(data stored in ACNUC1829 zone)

SWISSPROT: CD63_BOVIN

ID   CD63_BOVIN              Reviewed;         237 AA.
AC   Q9XSK2; Q3SZY2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   30-AUG-2017, entry version 116.
DE   RecName: Full=CD63 antigen;
DE   AltName: CD_antigen=CD63;
GN   Name=CD63;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Peripheral blood;
RX   PubMed=10398809; DOI=10.1007/s002510050556;
RA   Brooke G.P., Sopp P., Kwong L.S., Howard C.J.;
RT   "Molecular cloning of cattle CD63 and evidence for high level
RT   expression on subpopulations of dendritic cells.";
RL   Immunogenetics 49:812-814(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as cell surface receptor for TIMP1 and plays a
CC       role in the activation of cellular signaling cascades. Plays a
CC       role in the activation of ITGB1 and integrin signaling, leading to
CC       the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell
CC       survival, reorganization of the actin cytoskeleton, cell adhesion,
CC       spreading and migration, via its role in the activation of AKT and
CC       FAK/PTK2. Plays a role in VEGFA signaling via its role in
CC       regulating the internalization of KDR/VEGFR2. Plays a role in
CC       intracellular vesicular transport processes, and is required for
CC       normal trafficking of the PMEL luminal domain that is essential
CC       for the development and maturation of melanocytes. Plays a role in
CC       the adhesion of leukocytes onto endothelial cells via its role in
CC       the regulation of SELP trafficking. May play a role in mast cell
CC       degranulation in response to Ms4a2/FceRI stimulation, but not in
CC       mast cell degranulation in response to other stimuli (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TIMP1 and ITGB1 and recruits TIMP1 to
CC       ITGB1. Interacts with CD9. Identified in a complex with CD9 and
CC       ITGB3. Interacts with PMEL. Interacts with KDR/VEGFR2; identified
CC       in a complex with ITGB1 and KDR/VEGFR2 and is required to recruit
CC       KDR to ITGB1 complexes. Interacts with SYT7 (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P41731}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P08962}; Multi-pass membrane protein
CC       {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P08962};
CC       Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
CC       {ECO:0000250|UniProtKB:P08962}; Multi-pass membrane protein
CC       {ECO:0000255}. Endosome, multivesicular body
CC       {ECO:0000250|UniProtKB:P08962}. Melanosome
CC       {ECO:0000250|UniProtKB:P08962}. Secreted, exosome
CC       {ECO:0000250|UniProtKB:P08962}. Cell surface
CC       {ECO:0000250|UniProtKB:P08962}. Note=Also found in Weibel-Palade
CC       bodies of endothelial cells. Located in platelet dense granules.
CC       Detected in a subset of pre-melanosomes. Detected on intralumenal
CC       vesicles (ILVs) within multivesicular bodies.
CC       {ECO:0000250|UniProtKB:P08962}.
CC   -!- PTM: Palmitoylated at a low, basal level in unstimulated
CC       platelets. The level of palmitoylation increases when platelets
CC       are activated by thrombin (in vitro) (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
CC       {ECO:0000305}.
DR   EMBL; AJ012589; CAB40564.1; -; mRNA.
DR   EMBL; BC102657; AAI02658.1; -; mRNA.
DR   RefSeq; NP_991372.1; NM_205803.1.
DR   UniGene; Bt.13496; -.
DR   STRING; 9913.ENSBTAP00000015829; -.
DR   PaxDb; Q9XSK2; -.
DR   PRIDE; Q9XSK2; -.
DR   Ensembl; ENSBTAT00000015829; ENSBTAP00000015829; ENSBTAG00000011931.
DR   GeneID; 404156; -.
DR   KEGG; bta:404156; -.
DR   CTD; 967; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   eggNOG; ENOG4111IRY; LUCA.
DR   GeneTree; ENSGT00880000137851; -.
DR   HOGENOM; HOG000230651; -.
DR   HOVERGEN; HBG107306; -.
DR   InParanoid; Q9XSK2; -.
DR   KO; K06497; -.
DR   OMA; CFACCLS; -.
DR   OrthoDB; EOG091G12WV; -.
DR   TreeFam; TF352891; -.
DR   Reactome; R-BTA-114608; Platelet degranulation.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000011931; -.
DR   ExpressionAtlas; Q9XSK2; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0097487; C:multivesicular body, internal vesicle; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
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:0045807; P:positive regulation of endocytosis; IBA:GO_Central.
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   Gene3D; 1.10.1450.10; -; 1.
DR   InterPro; IPR000301; Tetraspanin.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR018503; Tetraspanin_CS.
DR   InterPro; IPR008952; Tetraspanin_EC2.
DR   Pfam; PF00335; Tetraspannin; 1.
DR   PIRSF; PIRSF002419; Tetraspanin; 1.
DR   PRINTS; PR00259; TMFOUR.
DR   SUPFAM; SSF48652; SSF48652; 1.
DR   PROSITE; PS00421; TM4_1; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q9XSK2.
DR   SWISS-2DPAGE; Q9XSK2.
KW   Cell membrane; Complete proteome; Endosome; Glycoprotein; Lipoprotein;
KW   Lysosome; Membrane; Palmitate; Protein transport; Reference proteome;
KW   Secreted; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    237       CD63 antigen.
FT                                /FTId=PRO_0000219215.
FT   TOPO_DOM      1     11       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     12     32       Helical. {ECO:0000255}.
FT   TOPO_DOM     33     51       Extracellular. {ECO:0000255}.
FT   TRANSMEM     52     72       Helical. {ECO:0000255}.
FT   TOPO_DOM     73     81       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     82    102       Helical. {ECO:0000255}.
FT   TOPO_DOM    103    202       Extracellular. {ECO:0000255}.
FT   TRANSMEM    203    223       Helical. {ECO:0000255}.
FT   TOPO_DOM    224    237       Cytoplasmic. {ECO:0000255}.
FT   MOTIF       233    237       Lysosomal targeting motif.
FT                                {ECO:0000250|UniProtKB:P41731}.
FT   CARBOHYD     40     40       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    150    150       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    171    171       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT    206    206       A -> V (in Ref. 1; CAB40564).
FT                                {ECO:0000305}.
SQ   SEQUENCE   237 AA;  25752 MW;  81F7C2CD12760AF3 CRC64;
     MAVEGGMKCV KFLLYVLLLV FCACAVGLIA VGVGTHLVLN QTITHGATPS FLLPVVIIAV
     GAFLFLVAFV GCCGACKENY CLMITFAIFL SLIMLVEVAA AIAGYVFRDK VRSEFNKDFR
     QQMKNYPKDN QTASILDKMQ KDFECCGAAN YTDWEKILAV TNKVPDSCCV NITHNCGINF
     VVKDIHTEGC VEKIAAWLRK NVLVVAAAAL GIAFVEILGI VLACCLVKSI RSGYEVM
//

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