CD81_HUMAN
ID CD81_HUMAN Reviewed; 236 AA.
AC P60033; P18582; Q5U0J6;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=CD81 antigen;
DE AltName: Full=26 kDa cell surface protein TAPA-1 {ECO:0000303|PubMed:1695320};
DE AltName: Full=Target of the antiproliferative antibody 1 {ECO:0000303|PubMed:1695320};
DE AltName: Full=Tetraspanin-28;
DE Short=Tspan-28;
DE AltName: CD_antigen=CD81 {ECO:0000303|PubMed:8766544};
GN Name=CD81 {ECO:0000303|PubMed:8766544, ECO:0000312|HGNC:HGNC:1701};
GN Synonyms=TAPA1 {ECO:0000303|PubMed:1695320}, TSPAN28;
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 SUBCELLULAR LOCATION.
RX PubMed=1695320; DOI=10.1128/mcb.10.8.4007-4015.1990;
RA Oren R., Takahashi S., Doss C., Levy R., Levy S.;
RT "TAPA-1, the target of an antiproliferative antibody, defines a new family
RT of transmembrane proteins.";
RL Mol. Cell. Biol. 10:4007-4015(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [GENOMIC DNA].
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
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 [6]
RP INTERACTION WITH IFITM1, AND SUBCELLULAR LOCATION.
RX PubMed=2398277;
RA Takahashi S., Doss C., Levy S., Levy R.;
RT "TAPA-1, the target of an antiproliferative antibody, is associated on the
RT cell surface with the Leu-13 antigen.";
RL J. Immunol. 145:2207-2213(1990).
RN [7]
RP TOPOLOGY.
RX PubMed=1860863; DOI=10.1016/s0021-9258(18)98728-4;
RA Levy S., Nguyen V.Q., Andria M.L., Takahashi S.;
RT "Structure and membrane topology of TAPA-1.";
RL J. Biol. Chem. 266:14597-14602(1991).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH CR2; CD19 AND IFITM1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=1383329;
RA Bradbury L.E., Kansas G.S., Levy S., Evans R.L., Tedder T.F.;
RT "The CD19/CD21 signal transducing complex of human B lymphocytes includes
RT the target of antiproliferative antibody-1 and Leu-13 molecules.";
RL J. Immunol. 149:2841-2850(1992).
RN [9]
RP FUNCTION, INTERACTION WITH IFITM1, AND INTERACTION WITH HLA-DR.
RX PubMed=8409388;
RA Schick M.R., Levy S.;
RT "The TAPA-1 molecule is associated on the surface of B cells with HLA-DR
RT molecules.";
RL J. Immunol. 151:4090-4097(1993).
RN [10]
RP FUNCTION.
RX PubMed=8766544; DOI=10.1002/eji.1830260706;
RA Secrist H., Levy S., DeKruyff R.H., Umetsu D.T.;
RT "Ligation of TAPA-1 (CD81) or major histocompatibility complex class II in
RT co-cultures of human B and T lymphocytes enhances interleukin-4 synthesis
RT by antigen-specific CD4+ T cells.";
RL Eur. J. Immunol. 26:1435-1442(1996).
RN [11]
RP INTERACTION WITH IGSF8.
RX PubMed=11504738; DOI=10.1074/jbc.m107338200;
RA Stipp C.S., Kolesnikova T.V., Hemler M.E.;
RT "EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein
RT subfamily.";
RL J. Biol. Chem. 276:40545-40554(2001).
RN [12]
RP INTERACTION WITH HCV E1/E2 ENVELOPE HETERODIMER (MICROBIAL INFECTION).
RX PubMed=12913001; DOI=10.1074/jbc.m305289200;
RA Bartosch B., Vitelli A., Granier C., Goujon C., Dubuisson J., Pascale S.,
RA Scarselli E., Cortese R., Nicosia A., Cosset F.-L.;
RT "Cell entry of hepatitis C virus requires a set of co-receptors that
RT include the CD81 tetraspanin and the SR-B1 scavenger receptor.";
RL J. Biol. Chem. 278:41624-41630(2003).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CD9.
RX PubMed=12796480; DOI=10.1083/jcb.200212031;
RA Takeda Y., Tachibana I., Miyado K., Kobayashi M., Miyazaki T.,
RA Funakoshi T., Kimura H., Yamane H., Saito Y., Goto H., Yoneda T.,
RA Yoshida M., Kumagai T., Osaki T., Hayashi S., Kawase I., Mekada E.;
RT "Tetraspanins CD9 and CD81 function to prevent the fusion of mononuclear
RT phagocytes.";
RL J. Cell Biol. 161:945-956(2003).
RN [14]
RP INTERACTION WITH HCV E1/E2 ENVELOPE HETERODIMER (MICROBIAL INFECTION).
