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CD81 antigen (26 kDa cell surface protein TAPA-1) (Target of the antiproliferative antibody 1) (Tetraspanin-28) (Tspan-28) (CD antigen CD81)

 CD81_HUMAN              Reviewed;         236 AA.
P60033; P18582; Q5U0J6;
21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
21-NOV-2003, sequence version 1.
22-NOV-2017, entry version 144.
RecName: Full=CD81 antigen;
AltName: Full=26 kDa cell surface protein TAPA-1;
AltName: Full=Target of the antiproliferative antibody 1;
AltName: Full=Tetraspanin-28;
Short=Tspan-28;
AltName: CD_antigen=CD81;
Name=CD81; Synonyms=TAPA1, TSPAN28;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1695320; DOI=10.1128/MCB.10.8.4007;
Oren R., Takahashi S., Doss C., Levy R., Levy S.;
"TAPA-1, the target of an antiproliferative antibody, defines a new
family of transmembrane proteins.";
Mol. Cell. Biol. 10:4007-4015(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH IFITM1.
PubMed=2398277;
Takahashi S., Doss C., Levy S., Levy R.;
"TAPA-1, the target of an antiproliferative antibody, is associated on
the cell surface with the Leu-13 antigen.";
J. Immunol. 145:2207-2213(1990).
[7]
TOPOLOGY.
PubMed=1860863;
Levy S., Nguyen V.Q., Andria M.L., Takahashi S.;
"Structure and membrane topology of TAPA-1.";
J. Biol. Chem. 266:14597-14602(1991).
[8]
INTERACTION WITH IGSF8.
PubMed=11504738; DOI=10.1074/jbc.M107338200;
Stipp C.S., Kolesnikova T.V., Hemler M.E.;
"EWI-2 is a major CD9 and CD81 partner and member of a novel Ig
protein subfamily.";
J. Biol. Chem. 276:40545-40554(2001).
[9]
INTERACTION WITH HCV E1/E2 ENVELOPE HETERODIMER.
PubMed=12970454; DOI=10.1128/JVI.77.19.10677-10683.2003;
Cocquerel L., Kuo C.-C., Dubuisson J., Levy S.;
"CD81-dependent binding of hepatitis C virus E1E2 heterodimers.";
J. Virol. 77:10677-10683(2003).
[10]
INTERACTION WITH HCV E1/E2 ENVELOPE HETERODIMER.
PubMed=12913001; DOI=10.1074/jbc.M305289200;
Bartosch B., Vitelli A., Granier C., Goujon C., Dubuisson J.,
Pascale S., Scarselli E., Cortese R., Nicosia A., Cosset F.-L.;
"Cell entry of hepatitis C virus requires a set of co-receptors that
include the CD81 tetraspanin and the SR-B1 scavenger receptor.";
J. Biol. Chem. 278:41624-41630(2003).
[11]
INTERACTION WITH ADGRG1 AND GNA11.
PubMed=15004227; DOI=10.1091/mbc.E03-12-0886;
Little K.D., Hemler M.E., Stipp C.S.;
"Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact
cells: central role of CD81 in facilitating GPR56-Galpha q/11
association.";
Mol. Biol. Cell 15:2375-2387(2004).
[12]
FUNCTION (MICROBIAL INFECTION), SUBUNIT, SUBCELLULAR LOCATION, AND
INTERACTION WITH CLDN1; CLDN6 AND CLDN9.
PubMed=20375010; DOI=10.1074/jbc.M110.104836;
Harris H.J., Davis C., Mullins J.G., Hu K., Goodall M., Farquhar M.J.,
Mee C.J., McCaffrey K., Young S., Drummer H., Balfe P.,
McKeating J.A.;
"Claudin association with CD81 defines hepatitis C virus entry.";
J. Biol. Chem. 285:21092-21102(2010).
[13]
INVOLVEMENT IN CVID6.
