CD63_RABIT
ID CD63_RABIT Reviewed; 238 AA.
AC Q28709;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=CD63 antigen;
DE AltName: CD_antigen=CD63;
GN Name=CD63;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aorta;
RX PubMed=7820873; DOI=10.1247/csf.19.219;
RA Sohma Y., Suzuki T., Sasano H., Nagura H., Nose M., Yamamoto T.;
RT "Increased mRNA for CD63 antigen in atherosclerotic lesions of Watanabe
RT heritable hyperlipidemic rabbits.";
RL Cell Struct. Funct. 19:219-225(1994).
CC -!- FUNCTION: Functions as cell surface receptor for TIMP1 and plays a role
CC in the activation of cellular signaling cascades. Plays a role in the
CC activation of ITGB1 and integrin signaling, leading to the activation
CC of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival,
CC reorganization of the actin cytoskeleton, cell adhesion, spreading and
CC migration, via its role in the activation of AKT and FAK/PTK2. Plays a
CC role in VEGFA signaling via its role in regulating the internalization
CC of KDR/VEGFR2. Plays a role in intracellular vesicular transport
CC processes, and is required for normal trafficking of the PMEL luminal
CC domain that is essential for the development and maturation of
CC melanocytes. Plays a role in the adhesion of leukocytes onto
CC endothelial cells via its role in the regulation of SELP trafficking.
CC May play a role in mast cell degranulation in response to Ms4a2/FceRI
CC stimulation, but not in mast cell degranulation in response to other
CC stimuli (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TIMP1 and ITGB1 and recruits TIMP1 to ITGB1.
CC Interacts with CD9. Identified in a complex with CD9 and ITGB3.
CC Interacts with PMEL. Interacts with KDR/VEGFR2; identified in a complex
CC with ITGB1 and KDR/VEGFR2 and is required to recruit KDR to ITGB1
CC complexes. Interacts with SYT7 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P41731}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08962};
CC Multi-pass membrane protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P08962}; Multi-pass membrane protein
CC {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:P08962};
CC Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular
CC body {ECO:0000250|UniProtKB:P08962}. Melanosome
CC {ECO:0000250|UniProtKB:P08962}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P08962}. Cell surface
CC {ECO:0000250|UniProtKB:P08962}. Note=Also found in Weibel-Palade bodies
CC of endothelial cells. Located in platelet dense granules. Detected in a
CC subset of pre-melanosomes. Detected on intralumenal vesicles (ILVs)
CC within multivesicular bodies. {ECO:0000250|UniProtKB:P08962}.
CC -!- PTM: Palmitoylated at a low, basal level in unstimulated platelets. The
CC level of palmitoylation increases when platelets are activated by
CC thrombin (in vitro) (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; D21264; BAA04804.1; -; mRNA.
DR PIR; JC2297; JC2297.
DR RefSeq; NP_001075668.1; NM_001082199.1.
DR AlphaFoldDB; Q28709; -.
DR SMR; Q28709; -.
DR STRING; 9986.ENSOCUP00000018861; -.
DR GeneID; 100008988; -.
DR KEGG; ocu:100008988; -.
DR CTD; 967; -.
DR InParanoid; Q28709; -.
DR OrthoDB; 1467737at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; ISS:UniProtKB.
DR GO; GO:0097487; C:multivesicular body, internal vesicle; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0035646; P:endosome to melanosome transport; ISS:UniProtKB.
DR GO; GO:0048757; P:pigment granule maturation; ISS:UniProtKB.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
DR CDD; cd03166; CD63_LEL; 1.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR042028; CD63_LEL.
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 2: Evidence at transcript level;
KW Cell membrane; Endosome; Glycoprotein; Lipoprotein; Lysosome; Membrane;
KW Palmitate; Protein transport; Reference proteome; Secreted; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..238
FT /note="CD63 antigen"
FT /id="PRO_0000219218"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..51
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 234..238
FT /note="Lysosomal targeting motif"
FT /evidence="ECO:0000250|UniProtKB:P41731"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 238 AA; 25630 MW; 8F24E20C4A49EDA8 CRC64;
MAVEGGMKCV KFLLYVLLLA FCACAVGLIA VGVGAQLVLS QTITHGATPG SLLPVVIIAV
GAFLFLVAFV GCCGTCKENY CLMITFAIFL SLIMLVEVAA AIAGYVFRDK VMSEFNKDFR
QQMQNYSTDN QTALILDRMQ KDFTCCGAAN YTDWATIPGM TRDRVPDSCC VNVTSGCGVK
FNVKDIYVEG CVEKIGLWLR KNVLVVAAAA LGIAFVEVLG IVFACCLVKS IRSGYEVM