RX PubMed=12970454; DOI=10.1128/jvi.77.19.10677-10683.2003;
RA Cocquerel L., Kuo C.-C., Dubuisson J., Levy S.;
RT "CD81-dependent binding of hepatitis C virus E1E2 heterodimers.";
RL J. Virol. 77:10677-10683(2003).
RN [15]
RP FUNCTION (MICROBIAL INFECTION), AND TISSUE SPECIFICITY.
RX PubMed=12483205; DOI=10.1038/nm808;
RA Silvie O., Rubinstein E., Franetich J.F., Prenant M., Belnoue E., Renia L.,
RA Hannoun L., Eling W., Levy S., Boucheix C., Mazier D.;
RT "Hepatocyte CD81 is required for Plasmodium falciparum and Plasmodium
RT yoelii sporozoite infectivity.";
RL Nat. Med. 9:93-96(2003).
RN [16]
RP PTM, AND FUNCTION.
RX PubMed=15161911; DOI=10.1074/jbc.m404410200;
RA Cherukuri A., Carter R.H., Brooks S., Bornmann W., Finn R., Dowd C.S.,
RA Pierce S.K.;
RT "B cell signaling is regulated by induced palmitoylation of CD81.";
RL J. Biol. Chem. 279:31973-31982(2004).
RN [17]
RP INTERACTION WITH ADGRG1 AND GNA11.
RX PubMed=15004227; DOI=10.1091/mbc.e03-12-0886;
RA Little K.D., Hemler M.E., Stipp C.S.;
RT "Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact
RT cells: central role of CD81 in facilitating GPR56-Galpha q/11
RT association.";
RL Mol. Biol. Cell 15:2375-2387(2004).
RN [18]
RP FUNCTION, AND INTERACTION WITH CD19.
RX PubMed=16449649; DOI=10.1128/mcb.26.4.1373-1385.2006;
RA Shoham T., Rajapaksa R., Kuo C.C., Haimovich J., Levy S.;
RT "Building of the tetraspanin web: distinct structural domains of CD81
RT function in different cellular compartments.";
RL Mol. Cell. Biol. 26:1373-1385(2006).
RN [19]
RP FUNCTION (MICROBIAL INFECTION), SUBUNIT, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CLDN1; CLDN6 AND CLDN9.
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 [20]
RP INVOLVEMENT IN CVID6, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20237408; DOI=10.1172/jci39748;
RA van Zelm M.C., Smet J., Adams B., Mascart F., Schandene L., Janssen F.,
RA Ferster A., Kuo C.-C., Levy S., van Dongen J.J.M., van der Burg M.;
RT "CD81 gene defect in humans disrupts CD19 complex formation and leads to
RT antibody deficiency.";
RL J. Clin. Invest. 120:1265-1274(2010).
RN [21]
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 [22]
RP INTERACTION WITH CD53 AND SCIMP.
RX PubMed=21930792; DOI=10.1128/mcb.05817-11;
RA Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T.,
RA Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T.;
RT "SCIMP, a transmembrane adapter protein involved in major
RT histocompatibility complex class II signaling.";
RL Mol. Cell. Biol. 31:4550-4562(2011).
RN [23]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CLDN1.
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 [24]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22307619; DOI=10.1073/pnas.1121307109;
RA Sagi Y., Landrigan A., Levy R., Levy S.;
RT "Complementary costimulation of human T-cell subpopulations by cluster of
RT differentiation 28 (CD28) and CD81.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:1613-1618(2012).
RN [25]
RP FUNCTION, INTERACTION WITH CD247, INTERACTION WITH ICAM1, AND INTERACTION
RP WITH CD9.
RX PubMed=23858057; DOI=10.1128/mcb.00302-13;
RA Rocha-Perugini V., Zamai M., Gonzalez-Granado J.M., Barreiro O., Tejera E.,
RA Yanez-Mo M., Caiolfa V.R., Sanchez-Madrid F.;
RT "CD81 controls sustained T cell activation signaling and defines the
RT maturation stages of cognate immunological synapses.";
RL Mol. Cell. Biol. 33:3644-3658(2013).
RN [26]
RP FUNCTION, INTERACTION WITH IFITM1, AND SUBCELLULAR LOCATION.
RX PubMed=26354436; DOI=10.1074/jbc.m115.657346;
RA Narayana S.K., Helbig K.J., McCartney E.M., Eyre N.S., Bull R.A.,
RA Eltahla A., Lloyd A.R., Beard M.R.;
RT "The Interferon-induced Transmembrane Proteins, IFITM1, IFITM2, and IFITM3
RT Inhibit Hepatitis C Virus Entry.";
RL J. Biol. Chem. 290:25946-25959(2015).
RN [27]
RP INTERACTION WITH INTEGRIN ITGAV:ITGB3, AND MUTAGENESIS OF LYS-116; ILE-119;
RP LYS-121; LYS-124; PHE-126; LYS-144; LYS-148; PHE-186 AND LYS-187.
