UNQ481/PRO944;
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 [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=9931503; DOI=10.1016/s0378-1119(98)00553-8;
RA   Swisshelm K.L., Machl A., Planitzer S., Robertson R., Kubbies M.,
RA   Hosier S.;
RT   "SEMP1, a senescence-associated cDNA isolated from human mammary epithelial
RT   cells, is a member of an epithelial membrane protein superfamily.";
RL   Gene 226:285-295(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mitic L.M., Anderson J.M.;
RT   "Human claudin-1 isolated from Caco-2 mRNA.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10828592; DOI=10.1159/000015553;
RA   Halford S., Spencer P., Greenwood J., Winton H., Hunt D.M., Adamson P.;
RT   "Assignment of claudin-1 (CLDN1) to human chromosome 3q28-->q29 with
RT   somatic cell hybrids.";
RL   Cytogenet. Cell Genet. 88:217-217(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11071387; DOI=10.1007/s004390000375;
RA   Kraemer F., White K., Kubbies M., Swisshelm K.L., Weber B.H.F.;
RT   "Genomic organization of claudin-1 and its assessment in hereditary and
RT   sporadic breast cancer.";
RL   Hum. Genet. 107:249-256(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Urinary bladder;
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   [8]
RP   INVOLVEMENT IN NISCH.
RX   PubMed=15521008; DOI=10.1053/j.gastro.2004.07.022;
RA   Hadj-Rabia S., Baala L., Vabres P., Hamel-Teillac D., Jacquemin E.,
RA   Fabre M., Lyonnet S., De Prost Y., Munnich A., Hadchouel M., Smahi A.;
RT   "Claudin-1 gene mutations in neonatal sclerosing cholangitis associated
RT   with ichthyosis: a tight junction disease.";
RL   Gastroenterology 127:1386-1390(2004).
RN   [9]
RP   INVOLVEMENT IN NISCH.
RX   PubMed=16619213; DOI=10.1002/humu.20333;
RA   Feldmeyer L., Huber M., Fellmann F., Beckmann J.S., Frenk E., Hohl D.;
RT   "Confirmation of the origin of NISCH syndrome.";
RL   Hum. Mutat. 27:408-410(2006).
RN   [10]
RP   FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF ILE-32 AND GLU-48.
RX   PubMed=17325668; DOI=10.1038/nature05654;
RA   Evans M.J., von Hahn T., Tscherne D.M., Syder A.J., Panis M., Wolk B.,
RA   Hatziioannou T., McKeating J.A., Bieniasz P.D., Rice C.M.;
RT   "Claudin-1 is a hepatitis C virus co-receptor required for a late step in
RT   entry.";
RL   Nature 446:801-805(2007).
RN   [11]
RP   FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, INTERACTION WITH
RP   OCLN; CD81; CLDN4; CLDN6 AND CLDN9, AND MUTAGENESIS OF ILE-32 AND GLU-48.
RX   PubMed=20375010; DOI=10.1074/jbc.m110.104836;
RA   Harris H.J., Davis C., Mullins J.G., Hu K., Goodall M., Farquhar M.J.,
RA   Mee C.J., McCaffrey K., Young S., Drummer H., Balfe P., McKeating J.A.;
RT   "Claudin association with CD81 defines hepatitis C virus entry.";
RL   J. Biol. Chem. 285:21092-21102(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   INTERACTION WITH CD81.
RX   PubMed=21516087; DOI=10.1038/nm.2341;
RA   Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L.,
RA   Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B., Zahid M.N.,
RA   Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M., Pietschmann T.,
RA   Patel A.H., Pessaux P., Doffoel M., Raffelsberger W., Poch O.,
RA   McKeating J.A., Brino L., Baumert T.F.;
RT   "EGFR and EphA2 are host factors for hepatitis C virus entry and possible
RT   targets for antiviral therapy.";
RL   Nat. Med. 17:589-595(2011).
RN   [14]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23407391; DOI=10.1038/jid.2012.507;
RA   Kirschner N., Rosenthal R., Furuse M., Moll I., Fromm M., Brandner J.M.;
RT   "Contribution of tight junction proteins to ion, macromolecule, and water
RT   barrier in keratinocytes.";
RL   J. Invest. Dermatol. 133:1161-1169(2013).