PubMed=20237408; DOI=10.1172/JCI39748;
van Zelm M.C., Smet J., Adams B., Mascart F., Schandene L.,
Janssen F., Ferster A., Kuo C.-C., Levy S., van Dongen J.J.M.,
van der Burg M.;
"CD81 gene defect in humans disrupts CD19 complex formation and leads
to antibody deficiency.";
J. Clin. Invest. 120:1265-1274(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
INTERACTION WITH CD53 AND SCIMP.
PubMed=21930792; DOI=10.1128/MCB.05817-11;
Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M.,
Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A.,
Brdicka T.;
"SCIMP, a transmembrane adapter protein involved in major
histocompatibility complex class II signaling.";
Mol. Cell. Biol. 31:4550-4562(2011).
[16]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CLDN1.
PubMed=21516087; DOI=10.1038/nm.2341;
Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L.,
Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B.,
Zahid M.N., Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M.,
Pietschmann T., Patel A.H., Pessaux P., Doffoel M., Raffelsberger W.,
Poch O., McKeating J.A., Brino L., Baumert T.F.;
"EGFR and EphA2 are host factors for hepatitis C virus entry and
possible targets for antiviral therapy.";
Nat. Med. 17:589-595(2011).
[17]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 113-202.
PubMed=11226150; DOI=10.1093/emboj/20.1.12;
Kitadokoro K., Bordo D., Galli G., Petracca R., Falugi F.,
Abrignani S., Grandi G., Bolognesi M.;
"CD81 extracellular domain 3D structure: insight into the tetraspanin
superfamily structural motifs.";
EMBO J. 20:12-18(2001).
[18]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 113-201.
PubMed=12437138; DOI=10.1515/BC.2002.164;
Kitadokoro K., Ponassi M., Galli G., Petracca R., Falugi F.,
Grandi G., Bolognesi M.;
"Subunit association and conformational flexibility in the head
subdomain of human CD81 large extracellular loop.";
Biol. Chem. 383:1447-1452(2002).
-!- FUNCTION: May play an important role in the regulation of lymphoma
cell growth. Interacts with a 16-kDa Leu-13 protein to form a
complex possibly involved in signal transduction. May act as the
viral receptor for HCV.
-!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
virus (HCV) in hepatocytes. Associates with CLDN1 and the CLDN1-
CD81 receptor complex is essential for HCV entry into host cell.
{ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:21516087}.
-!- SUBUNIT: Homodimer (PubMed:20375010). Interacts directly with
IGSF8 (PubMed:11504738). Interacts with CD53 and SCIMP
(PubMed:21930792). Interacts with IFITM1 (PubMed:2398277).
Interacts with IFITM2 and IFITM3 (By similarity). Part of a GPCR-
tetraspanin complex consisting at least of ADGRG1, CD81,
eventually CD9, and GNA11 in which CD81 is enhancing the
association of ADGRG1 with GNA11 (PubMed:15004227). Interacts with
CLDN1 (PubMed:20375010, PubMed:21516087). Interacts with CLDN6 and
CLDN9 (PubMed:20375010). {ECO:0000250|UniProtKB:P35762,
ECO:0000269|PubMed:11504738, ECO:0000269|PubMed:15004227,
ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:21516087,
ECO:0000269|PubMed:21930792, ECO:0000269|PubMed:2398277}.
-!- SUBUNIT: (Microbial infection) Plays a critical role in HCV
attachment and/or cell entry by interacting with HCV E1/E2
glycoproteins heterodimer. {ECO:0000269|PubMed:12913001,
ECO:0000269|PubMed:12970454}.
-!- INTERACTION:
P27958:- (xeno); NbExp=11; IntAct=EBI-712921, EBI-6904269;
Q99IB8:- (xeno); NbExp=2; IntAct=EBI-712921, EBI-6901449;
Q14739:LBR; NbExp=4; IntAct=EBI-712921, EBI-1055147;
-!- SUBCELLULAR LOCATION: Basolateral cell membrane
{ECO:0000269|PubMed:20375010}; Multi-pass membrane protein
{ECO:0000255}. Note=Associates with CLDN1 and the CLDN1-CD81
complex localizes to the basolateral cell membrane.