RX PubMed=27993971; DOI=10.1042/bcj20160998;
RA Yu J., Lee C.Y., Changou C.A., Cedano-Prieto D.M., Takada Y.K., Takada Y.;
RT "The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding
RT site of integrin alphavbeta3.";
RL Biochem. J. 474:589-596(2017).
RN [28]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SAMHD1.
RX PubMed=28871089; DOI=10.1038/s41564-017-0019-0;
RA Rocha-Perugini V., Suarez H., Alvarez S., Lopez-Martin S., Lenzi G.M.,
RA Vences-Catalan F., Levy S., Kim B., Munoz-Fernandez M.A.,
RA Sanchez-Madrid F., Yanez-Mo M.;
RT "CD81 association with SAMHD1 enhances HIV-1 reverse transcription by
RT increasing dNTP levels.";
RL Nat. Microbiol. 2:1513-1522(2017).
RN [29] {ECO:0007744|PDB:1G8Q}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 113-202.
RX PubMed=11226150; DOI=10.1093/emboj/20.1.12;
RA Kitadokoro K., Bordo D., Galli G., Petracca R., Falugi F., Abrignani S.,
RA Grandi G., Bolognesi M.;
RT "CD81 extracellular domain 3D structure: insight into the tetraspanin
RT superfamily structural motifs.";
RL EMBO J. 20:12-18(2001).
RN [30] {ECO:0007744|PDB:1IV5}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 113-201.
RX PubMed=12437138; DOI=10.1515/bc.2002.164;
RA Kitadokoro K., Ponassi M., Galli G., Petracca R., Falugi F., Grandi G.,
RA Bolognesi M.;
RT "Subunit association and conformational flexibility in the head subdomain
RT of human CD81 large extracellular loop.";
RL Biol. Chem. 383:1447-1452(2002).
RN [31] {ECO:0007744|PDB:3X0E}
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 113-202, FUNCTION (MICROBIAL
RP INFECTION), INTERACTION WITH HCV ENVELOPE PROTEIN E2 (MICROBIAL INFECTION),
RP DISULFIDE BONDS, AND MUTAGENESIS OF GLU-188 AND ASP-196.
RX PubMed=26116703; DOI=10.1096/fj.15-272880;
RA Yang W., Zhang M., Chi X., Liu X., Qin B., Cui S.;
RT "An intramolecular bond at cluster of differentiation 81 ectodomain is
RT important for hepatitis C virus entry.";
RL FASEB J. 29:4214-4226(2015).
RN [32] {ECO:0007744|PDB:5TCX}
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS), FUNCTION, TOPOLOGY, DISULFIDE
RP BONDS, CHOLESTEROL BINDING, DOMAIN, AND MUTAGENESIS OF GLU-219.
RX PubMed=27881302; DOI=10.1016/j.cell.2016.09.056;
RA Zimmerman B., Kelly B., McMillan B.J., Seegar T.C.M., Dror R.O.,
RA Kruse A.C., Blacklow S.C.;
RT "Crystal Structure of a Full-Length Human Tetraspanin Reveals a
RT Cholesterol-Binding Pocket.";
RL Cell 167:1041-1051.E11(2016).
RN [33] {ECO:0007744|PDB:5M2C, ECO:0007744|PDB:5M33, ECO:0007744|PDB:5M3D, ECO:0007744|PDB:5M3T, ECO:0007744|PDB:5M4R}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 113-201, AND DISULFIDE BONDS.
RX PubMed=27916518; DOI=10.1016/j.str.2016.11.003;
RA Cunha E.S., Sfriso P., Rojas A.L., Roversi P., Hospital A., Orozco M.,
RA Abrescia N.G.A.;
RT "Mechanism of Structural Tuning of the Hepatitis C Virus Human Cellular
RT Receptor CD81 Large Extracellular Loop.";
RL Structure 25:53-65(2017).
CC -!- FUNCTION: Structural component of specialized membrane microdomains
CC known as tetraspanin-enriched microdomains (TERMs), which act as
CC platforms for receptor clustering and signaling. Essential for
CC trafficking and compartmentalization of CD19 receptor on the surface of
CC activated B cells (PubMed:20237408, PubMed:27881302, PubMed:16449649).
CC Upon initial encounter with microbial pathogens, enables the assembly
CC of CD19-CR2/CD21 and B cell receptor (BCR) complexes at signaling
CC TERMs, lowering the threshold dose of antigen required to trigger B
CC cell clonal expansion and antibody production (PubMed:15161911,
CC PubMed:20237408). In T cells, facilitates the localization of CD247/CD3
CC zeta at antigen-induced synapses with B cells, providing for
CC costimulation and polarization toward T helper type 2 phenotype
CC (PubMed:22307619, PubMed:23858057, PubMed:8766544). Present in MHC
CC class II compartments, may also play a role in antigen presentation
CC (PubMed:8409388, PubMed:8766544). Can act both as positive and negative
CC regulator of homotypic or heterotypic cell-cell fusion processes.