RN   [15]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH DENGUE VIRUS SMALL
RP   ENVELOPE PROTEIN M.
RX   PubMed=24074594; DOI=10.1016/j.virol.2013.08.009;
RA   Che P., Tang H., Li Q.;
RT   "The interaction between claudin-1 and dengue viral prM/M protein for its
RT   entry.";
RL   Virology 446:303-313(2013).
RN   [16]
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=23704991; DOI=10.1371/journal.pone.0064517;
RA   Bonander N., Jamshad M., Oberthuer D., Clare M., Barwell J., Hu K.,
RA   Farquhar M.J., Stamataki Z., Harris H.J., Dierks K., Dafforn T.R.,
RA   Betzel C., McKeating J.A., Bill R.M.;
RT   "Production, purification and characterization of recombinant, full-length
RT   human claudin-1.";
RL   PLoS ONE 8:E64517-E64517(2013).
RN   [17]
RP   INTERACTION WITH HCV HETERODIMER E1/E2 (MICROBIAL INFECTION), AND FUNCTION
RP   (MICROBIAL INFECTION).
RX   PubMed=24038151; DOI=10.1002/hep.26733;
RA   Douam F., Dao Thi V.L., Maurin G., Fresquet J., Mompelat D., Zeisel M.B.,
RA   Baumert T.F., Cosset F.L., Lavillette D.;
RT   "Critical interaction between E1 and E2 glycoproteins determines binding
RT   and fusion properties of hepatitis C virus during cell entry.";
RL   Hepatology 59:776-788(2014).
CC   -!- FUNCTION: Claudins function as major constituents of the tight junction
CC       complexes that regulate the permeability of epithelia. While some
CC       claudin family members play essential roles in the formation of
CC       impermeable barriers, others mediate the permeability to ions and small
CC       molecules. Often, several claudin family members are coexpressed and
CC       interact with each other, and this determines the overall permeability.
CC       CLDN1 is required to prevent the paracellular diffusion of small
CC       molecules through tight junctions in the epidermis and is required for
CC       the normal barrier function of the skin. Required for normal water
CC       homeostasis and to prevent excessive water loss through the skin,
CC       probably via an indirect effect on the expression levels of other
CC       proteins, since CLDN1 itself seems to be dispensable for water barrier
CC       formation in keratinocyte tight junctions (PubMed:23407391).
CC       {ECO:0000269|PubMed:23407391}.
CC   -!- FUNCTION: (Microbial infection) Acts as a co-receptor for hepatitis C
CC       virus (HCV) in hepatocytes (PubMed:17325668, PubMed:20375010,
CC       PubMed:24038151). Associates with CD81 and the CLDN1-CD81 receptor
CC       complex is essential for HCV entry into host cell (PubMed:20375010).
CC       Acts as a receptor for dengue virus (PubMed:24074594).
CC       {ECO:0000269|PubMed:17325668, ECO:0000269|PubMed:20375010,
CC       ECO:0000269|PubMed:24038151, ECO:0000269|PubMed:24074594}.
CC   -!- SUBUNIT: Homopolymers interact with CLDN3, but not CLDN2, homopolymers.
CC       Can form homo- and heteropolymers with other claudin family members
CC       (PubMed:23704991). Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and
CC       TJP3/ZO-3. Interacts with MPDZ and PATJ (By similarity). Interacts with
CC       OCLN, CLDN4, CLDN6 and CLDN9 (PubMed:20375010). Interacts with CD81
CC       (PubMed:20375010, PubMed:21516087). {ECO:0000250|UniProtKB:O88551,
CC       ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:21516087,
CC       ECO:0000269|PubMed:23704991}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with hepatitis c virus
CC       heterodimer E1/E2. {ECO:0000269|PubMed:24038151}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with dengue virus small
CC       envelope protein M. {ECO:0000269|PubMed:24074594}.
