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CD63 antigen (Granulophysin) (Lysosomal-associated membrane protein 3) (LAMP-3) (Melanoma-associated antigen ME491) (OMA81H) (Ocular melanoma-associated antigen) (Tetraspanin-30) (Tspan-30) (CD antigen CD63)

 CD63_HUMAN              Reviewed;         238 AA.
P08962; F8VZE2; Q5TZP3; Q8N6Z9; Q9UCG6;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
18-JUL-2018, entry version 188.
RecName: Full=CD63 antigen;
AltName: Full=Granulophysin;
AltName: Full=Lysosomal-associated membrane protein 3;
Short=LAMP-3;
AltName: Full=Melanoma-associated antigen ME491;
AltName: Full=OMA81H;
AltName: Full=Ocular melanoma-associated antigen;
AltName: Full=Tetraspanin-30;
Short=Tspan-30;
AltName: CD_antigen=CD63;
Name=CD63; Synonyms=MLA1, TSPAN30;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3365686;
Hotta H., Ross A.H., Huebner K., Isobe M., Wendeborn S., Chao M.V.,
Ricciardi R.P., Tsujimoto Y., Croce C.M., Koprowski H.;
"Molecular cloning and characterization of an antigen associated with
early stages of melanoma tumor progression.";
Cancer Res. 48:2955-2962(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Ovary;
PubMed=2171551; DOI=10.1089/dna.1990.9.479;
Rapp G., Freudenstein J., Klaudiny J., Mucha J., Wempe F., Zimmer M.,
Scheit K.H.;
"Characterization of three abundant mRNAs from human ovarian granulosa
cells.";
DNA Cell Biol. 9:479-485(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
PubMed=1993697;
Metzelaar M.J., Wigngaard P.L., Peters P.J., Sixma J.J.,
Nieuwenhuis H.K., Clevers H.C.;
"CD63 antigen. A novel lysosomal membrane glycoprotein, cloned by a
screening procedure for intracellular antigens in eukaryotic cells.";
J. Biol. Chem. 266:3239-3245(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1339263; DOI=10.1001/archopht.1992.01080150097036;
Wang M.X., Earley J.J. Jr., Shields J.A., Donoso L.A.;
"An ocular melanoma-associated antigen. Molecular characterization.";
Arch. Ophthalmol. 110:399-404(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1599482; DOI=10.1016/S0006-291X(05)81004-6;
Hotta H., Miyamoto H., Hara I., Takahashi N., Homma M.;
"Genomic structure of the ME491/CD63 antigen gene and functional
analysis of the 5'-flanking regulatory sequences.";
Biochem. Biophys. Res. Commun. 185:436-442(1992).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Skin;
Ancans J., Suzuki I., Thody A.J.;
"Melanocyte variant of lysosome-associated membrane protein-3 (LAMP3;
also CD63 and melanoma associated antigen ME419) mRNA.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Muscle;
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).
[13]
PROTEIN SEQUENCE OF 2-38 (ISOFORM 1), SUBCELLULAR LOCATION, AND LACK
OF EXPRESSION IN HERMANSKY-PUDLAK SYNDROME.
TISSUE=Platelet;
PubMed=7682577; DOI=10.1172/JCI116388;
Nishibori M., Cham B., McNicol A., Shalev A., Jain N., Gerrard J.M.;
"The protein CD63 is in platelet dense granules, is deficient in a
patient with Hermansky-Pudlak syndrome, and appears identical to
granulophysin.";
J. Clin. Invest. 91:1775-1782(1993).
[14]
PROTEIN SEQUENCE OF 2-21 (ISOFORMS 1/2).
PubMed=4062294; DOI=10.1016/0003-9861(85)90241-3;
Ross A.H., Dietzschold B., Jackson D.M., Earley J.J., Ghrist B.F.D.,
Atkinson B., Koprowski H.;
"Isolation and amino terminal sequencing of a novel melanoma-
associated antigen.";
Arch. Biochem. Biophys. 242:540-548(1985).
[15]
SUBCELLULAR LOCATION.