CC Positively regulates sperm-egg fusion and may be involved in acrosome
CC reaction (By similarity). In myoblasts, associates with CD9 and PTGFRN
CC and inhibits myotube fusion during muscle regeneration (By similarity).
CC In macrophages, associates with CD9 and beta-1 and beta-2 integrins,
CC and prevents macrophage fusion into multinucleated giant cells
CC specialized in ingesting complement-opsonized large particles
CC (PubMed:12796480). Also prevents the fusion of mononuclear cell
CC progenitors into osteoclasts in charge of bone resorption (By
CC similarity). May regulate the compartmentalization of enzymatic
CC activities. In T cells, defines the subcellular localization of dNTPase
CC SAMHD1 and permits its degradation by the proteasome, thereby
CC controlling intracellular dNTP levels (PubMed:28871089). Also involved
CC in cell adhesion and motility. Positively regulates integrin-mediated
CC adhesion of macrophages, particularly relevant for the inflammatory
CC response in the lung (By similarity). {ECO:0000250|UniProtKB:P35762,
CC ECO:0000269|PubMed:12796480, ECO:0000269|PubMed:15161911,
CC ECO:0000269|PubMed:16449649, ECO:0000269|PubMed:20237408,
CC ECO:0000269|PubMed:22307619, ECO:0000269|PubMed:23858057,
CC ECO:0000269|PubMed:27881302, ECO:0000269|PubMed:28871089,
CC ECO:0000269|PubMed:8409388, ECO:0000269|PubMed:8766544}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
CC virus (HCV) in hepatocytes. Association with CLDN1 and the CLDN1-CD81
CC receptor complex is essential for HCV entry into host cell.
CC {ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:21516087,
CC ECO:0000269|PubMed:26116703, ECO:0000269|PubMed:26354436}.
CC -!- FUNCTION: (Microbial infection) Involved in SAMHD1-dependent
CC restriction of HIV-1 replication. May support early replication of both
CC R5- and X4-tropic HIV-1 viruses in T cells, likely via proteasome-
CC dependent degradation of SAMHD1. {ECO:0000269|PubMed:28871089}.
CC -!- FUNCTION: (Microbial infection) Specifically required for Plasmodium
CC falciparum infectivity of hepatocytes, controlling sporozoite entry
CC into hepatocytes via the parasitophorous vacuole and subsequent
CC parasite differentiation to exoerythrocytic forms.
CC {ECO:0000269|PubMed:12483205}.
CC -!- SUBUNIT: Homodimer (PubMed:20375010). Part of a complex composed of
CC CD19, CR2/CD21, CD81 and IFITM1/CD225 in the membrane of mature B
CC cells. Interacts (via the second extracellular domain) with CD19; this
CC interaction is initiated early during biosynthesis in the ER and
CC enables trafficking of only properly folded CD19 (PubMed:16449649,
CC PubMed:1383329). Part of a complex that includes MHC class II/HLA-DR
CC molecules and IFITM1 (PubMed:8409388). Interacts with IFITM1
CC (PubMed:2398277, PubMed:26354436). Interacts with IFITM2 and IFITM3 (By
CC similarity). Part of integrin-tetraspanin complex composed of CD9,
CC CD81, beta-1 and beta-2 integrins in the membrane of
CC monocyte/macrophages (PubMed:12796480). Interacts (via the second
CC extracellular domain) with integrin ITGAV:ITGB3 (PubMed:27993971).
CC Interacts with CD247/CD3 zeta, ICAM1 and CD9 at the immune synapse on T
CC cell membrane (PubMed:23858057). Part of a GPCR-tetraspanin complex
CC consisting at least of ADGRG1, CD81, possibly CD9, and GNA11 in which
CC CD81 enhances the association of ADGRG1 with GNA11 (PubMed:15004227).
CC Part of a complex composed of CD9, CD81, PTGFRN and IGSF8 (By
CC similarity). Interacts directly with IGSF8 (PubMed:11504738). Interacts
CC with CD53 and SCIMP (PubMed:21930792). Interacts with SAMHD1 (via its
CC C-terminus) (PubMed:28871089). Interacts with glypican GPC3 and with
CC the transcriptional repressor HHEX; binding to GPC3 decreases the
CC availability of free CD81 for binding to HHEX, resulting in nuclear
CC translocation of HHEX and transcriptional repression (By similarity).