{ECO:0000269|PubMed:20375010}.
-!- TISSUE SPECIFICITY: Hematolymphoid, neuroectodermal and
mesenchymal tumor cell lines.
-!- PTM: Not glycosylated. {ECO:0000305}.
-!- DISEASE: Immunodeficiency, common variable, 6 (CVID6)
[MIM:613496]: A primary immunodeficiency characterized by antibody
deficiency, hypogammaglobulinemia, recurrent bacterial infections
and an inability to mount an antibody response to antigen. The
defect results from a failure of B-cell differentiation and
impaired secretion of immunoglobulins; the numbers of circulating
B-cells is usually in the normal range, but can be low.
{ECO:0000269|PubMed:20237408}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
{ECO:0000305}.
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EMBL; M33680; AAA36663.1; -; mRNA.
EMBL; BT019507; AAV38314.1; -; mRNA.
EMBL; BT019508; AAV38315.1; -; mRNA.
EMBL; EF064749; ABK41932.1; -; Genomic_DNA.
EMBL; AC129929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002978; AAH02978.1; -; mRNA.
EMBL; BC093047; AAH93047.1; -; mRNA.
CCDS; CCDS7734.1; -.
PIR; A35649; A35649.
RefSeq; NP_001284578.1; NM_001297649.1.
RefSeq; NP_004347.1; NM_004356.3.
UniGene; Hs.54457; -.
PDB; 1G8Q; X-ray; 1.60 A; A/B=113-201.
PDB; 1IV5; X-ray; 2.60 A; A/B=113-201.
PDB; 2AVZ; Model; -; A=1-236.
PDB; 3X0E; X-ray; 1.84 A; A/B=113-202.
PDB; 5DFV; X-ray; 2.80 A; A/B=112-201.
PDB; 5DFW; X-ray; 2.33 A; A=112-201.
PDB; 5M2C; X-ray; 1.96 A; A/B=112-201.
PDB; 5M33; X-ray; 1.28 A; A/B=113-201.
PDB; 5M3D; X-ray; 2.38 A; A/B/C/D=112-201.
PDB; 5M3T; X-ray; 2.02 A; A/B=112-201.
PDB; 5M4R; X-ray; 3.10 A; A/B/C/D/E=112-201.
PDB; 5TCX; X-ray; 2.96 A; A=2-236.
PDBsum; 1G8Q; -.
PDBsum; 1IV5; -.
PDBsum; 2AVZ; -.
PDBsum; 3X0E; -.
PDBsum; 5DFV; -.
PDBsum; 5DFW; -.
PDBsum; 5M2C; -.
PDBsum; 5M33; -.
PDBsum; 5M3D; -.
PDBsum; 5M3T; -.
PDBsum; 5M4R; -.
PDBsum; 5TCX; -.
ProteinModelPortal; P60033; -.
SMR; P60033; -.
BioGrid; 107413; 199.
CORUM; P60033; -.
IntAct; P60033; 41.
MINT; MINT-5001104; -.
STRING; 9606.ENSP00000263645; -.
BindingDB; P60033; -.
ChEMBL; CHEMBL1075180; -.
TCDB; 8.A.40.1.1; the tetraspanin (tetraspanin) family.
iPTMnet; P60033; -.
PhosphoSitePlus; P60033; -.
SwissPalm; P60033; -.
BioMuta; CD81; -.
DMDM; 38503376; -.
EPD; P60033; -.
MaxQB; P60033; -.
PaxDb; P60033; -.
PeptideAtlas; P60033; -.
PRIDE; P60033; -.
DNASU; 975; -.
Ensembl; ENST00000263645; ENSP00000263645; ENSG00000110651.
GeneID; 975; -.
KEGG; hsa:975; -.
UCSC; uc001lwf.2; human.
CTD; 975; -.
DisGeNET; 975; -.
EuPathDB; HostDB:ENSG00000110651.11; -.
GeneCards; CD81; -.
HGNC; HGNC:1701; CD81.