PubMed=10793155; DOI=10.1091/mbc.11.5.1829;
Kobayashi T., Vischer U.M., Rosnoblet C., Lebrand C., Lindsay M.,
Parton R.G., Kruithof E.K.O., Gruenberg J.;
"The tetraspanin CD63/lamp3 cycles between endocytic and secretory
compartments in human endothelial cells.";
Mol. Biol. Cell 11:1829-1843(2000).
[16]
GLYCOSYLATION AT ASN-130.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[17]
SUBCELLULAR LOCATION.
PubMed=15351990; DOI=10.1002/cyto.a.20068;
Gruetzkau A., Smorodchenko A., Lippert U., Kirchhof L., Artuc M.,
Henz B.M.;
"LAMP-1 and LAMP-2, but not LAMP-3, are reliable markers for
activation-induced secretion of human mast cells.";
Cytometry 61:62-68(2004).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TIMP1 AND ITGB1.
PubMed=16917503; DOI=10.1038/sj.emboj.7601281;
Jung K.K., Liu X.W., Chirco R., Fridman R., Kim H.R.;
"Identification of CD63 as a tissue inhibitor of metalloproteinase-1
interacting cell surface protein.";
EMBO J. 25:3934-3942(2006).
[19]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Placenta;
PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
"Integral and associated lysosomal membrane proteins.";
Traffic 8:1676-1686(2007).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[21]
PALMITOYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION
WITH CD9, AND IDENTIFICATION IN A COMPLEX WITH ITGB3.
PubMed=19640571; DOI=10.1016/j.thromres.2009.07.005;
Israels S.J., McMillan-Ward E.M.;
"Palmitoylation supports the association of tetraspanin CD63 with CD9
and integrin alphaIIbbeta3 in activated platelets.";
Thromb. Res. 125:152-158(2010).
[22]
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).
[23]
FUNCTION IN CELL-CELL ADHESION, AND SUBCELLULAR LOCATION.
PubMed=21803846; DOI=10.1182/blood-2010-11-321489;
Doyle E.L., Ridger V., Ferraro F., Turmaine M., Saftig P.,
Cutler D.F.;
"CD63 is an essential cofactor to leukocyte recruitment by endothelial
P-selectin.";
Blood 118:4265-4273(2011).
[24]
FUNCTION IN MELANOCYTE DEVELOPMENT, SUBCELLULAR LOCATION, AND
INTERACTION WITH PMEL.
PubMed=21962903; DOI=10.1016/j.devcel.2011.08.019;
van Niel G., Charrin S., Simoes S., Romao M., Rochin L., Saftig P.,
Marks M.S., Rubinstein E., Raposo G.;
"The tetraspanin CD63 regulates ESCRT-independent and -dependent
endosomal sorting during melanogenesis.";
Dev. Cell 21:708-721(2011).
[25]
SUBCELLULAR LOCATION.
PubMed=22431521; DOI=10.1128/MCB.06726-11;
Mamo A., Jules F., Dumaresq-Doiron K., Costantino S., Lefrancois S.;
"The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in
endosomal sorting.";
Mol. Cell. Biol. 32:1855-1866(2012).
[26]
SUBCELLULAR LOCATION.
PubMed=22660413; DOI=10.1038/ncb2502;
Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G.,
Geeraerts A., Ivarsson Y., Depoortere F., Coomans C., Vermeiren E.,
Zimmermann P., David G.;
"Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
Nat. Cell Biol. 14:677-685(2012).
[27]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KDR.
PubMed=23632027; DOI=10.1074/jbc.M113.468199;
Tugues S., Honjo S., Konig C., Padhan N., Kroon J., Gualandi L.,
Li X., Barkefors I., Thijssen V.L., Griffioen A.W., Claesson-Welsh L.;
"Tetraspanin CD63 promotes vascular endothelial growth factor receptor
2-beta1 integrin complex formation, thereby regulating activation and
downstream signaling in endothelial cells in vitro and in vivo.";
J. Biol. Chem. 288:19060-19071(2013).
[28]
FUNCTION, AND INTERACTION WITH ITGB1.