CC Interacts with CLDN1 (PubMed:20375010, PubMed:21516087). Interacts with
CC CLDN6 and CLDN9 (PubMed:20375010). {ECO:0000250|UniProtKB:P35762,
CC ECO:0000269|PubMed:12796480, ECO:0000269|PubMed:1383329,
CC ECO:0000269|PubMed:16449649, ECO:0000269|PubMed:20375010,
CC ECO:0000269|PubMed:23858057, ECO:0000269|PubMed:2398277,
CC ECO:0000269|PubMed:26354436, ECO:0000269|PubMed:28871089,
CC ECO:0000269|PubMed:8409388}.
CC -!- SUBUNIT: (Microbial infection) Plays a critical role in HCV attachment
CC and/or cell entry by interacting with HCV E1/E2 glycoproteins
CC heterodimer. {ECO:0000269|PubMed:12913001, ECO:0000269|PubMed:12970454,
CC ECO:0000269|PubMed:26116703}.
CC -!- INTERACTION:
CC P60033; O14672: ADAM10; NbExp=9; IntAct=EBI-712921, EBI-1536151;
CC P60033; PRO_0000029067 [O14672]: ADAM10; NbExp=2; IntAct=EBI-712921, EBI-21222747;
CC P60033; Q13520: AQP6; NbExp=3; IntAct=EBI-712921, EBI-13059134;
CC P60033; Q10589: BST2; NbExp=3; IntAct=EBI-712921, EBI-2476339;
CC P60033; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-712921, EBI-18013275;
CC P60033; Q15125: EBP; NbExp=3; IntAct=EBI-712921, EBI-3915253;
CC P60033; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-712921, EBI-781551;
CC P60033; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-712921, EBI-18304435;
CC P60033; P35212: GJA4; NbExp=3; IntAct=EBI-712921, EBI-6918707;
CC P60033; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-712921, EBI-3917143;
CC P60033; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-712921, EBI-13345167;
CC P60033; Q8TED1: GPX8; NbExp=3; IntAct=EBI-712921, EBI-11721746;
CC P60033; Q14739: LBR; NbExp=3; IntAct=EBI-712921, EBI-1055147;
CC P60033; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-712921, EBI-2820517;
CC P60033; Q96PE7: MCEE; NbExp=3; IntAct=EBI-712921, EBI-10292326;
CC P60033; Q9Y676: MRPS18B; NbExp=3; IntAct=EBI-712921, EBI-750085;
CC P60033; O14524-2: NEMP1; NbExp=3; IntAct=EBI-712921, EBI-10969203;
CC P60033; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-712921, EBI-716063;
CC P60033; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-712921, EBI-3920694;
CC P60033; Q8WTV0: SCARB1; NbExp=4; IntAct=EBI-712921, EBI-78657;
CC P60033; Q5VUM1: SDHAF4; NbExp=3; IntAct=EBI-712921, EBI-16769525;
CC P60033; Q9BXS9-3: SLC26A6; NbExp=3; IntAct=EBI-712921, EBI-12814225;
CC P60033; Q16623: STX1A; NbExp=3; IntAct=EBI-712921, EBI-712466;
CC P60033; Q8WY91: THAP4; NbExp=3; IntAct=EBI-712921, EBI-726691;
CC P60033; Q9Y320: TMX2; NbExp=3; IntAct=EBI-712921, EBI-6447886;
CC P60033; Q9NSU2-1: TREX1; NbExp=3; IntAct=EBI-712921, EBI-16746122;
CC P60033; PRO_0000037570 [P27958]; Xeno; NbExp=11; IntAct=EBI-712921, EBI-6904269;
CC P60033; PRO_0000045596 [Q99IB8]; Xeno; NbExp=2; IntAct=EBI-712921, EBI-6901449;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1383329,
CC ECO:0000269|PubMed:1695320, ECO:0000269|PubMed:20237408,
CC ECO:0000269|PubMed:22307619, ECO:0000269|PubMed:2398277,
CC ECO:0000269|PubMed:26354436}; Multi-pass membrane protein
CC {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:20375010};
CC Multi-pass membrane protein {ECO:0000255}. Note=Associates with CLDN1
CC and the CLDN1-CD81 complex localizes to the basolateral cell membrane.
CC {ECO:0000269|PubMed:20375010}.
CC -!- TISSUE SPECIFICITY: Expressed on B cells (at protein level)
CC (PubMed:20237408). Expressed in hepatocytes (at protein level)
CC (PubMed:12483205). Expressed in monocytes/macrophages (at protein
CC level) (PubMed:12796480). Expressed on both naive and memory CD4-
CC positive T cells (at protein level) (PubMed:22307619).
CC {ECO:0000269|PubMed:12483205, ECO:0000269|PubMed:12796480,
CC ECO:0000269|PubMed:20237408, ECO:0000269|PubMed:22307619}.
CC -!- DOMAIN: Binds cholesterol in a cavity lined by the transmembrane spans.
CC {ECO:0000269|PubMed:27881302}.