CC   -!- INTERACTION:
CC       O95832; Q07108: CD69; NbExp=3; IntAct=EBI-723889, EBI-2836595;
CC       O95832; P11912: CD79A; NbExp=3; IntAct=EBI-723889, EBI-7797864;
CC       O95832; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-723889, EBI-12142257;
CC       O95832; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-723889, EBI-12806656;
CC       O95832; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-723889, EBI-11724423;
CC       O95832; Q9P0T7: TMEM9; NbExp=3; IntAct=EBI-723889, EBI-723976;
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:23407391}. Cell
CC       membrane {ECO:0000269|PubMed:23704991}; Multi-pass membrane protein
CC       {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:20375010}.
CC       Note=Associates with CD81 and the CLDN1-CD81 complex localizes to the
CC       basolateral cell membrane. {ECO:0000269|PubMed:20375010}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in liver and kidney. Expressed
CC       in heart, brain, spleen, lung and testis. {ECO:0000269|PubMed:9931503}.
CC   -!- DISEASE: Ichthyosis-sclerosing cholangitis neonatal syndrome (NISCH)
CC       [MIM:607626]: A rare autosomal recessive complex ichthyosis syndrome
CC       characterized by scalp hypotrichosis, scarring alopecia, mild diffuse
CC       ichthyosis, sclerosing cholangitis and leukocyte vacuolization.
CC       {ECO:0000269|PubMed:15521008, ECO:0000269|PubMed:16619213}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR   EMBL; AF101051; AAD16433.1; -; mRNA.
DR   EMBL; AF115546; AAD22962.1; -; mRNA.
DR   EMBL; AF134160; AAF61393.1; -; mRNA.
DR   EMBL; AF260406; AAK20945.1; -; Genomic_DNA.
DR   EMBL; AF260403; AAK20945.1; JOINED; Genomic_DNA.
DR   EMBL; AF260404; AAK20945.1; JOINED; Genomic_DNA.
DR   EMBL; AF260405; AAK20945.1; JOINED; Genomic_DNA.
DR   EMBL; AY358652; AAQ89015.1; -; mRNA.
DR   EMBL; CR457138; CAG33419.1; -; mRNA.
DR   EMBL; BC012471; AAH12471.1; -; mRNA.
DR   CCDS; CCDS3295.1; -.
DR   RefSeq; NP_066924.1; NM_021101.4.
DR   AlphaFoldDB; O95832; -.
DR   SMR; O95832; -.
DR   BioGRID; 114533; 23.
DR   CORUM; O95832; -.
DR   IntAct; O95832; 11.
DR   MINT; O95832; -.
DR   STRING; 9606.ENSP00000295522; -.
DR   TCDB; 1.H.1.1.14; the claudin tight junction (claudin1) family.
DR   GlyGen; O95832; 4 sites.
DR   iPTMnet; O95832; -.
DR   PhosphoSitePlus; O95832; -.
DR   SwissPalm; O95832; -.
DR   BioMuta; CLDN1; -.
DR   EPD; O95832; -.
DR   jPOST; O95832; -.
DR   MassIVE; O95832; -.
DR   MaxQB; O95832; -.
DR   PaxDb; O95832; -.
DR   PeptideAtlas; O95832; -.
DR   PRIDE; O95832; -.
DR   ProteomicsDB; 51077; -.
DR   Antibodypedia; 3613; 816 antibodies from 43 providers.
DR   DNASU; 9076; -.
DR   Ensembl; ENST00000295522.4; ENSP00000295522.3; ENSG00000163347.6.
DR   GeneID; 9076; -.
DR   KEGG; hsa:9076; -.
DR   MANE-Select; ENST00000295522.4; ENSP00000295522.3; NM_021101.5; NP_066924.1.
DR   UCSC; uc003fsh.4; human.
DR   CTD; 9076; -.
DR   DisGeNET; 9076; -.
DR   GeneCards; CLDN1; -.
DR   HGNC; HGNC:2032; CLDN1.
DR   HPA; ENSG00000163347; Tissue enhanced (liver, skin).
DR   MalaCards; CLDN1; -.
DR   MIM; 603718; gene.
DR   MIM; 607626; phenotype.
DR   neXtProt; NX_O95832; -.
DR   OpenTargets; ENSG00000163347; -.
DR   Orphanet; 59303; Neonatal ichthyosis-sclerosing cholangitis syndrome.
DR   PharmGKB; PA26557; -.