PubMed=24635319; DOI=10.1042/BJ20131119;
Lee S.Y., Kim J.M., Cho S.Y., Kim H.S., Shin H.S., Jeon J.Y.,
Kausar R., Jeong S.Y., Lee Y.S., Lee M.A.;
"TIMP-1 modulates chemotaxis of human neural stem cells through CD63
and integrin signalling.";
Biochem. J. 459:565-576(2014).
[29]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Functions as cell surface receptor for TIMP1 and plays a
role in the activation of cellular signaling cascades. Plays a
role in the activation of ITGB1 and integrin signaling, leading to
the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell
survival, reorganization of the actin cytoskeleton, cell adhesion,
spreading and migration, via its role in the activation of AKT and
FAK/PTK2. Plays a role in VEGFA signaling via its role in
regulating the internalization of KDR/VEGFR2. Plays a role in
intracellular vesicular transport processes, and is required for
normal trafficking of the PMEL luminal domain that is essential
for the development and maturation of melanocytes. Plays a role in
the adhesion of leukocytes onto endothelial cells via its role in
the regulation of SELP trafficking. May play a role in mast cell
degranulation in response to Ms4a2/FceRI stimulation, but not in
mast cell degranulation in response to other stimuli.
{ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:21803846,
ECO:0000269|PubMed:21962903, ECO:0000269|PubMed:23632027,
ECO:0000269|PubMed:24635319}.
-!- SUBUNIT: Interacts with TIMP1 and ITGB1 and recruits TIMP1 to
ITGB1 (PubMed:16917503, PubMed:24635319). Interacts with CD9.
Identified in a complex with CD9 and ITGB3 (PubMed:19640571).
Interacts with PMEL (PubMed:21962903). Interacts with KDR/VEGFR2;
identified in a complex with ITGB1 and KDR/VEGFR2 and is required
to recruit KDR to ITGB1 complexes (PubMed:23632027). Interacts
with SYT7 (By similarity). {ECO:0000250|UniProtKB:P41731,
ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:19640571,
ECO:0000269|PubMed:21962903, ECO:0000269|PubMed:23632027,
ECO:0000269|PubMed:24635319}.
-!- INTERACTION:
P04578:env (xeno); NbExp=4; IntAct=EBI-762053, EBI-6179711;
P01033:TIMP1; NbExp=5; IntAct=EBI-762053, EBI-712536;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15351990,
ECO:0000269|PubMed:19640571, ECO:0000269|PubMed:23632027}; Multi-
pass membrane protein {ECO:0000255}. Lysosome membrane
{ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:19640571,
ECO:0000269|PubMed:1993697, ECO:0000269|PubMed:22431521,
ECO:0000269|PubMed:23632027}; Multi-pass membrane protein
{ECO:0000255}. Late endosome membrane
{ECO:0000269|PubMed:10793155, ECO:0000269|PubMed:23632027}; Multi-
pass membrane protein {ECO:0000255}. Endosome, multivesicular body
{ECO:0000269|PubMed:21962903}. Melanosome
{ECO:0000269|PubMed:21962903}. Secreted, exosome
{ECO:0000269|PubMed:22660413}. Cell surface
{ECO:0000269|PubMed:16917503, ECO:0000269|PubMed:23632027,
ECO:0000269|PubMed:24635319}. Note=Also found in Weibel-Palade
bodies of endothelial cells (PubMed:10793155). Located in platelet
dense granules (PubMed:7682577). Detected in a subset of pre-
melanosomes. Detected on intralumenal vesicles (ILVs) within
multivesicular bodies (PubMed:21962903).
{ECO:0000269|PubMed:10793155, ECO:0000269|PubMed:21962903,
ECO:0000269|PubMed:7682577}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P08962-1; Sequence=Displayed;
Name=2;
IsoId=P08962-2; Sequence=VSP_045300;
Name=3;
IsoId=P08962-3; Sequence=VSP_046996;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Detected in platelets (at protein level).
Dysplastic nevi, radial growth phase primary melanomas,
hematopoietic cells, tissue macrophages.