CC -!- PTM: Not glycosylated. {ECO:0000305}.
CC -!- PTM: Likely constitutively palmitoylated at low levels. Protein
CC palmitoylation is up-regulated upon coligation of BCR and CD9-C2R-CD81
CC complexes in lipid rafts. {ECO:0000269|PubMed:15161911}.
CC -!- DISEASE: Immunodeficiency, common variable, 6 (CVID6) [MIM:613496]: A
CC primary immunodeficiency characterized by antibody deficiency,
CC hypogammaglobulinemia, recurrent bacterial infections and an inability
CC to mount an antibody response to antigen. The defect results from a
CC failure of B-cell differentiation and impaired secretion of
CC immunoglobulins; the numbers of circulating B-cells is usually in the
CC normal range, but can be low. {ECO:0000269|PubMed:20237408}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; M33680; AAA36663.1; -; mRNA.
DR EMBL; BT019507; AAV38314.1; -; mRNA.
DR EMBL; BT019508; AAV38315.1; -; mRNA.
DR EMBL; EF064749; ABK41932.1; -; Genomic_DNA.
DR EMBL; AC129929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002978; AAH02978.1; -; mRNA.
DR EMBL; BC093047; AAH93047.1; -; mRNA.
DR CCDS; CCDS7734.1; -.
DR PIR; A35649; A35649.
DR RefSeq; NP_001284578.1; NM_001297649.1.
DR RefSeq; NP_004347.1; NM_004356.3.
DR PDB; 1G8Q; X-ray; 1.60 A; A/B=113-201.
DR PDB; 1IV5; X-ray; 2.60 A; A/B=113-201.
DR PDB; 3X0E; X-ray; 1.84 A; A/B=113-202.
DR PDB; 5DFV; X-ray; 2.80 A; A/B=112-201.
DR PDB; 5DFW; X-ray; 2.33 A; A=112-201.
DR PDB; 5M2C; X-ray; 1.96 A; A/B=112-201.
DR PDB; 5M33; X-ray; 1.28 A; A/B=113-201.
DR PDB; 5M3D; X-ray; 2.38 A; A/B/C/D=112-201.
DR PDB; 5M3T; X-ray; 2.02 A; A/B=112-201.
DR PDB; 5M4R; X-ray; 3.10 A; A/B/C/D/E=112-201.
DR PDB; 5TCX; X-ray; 2.96 A; A=2-236.
DR PDB; 6EJG; X-ray; 2.82 A; A/B=112-202.
DR PDB; 6EJM; X-ray; 2.15 A; A/B=112-202.
DR PDB; 6EK2; X-ray; 2.65 A; A/B=112-201.
DR PDB; 6U9S; X-ray; 2.40 A; C/F=112-200.
DR PDB; 7JIC; EM; 3.80 A; B=2-236.
DR PDBsum; 1G8Q; -.
DR PDBsum; 1IV5; -.
DR PDBsum; 3X0E; -.
DR PDBsum; 5DFV; -.
DR PDBsum; 5DFW; -.
DR PDBsum; 5M2C; -.
DR PDBsum; 5M33; -.
DR PDBsum; 5M3D; -.
DR PDBsum; 5M3T; -.
DR PDBsum; 5M4R; -.
DR PDBsum; 5TCX; -.
DR PDBsum; 6EJG; -.
DR PDBsum; 6EJM; -.
DR PDBsum; 6EK2; -.
DR PDBsum; 6U9S; -.
DR PDBsum; 7JIC; -.
DR AlphaFoldDB; P60033; -.
DR BMRB; P60033; -.
DR SMR; P60033; -.
DR BioGRID; 107413; 283.
DR CORUM; P60033; -.
DR IntAct; P60033; 293.
DR MINT; P60033; -.
DR STRING; 9606.ENSP00000263645; -.
DR BindingDB; P60033; -.
DR ChEMBL; CHEMBL1075180; -.
DR TCDB; 8.A.40.1.1; the tetraspanin (tetraspanin) family.
DR GlyGen; P60033; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P60033; -.
DR PhosphoSitePlus; P60033; -.
DR SwissPalm; P60033; -.
DR BioMuta; CD81; -.
DR DMDM; 38503376; -.
DR EPD; P60033; -.
DR jPOST; P60033; -.
DR MassIVE; P60033; -.
DR MaxQB; P60033; -.
DR PaxDb; P60033; -.
DR PeptideAtlas; P60033; -.
DR PRIDE; P60033; -.
DR ProteomicsDB; 57182; -.
DR ABCD; P60033; 10 sequenced antibodies.
DR Antibodypedia; 1570; 1293 antibodies from 46 providers.
DR DNASU; 975; -.
DR Ensembl; ENST00000263645.10; ENSP00000263645.5; ENSG00000110651.12.
DR GeneID; 975; -.