DR   VEuPathDB; HostDB:ENSG00000163347; -.
DR   eggNOG; ENOG502R7HF; Eukaryota.
DR   GeneTree; ENSGT00940000155387; -.
DR   HOGENOM; CLU_076370_2_3_1; -.
DR   InParanoid; O95832; -.
DR   OMA; CCCPQKA; -.
DR   OrthoDB; 1244077at2759; -.
DR   PhylomeDB; O95832; -.
DR   TreeFam; TF331936; -.
DR   PathwayCommons; O95832; -.
DR   Reactome; R-HSA-420029; Tight junction interactions.
DR   SignaLink; O95832; -.
DR   BioGRID-ORCS; 9076; 15 hits in 1073 CRISPR screens.
DR   ChiTaRS; CLDN1; human.
DR   GeneWiki; CLDN1; -.
DR   GenomeRNAi; 9076; -.
DR   Pharos; O95832; Tbio.
DR   PRO; PR:O95832; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O95832; protein.
DR   Bgee; ENSG00000163347; Expressed in upper leg skin and 139 other tissues.
DR   ExpressionAtlas; O95832; baseline and differential.
DR   Genevisible; O95832; HS.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR   GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0001618; F:virus receptor activity; IMP:UniProtKB.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0034331; P:cell junction maintenance; ISS:ARUK-UCL.
DR   GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR   GO; GO:1903545; P:cellular response to butyrate; IEA:Ensembl.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR   GO; GO:0071284; P:cellular response to lead ion; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0008065; P:establishment of blood-nerve barrier; IEA:Ensembl.
DR   GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
DR   GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
DR   GO; GO:0042538; P:hyperosmotic salinity response; IEA:Ensembl.
DR   GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR   GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR   GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL.
DR   GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IMP:ARUK-UCL.
DR   GO; GO:0090303; P:positive regulation of wound healing; IMP:ARUK-UCL.
DR   GO; GO:0051259; P:protein complex oligomerization; IDA:ARUK-UCL.
DR   GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0070673; P:response to interleukin-18; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0061772; P:xenobiotic transport across blood-nerve barrier; IEA:Ensembl.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR003548; Claudin1.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; PTHR12002; 1.
DR   PANTHER; PTHR12002:SF92; PTHR12002:SF92; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01377; CLAUDIN1.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Disulfide bond;
KW   Host cell receptor for virus entry; Host-virus interaction; Ichthyosis;
KW   Membrane; Receptor; Reference proteome; Tight junction; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..211
FT                   /note="Claudin-1"
FT                   /id="PRO_0000144729"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..81
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..163
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..211
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          192..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..211
FT                   /note="Interactions with TJP1, TJP2, TJP3 and PATJ"
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..64
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         32
FT                   /note="I->M: Loss of HCV receptor activity. Significant
FT                   loss of interaction with CD81. Reduced interaction with
FT                   OCLN."
FT                   /evidence="ECO:0000269|PubMed:17325668,
FT                   ECO:0000269|PubMed:20375010"
FT   MUTAGEN         48
FT                   /note="E->K: Loss of HCV receptor activity. Significant
FT                   loss of interaction with CD81. Reduced interaction with
FT                   OCLN. According to PubMed:17325668 no effect observed on
FT                   HCV infection susceptibility in cell culture."
FT                   /evidence="ECO:0000269|PubMed:17325668,
FT                   ECO:0000269|PubMed:20375010"
FT   CONFLICT        62
FT                   /note="I -> V (in Ref. 2; AAD22962)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="V -> A (in Ref. 2; AAD22962)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   211 AA;  22744 MW;  07269000E6C214F0 CRC64;
     MANAGLQLLG FILAFLGWIG AIVSTALPQW RIYSYAGDNI VTAQAMYEGL WMSCVSQSTG
     QIQCKVFDSL LNLSSTLQAT RALMVVGILL GVIAIFVATV GMKCMKCLED DEVQKMRMAV
     IGGAIFLLAG LAILVATAWY GNRIVQEFYD PMTPVNARYE FGQALFTGWA AASLCLLGGA
     LLCCSCPRKT TSYPTPRPYP KPAPSSGKDY V
//