{ECO:0000269|PubMed:19640571}.
-!- PTM: Palmitoylated at a low, basal level in unstimulated
platelets. The level of palmitoylation increases when platelets
are activated by thrombin (in vitro).
{ECO:0000269|PubMed:19640571}.
-!- MISCELLANEOUS: Lack of expression of CD63 in platelets has been
observed in a patient with Hermansky-Pudlak syndrome (HPS).
Hermansky-Pudlak syndrome (HPS) is a genetically heterogeneous,
rare, autosomal recessive disorder characterized by oculocutaneous
albinism, bleeding due to platelet storage pool deficiency, and
lysosomal storage defects. This syndrome results from defects of
diverse cytoplasmic organelles including melanosomes, platelet
dense granules and lysosomes. Ceroid storage in the lungs is
associated with pulmonary fibrosis, a common cause of premature
death in individuals with HPS.
-!- MISCELLANEOUS: This antigen is associated with early stages of
melanoma tumor progression.
-!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
{ECO:0000305}.
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EMBL; X07982; CAA30792.1; -; mRNA.
EMBL; M59907; AAA63235.1; -; mRNA.
EMBL; M58485; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S93788; AAB21617.1; -; mRNA.
EMBL; X62654; CAA44519.1; -; Genomic_DNA.
EMBL; AF508304; AAM34259.1; -; mRNA.
EMBL; AK311893; BAG34834.1; -; mRNA.
EMBL; CR542096; CAG46893.1; -; mRNA.
EMBL; BT007073; AAP35736.1; -; mRNA.
EMBL; BT020137; AAV38939.1; -; mRNA.
EMBL; BT020138; AAV38940.1; -; mRNA.
EMBL; AC009779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96827.1; -; Genomic_DNA.
EMBL; BC002349; AAH02349.1; -; mRNA.
EMBL; BC013017; AAH13017.1; -; mRNA.
CCDS; CCDS58242.1; -. [P08962-3]
CCDS; CCDS58243.1; -. [P08962-2]
CCDS; CCDS8890.1; -. [P08962-1]
PIR; I38016; I38016.
RefSeq; NP_001244318.1; NM_001257389.1. [P08962-1]
RefSeq; NP_001244319.1; NM_001257390.1. [P08962-1]
RefSeq; NP_001244320.1; NM_001257391.1. [P08962-1]
RefSeq; NP_001244321.1; NM_001257392.1. [P08962-2]
RefSeq; NP_001244329.1; NM_001257400.1. [P08962-3]
RefSeq; NP_001244330.1; NM_001257401.1. [P08962-3]
RefSeq; NP_001254627.1; NM_001267698.1. [P08962-1]
RefSeq; NP_001771.1; NM_001780.5. [P08962-1]
UniGene; Hs.445570; -.
ProteinModelPortal; P08962; -.
BioGrid; 107405; 37.
CORUM; P08962; -.
IntAct; P08962; 20.
MINT; P08962; -.
STRING; 9606.ENSP00000257857; -.
BindingDB; P08962; -.
ChEMBL; CHEMBL3713303; -.
TCDB; 8.A.40.1.19; the tetraspanin (tetraspanin) family.
iPTMnet; P08962; -.
PhosphoSitePlus; P08962; -.
SwissPalm; P08962; -.
BioMuta; CD63; -.
DMDM; 116026; -.
EPD; P08962; -.
MaxQB; P08962; -.
PaxDb; P08962; -.
PeptideAtlas; P08962; -.
PRIDE; P08962; -.
ProteomicsDB; 52180; -.
DNASU; 967; -.
Ensembl; ENST00000257857; ENSP00000257857; ENSG00000135404. [P08962-1]
Ensembl; ENST00000420846; ENSP00000393502; ENSG00000135404. [P08962-1]
Ensembl; ENST00000546939; ENSP00000447356; ENSG00000135404. [P08962-3]
Ensembl; ENST00000549117; ENSP00000447730; ENSG00000135404. [P08962-1]
Ensembl; ENST00000550776; ENSP00000448091; ENSG00000135404. [P08962-3]
Ensembl; ENST00000552692; ENSP00000449337; ENSG00000135404. [P08962-1]
Ensembl; ENST00000552754; ENSP00000446807; ENSG00000135404. [P08962-2]
GeneID; 967; -.