DR KEGG; hsa:975; -.
DR MANE-Select; ENST00000263645.10; ENSP00000263645.5; NM_004356.4; NP_004347.1.
DR UCSC; uc001lwf.2; human.
DR CTD; 975; -.
DR DisGeNET; 975; -.
DR GeneCards; CD81; -.
DR HGNC; HGNC:1701; CD81.
DR HPA; ENSG00000110651; Low tissue specificity.
DR MalaCards; CD81; -.
DR MIM; 186845; gene.
DR MIM; 613496; phenotype.
DR neXtProt; NX_P60033; -.
DR OpenTargets; ENSG00000110651; -.
DR Orphanet; 1572; Common variable immunodeficiency.
DR PharmGKB; PA26240; -.
DR VEuPathDB; HostDB:ENSG00000110651; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000158805; -.
DR HOGENOM; CLU_055524_10_0_1; -.
DR InParanoid; P60033; -.
DR OMA; HETLSCC; -.
DR OrthoDB; 1205716at2759; -.
DR PhylomeDB; P60033; -.
DR TreeFam; TF352895; -.
DR PathwayCommons; P60033; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P60033; -.
DR BioGRID-ORCS; 975; 22 hits in 1078 CRISPR screens.
DR ChiTaRS; CD81; human.
DR EvolutionaryTrace; P60033; -.
DR GeneWiki; CD81; -.
DR GenomeRNAi; 975; -.
DR Pharos; P60033; Tchem.
DR PRO; PR:P60033; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P60033; protein.
DR Bgee; ENSG00000110651; Expressed in stromal cell of endometrium and 211 other tissues.
DR ExpressionAtlas; P60033; baseline and differential.
DR Genevisible; P60033; HS.
DR GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0042289; F:MHC class II protein binding; IDA:UniProtKB.
DR GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
DR GO; GO:1990459; F:transferrin receptor binding; IPI:BHF-UCL.
DR GO; GO:0001618; F:virus receptor activity; IMP:UniProtKB.
DR GO; GO:0035783; P:CD4-positive, alpha-beta T cell costimulation; IDA:UniProtKB.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IMP:UniProtKB.
DR GO; GO:0001771; P:immunological synapse formation; IMP:UniProtKB.
DR GO; GO:0034238; P:macrophage fusion; IDA:UniProtKB.
DR GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; ISS:UniProtKB.
DR GO; GO:0072675; P:osteoclast fusion; ISS:UniProtKB.
DR GO; GO:0043128; P:positive regulation of 1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB.
DR GO; GO:1905676; P:positive regulation of adaptive immune memory response; IMP:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:AgBase.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0002863; P:positive regulation of inflammatory response to antigenic stimulus; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:1904352; P:positive regulation of protein catabolic process in the vacuole; IMP:BHF-UCL.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:1903911; P:positive regulation of receptor clustering; IDA:UniProtKB.
DR GO; GO:2001190; P:positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IDA:UniProtKB.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; IMP:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; TAS:UniProtKB.
DR GO; GO:1905521; P:regulation of macrophage migration; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:BHF-UCL.
DR GO; GO:0046718; P:viral entry into host cell; TAS:UniProtKB.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR000301; Tetraspanin_animals.
DR InterPro; IPR018503; Tetraspanin_CS.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PIRSF; PIRSF002419; Tetraspanin; 1.
DR SUPFAM; SSF48652; SSF48652; 1.