HPA; CAB002507; -.
HPA; HPA007234; -.
MalaCards; CD81; -.
MIM; 186845; gene.
MIM; 613496; phenotype.
neXtProt; NX_P60033; -.
OpenTargets; ENSG00000110651; -.
Orphanet; 1572; Common variable immunodeficiency.
PharmGKB; PA26240; -.
eggNOG; KOG3882; Eukaryota.
eggNOG; ENOG4111IRY; LUCA.
GeneTree; ENSGT00880000137858; -.
HOGENOM; HOG000230651; -.
HOVERGEN; HBG002324; -.
InParanoid; P60033; -.
KO; K06508; -.
PhylomeDB; P60033; -.
TreeFam; TF352895; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SignaLink; P60033; -.
ChiTaRS; CD81; human.
EvolutionaryTrace; P60033; -.
GeneWiki; CD81; -.
GenomeRNAi; 975; -.
PRO; PR:P60033; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110651; -.
CleanEx; HS_CD81; -.
ExpressionAtlas; P60033; baseline and differential.
Genevisible; P60033; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:1990459; F:transferrin receptor binding; IPI:BHF-UCL.
GO; GO:0001618; F:virus receptor activity; IMP:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0043128; P:positive regulation of 1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:AgBase.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:1904352; P:positive regulation of protein catabolic process in the vacuole; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:BHF-UCL.
GO; GO:0008104; P:protein localization; IDA:UniProtKB.
GO; GO:0061462; P:protein localization to lysosome; IMP:BHF-UCL.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; TAS:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; IEA:Ensembl.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0031647; P:regulation of protein stability; IMP:BHF-UCL.
GO; GO:0046718; P:viral entry into host cell; TAS:UniProtKB.
Gene3D; 1.10.1450.10; -; 1.
InterPro; IPR000301; Tetraspanin.
InterPro; IPR018499; Tetraspanin/Peripherin.
InterPro; IPR018503; Tetraspanin_CS.
InterPro; IPR008952; Tetraspanin_EC2_sf.
Pfam; PF00335; Tetraspannin; 1.
PIRSF; PIRSF002419; Tetraspanin; 1.
PRINTS; PR00259; TMFOUR.
SUPFAM; SSF48652; SSF48652; 1.
PROSITE; PS00421; TM4_1; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Host cell receptor for virus entry; Host-virus interaction; Membrane;
Receptor; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 236 CD81 antigen.
/FTId=PRO_0000219221.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 33 Helical. {ECO:0000255}.
TOPO_DOM 34 63 Extracellular. {ECO:0000255}.
TRANSMEM 64 84 Helical. {ECO:0000255}.
TOPO_DOM 85 89 Cytoplasmic. {ECO:0000255}.
TRANSMEM 90 112 Helical. {ECO:0000255}.
TOPO_DOM 113 201 Extracellular. {ECO:0000255}.
TRANSMEM 202 224 Helical. {ECO:0000255}.
TOPO_DOM 225 236 Cytoplasmic. {ECO:0000255}.
DISULFID 156 190
DISULFID 157 175
HELIX 10 36 {ECO:0000244|PDB:5TCX}.
HELIX 57 80 {ECO:0000244|PDB:5TCX}.
HELIX 81 84 {ECO:0000244|PDB:5TCX}.
HELIX 89 114 {ECO:0000244|PDB:5TCX}.
HELIX 116 136 {ECO:0000244|PDB:5M33}.
HELIX 141 154 {ECO:0000244|PDB:5M33}.
STRAND 158 160 {ECO:0000244|PDB:5M3D}.
HELIX 163 165 {ECO:0000244|PDB:5M33}.
HELIX 166 171 {ECO:0000244|PDB:5M33}.
HELIX 172 174 {ECO:0000244|PDB:5M2C}.
HELIX 181 185 {ECO:0000244|PDB:5M33}.
HELIX 190 199 {ECO:0000244|PDB:5M33}.
HELIX 202 230 {ECO:0000244|PDB:5TCX}.
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


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