KEGG; hsa:967; -.
UCSC; uc001shn.5; human. [P08962-1]
CTD; 967; -.
DisGeNET; 967; -.
EuPathDB; HostDB:ENSG00000135404.11; -.
GeneCards; CD63; -.
HGNC; HGNC:1692; CD63.
HPA; CAB026356; -.
HPA; HPA010088; -.
MIM; 155740; gene.
neXtProt; NX_P08962; -.
OpenTargets; ENSG00000135404; -.
PharmGKB; PA26231; -.
eggNOG; KOG3882; Eukaryota.
eggNOG; ENOG4111IRY; LUCA.
GeneTree; ENSGT00880000137851; -.
HOGENOM; HOG000230651; -.
HOVERGEN; HBG107306; -.
InParanoid; P08962; -.
KO; K06497; -.
OMA; AFGCCGA; -.
OrthoDB; EOG091G12WV; -.
PhylomeDB; P08962; -.
TreeFam; TF316345; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; CD63; human.
GeneWiki; CD63; -.
GenomeRNAi; 967; -.
PRO; PR:P08962; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135404; -.
CleanEx; HS_CD63; -.
ExpressionAtlas; P08962; baseline and differential.
Genevisible; P08962; HS.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0031904; C:endosome lumen; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0032585; C:multivesicular body membrane; IDA:UniProtKB.
GO; GO:0097487; C:multivesicular body, internal vesicle; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031088; C:platelet dense granule membrane; TAS:Reactome.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0034613; P:cellular protein localization; IDA:MGI.
GO; GO:0035646; P:endosome to melanosome transport; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0048757; P:pigment granule maturation; IMP:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0002092; P:positive regulation of receptor internalization; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:MGI.
GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; IMP: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;
Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Endosome; Glycoprotein; Lipoprotein;
Lysosome; Membrane; Palmitate; Protein transport; Reference proteome;
Secreted; Transmembrane; Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:25944712}.
CHAIN 2 238 CD63 antigen.
/FTId=PRO_0000219216.
TOPO_DOM 2 11 Cytoplasmic. {ECO:0000255}.
TRANSMEM 12 32 Helical. {ECO:0000255}.
TOPO_DOM 33 51 Extracellular. {ECO:0000255}.
TRANSMEM 52 72 Helical. {ECO:0000255}.
TOPO_DOM 73 81 Cytoplasmic. {ECO:0000255}.
TRANSMEM 82 102 Helical. {ECO:0000255}.
TOPO_DOM 103 203 Extracellular. {ECO:0000255}.
TRANSMEM 204 224 Helical. {ECO:0000255}.
TOPO_DOM 225 238 Cytoplasmic. {ECO:0000255}.
MOTIF 234 238 Lysosomal targeting motif.
{ECO:0000250|UniProtKB:P41731}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 82 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_046996.
VAR_SEQ 23 45 Missing (in isoform 2).
{ECO:0000303|Ref.6}.
/FTId=VSP_045300.
CONFLICT 36 36 Q -> E (in Ref. 13; AA sequence).
{ECO:0000305}.
SEQUENCE 238 AA; 25637 MW; 85AC8E235C6E425F CRC64;
MAVEGGMKCV KFLLYVLLLA FCACAVGLIA VGVGAQLVLS QTIIQGATPG SLLPVVIIAV
GVFLFLVAFV GCCGACKENY CLMITFAIFL SLIMLVEVAA AIAGYVFRDK VMSEFNNNFR
QQMENYPKNN HTASILDRMQ ADFKCCGAAN YTDWEKIPSM SKNRVPDSCC INVTVGCGIN
FNEKAIHKEG CVEKIGGWLR KNVLVVAAAA LGIAFVEVLG IVFACCLVKS IRSGYEVM


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