DR PROSITE; PS00421; TM4_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond;
KW Host cell receptor for virus entry; Host-virus interaction; Immunity;
KW Lipid-binding; Membrane; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..236
FT /note="CD81 antigen"
FT /id="PRO_0000219221"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27881302,
FT ECO:0000305|PubMed:1860863"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27881302"
FT TOPO_DOM 34..63
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27881302"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27881302"
FT TOPO_DOM 85..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27881302"
FT TRANSMEM 90..112
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27881302"
FT TOPO_DOM 113..201
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27881302"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27881302"
FT TOPO_DOM 225..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27881302,
FT ECO:0000305|PubMed:1860863"
FT BINDING 219
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0000269|PubMed:27881302,
FT ECO:0007744|PDB:5TCX"
FT SITE 116
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:27993971"
FT SITE 144
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:27993971"
FT SITE 148
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000269|PubMed:27993971"
FT DISULFID 156..190
FT /evidence="ECO:0000269|PubMed:11226150,
FT ECO:0000269|PubMed:12437138, ECO:0000269|PubMed:26116703,
FT ECO:0000269|PubMed:27881302, ECO:0000269|PubMed:27916518,
FT ECO:0007744|PDB:1G8Q, ECO:0007744|PDB:1IV5,
FT ECO:0007744|PDB:3X0E, ECO:0007744|PDB:5DFV,
FT ECO:0007744|PDB:5DFW, ECO:0007744|PDB:5M2C,
FT ECO:0007744|PDB:5M33, ECO:0007744|PDB:5M3D,
FT ECO:0007744|PDB:5M3T, ECO:0007744|PDB:5M4R,
FT ECO:0007744|PDB:5TCX, ECO:0007744|PDB:6EJG,
FT ECO:0007744|PDB:6EJM, ECO:0007744|PDB:6EK2"
FT DISULFID 157..175
FT /evidence="ECO:0000269|PubMed:11226150,
FT ECO:0000269|PubMed:12437138, ECO:0000269|PubMed:26116703,
FT ECO:0000269|PubMed:27881302, ECO:0000269|PubMed:27916518,
FT ECO:0007744|PDB:1G8Q, ECO:0007744|PDB:1IV5,
FT ECO:0007744|PDB:3X0E, ECO:0007744|PDB:5DFV,
FT ECO:0007744|PDB:5DFW, ECO:0007744|PDB:5M2C,
FT ECO:0007744|PDB:5M33, ECO:0007744|PDB:5M3D,
FT ECO:0007744|PDB:5M3T, ECO:0007744|PDB:5M4R,
FT ECO:0007744|PDB:5TCX, ECO:0007744|PDB:6EJG,
FT ECO:0007744|PDB:6EJM, ECO:0007744|PDB:6EK2"
FT MUTAGEN 116
FT /note="K->E: Reduces binding to integrin."
FT /evidence="ECO:0000269|PubMed:27993971"
FT MUTAGEN 119
FT /note="I->A: No effect on integrin binding."
FT /evidence="ECO:0000269|PubMed:27993971"
FT MUTAGEN 121
FT /note="K->E: No effect on integrin binding."
FT /evidence="ECO:0000269|PubMed:27993971"
FT MUTAGEN 124
FT /note="K->E: No effect on integrin binding."
FT /evidence="ECO:0000269|PubMed:27993971"
FT MUTAGEN 126
FT /note="F->A: No effect on integrin binding."
FT /evidence="ECO:0000269|PubMed:27993971"
FT MUTAGEN 144
FT /note="K->E: Reduces binding to integrin; when associated
FT with E-148."
FT /evidence="ECO:0000269|PubMed:27993971"
FT MUTAGEN 148
FT /note="K->E: Reduces binding to integrin; when associated
FT with E-144."
FT /evidence="ECO:0000269|PubMed:27993971"
FT MUTAGEN 186
FT /note="F->A: No effect on integrin binding."
FT /evidence="ECO:0000269|PubMed:27993971"
FT MUTAGEN 187
FT /note="K->E: No effect on integrin binding."
FT /evidence="ECO:0000269|PubMed:27993971"
FT MUTAGEN 188
FT /note="E->K,Q: Strongly reduced affinity for HCV protein
FT E2; when associated with E-196."
FT /evidence="ECO:0000269|PubMed:26116703"
FT MUTAGEN 188
FT /note="E->K: Mildly reduced affinity for HCV protein E2."
FT /evidence="ECO:0000269|PubMed:26116703"
FT MUTAGEN 196
FT /note="D->E: Strongly reduced affinity for HCV protein E2;
FT when associated with K-188 or Q-188."
FT /evidence="ECO:0000269|PubMed:26116703"
FT MUTAGEN 196
FT /note="D->K,Q,R: Strongly reduced affinity for HCV protein
FT E2."
FT /evidence="ECO:0000269|PubMed:26116703"
FT MUTAGEN 219
FT /note="E->A,Q: Reduced affinity for cholesterol binding."
FT /evidence="ECO:0000269|PubMed:27881302"
FT HELIX 10..36
FT /evidence="ECO:0007829|PDB:5TCX"
FT HELIX 57..80
FT /evidence="ECO:0007829|PDB:5TCX"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:5TCX"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6U9S"
FT HELIX 116..136
FT /evidence="ECO:0007829|PDB:5M33"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:5M33"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5M3D"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:5M33"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:5M33"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5M2C"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:5M33"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:5M33"
FT HELIX 202..230
FT /evidence="ECO:0007829|PDB:5TCX"
SQ SEQUENCE 236 AA; 25809 MW; EB9BD7671AC91B4A CRC64;
MGVEGCTKCI KYLLFVFNFV FWLAGGVILG VALWLRHDPQ TTNLLYLELG DKPAPNTFYV
GIYILIAVGA VMMFVGFLGC YGAIQESQCL LGTFFTCLVI LFACEVAAGI WGFVNKDQIA
KDVKQFYDQA LQQAVVDDDA NNAKAVVKTF HETLDCCGSS TLTALTTSVL KNNLCPSGSN
IISNLFKEDC HQKIDDLFSG KLYLIGIAAI VVAVIMIFEM ILSMVLCCGI RNSSVY
