CD63_RAT
ID CD63_RAT Reviewed; 238 AA.
AC P28648;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=CD63 antigen;
DE AltName: Full=Mast cell antigen AD1;
DE AltName: CD_antigen=CD63;
GN Name=Cd63;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1634775;
RA Nishikata H., Oliver C., Mergenhagen S.E., Siraganian R.P.;
RT "The rat mast cell antigen AD1 (homologue to human CD63 or melanoma antigen
RT ME491) is expressed in other cells in culture.";
RL J. Immunol. 149:862-870(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [3]
RP PROTEIN SEQUENCE OF 2-44, AND SUBCELLULAR LOCATION.
RX PubMed=1703158; DOI=10.1016/s0021-9258(18)52378-4;
RA Kitani S., Berenstein E., Mergenhagen S.E., Tempst P., Siraganian R.P.;
RT "A cell surface glycoprotein of rat basophilic leukemia cells close to the
RT high affinity IgE receptor (Fc epsilon RI). Similarity to human melanoma
RT differentiation antigen ME491.";
RL J. Biol. Chem. 266:1903-1909(1991).
RN [4]
RP PROTEIN SEQUENCE OF 183-200, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
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 -!- INTERACTION:
CC P28648; Q03348: Ptpra; NbExp=5; IntAct=EBI-7784314, EBI-7784341;
CC P28648; Q9WUD9: Src; NbExp=2; IntAct=EBI-7784314, EBI-7784541;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1634775};
CC Multi-pass membrane protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000269|PubMed:1634775}; Multi-pass membrane protein. Late
CC endosome membrane {ECO:0000250|UniProtKB:P08962}; Multi-pass membrane
CC protein {ECO:0000255}. Endosome, multivesicular body
CC {ECO:0000250|UniProtKB:P08962}. Melanosome
CC {ECO:0000250|UniProtKB:P08962}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P08962}. Cell surface
CC {ECO:0000269|PubMed:1703158}. 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 -!- TISSUE SPECIFICITY: Detected in mast cells and platelets (at protein
CC level). {ECO:0000269|PubMed:1634775}.
CC -!- DEVELOPMENTAL STAGE: Increased expression in embryonal tissues.
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; X61654; CAA43835.1; -; mRNA.
DR EMBL; BC063173; AAH63173.1; -; mRNA.
DR PIR; A46508; A46508.
DR RefSeq; NP_058821.1; NM_017125.3.
DR RefSeq; XP_008763247.1; XM_008765025.2.
DR AlphaFoldDB; P28648; -.
DR SMR; P28648; -.
DR IntAct; P28648; 2.
DR MINT; P28648; -.
DR STRING; 10116.ENSRNOP00000010180; -.
DR GlyGen; P28648; 3 sites.
DR jPOST; P28648; -.
DR PaxDb; P28648; -.
DR PRIDE; P28648; -.
DR Ensembl; ENSRNOT00000010180; ENSRNOP00000010180; ENSRNOG00000007650.
DR GeneID; 29186; -.
DR KEGG; rno:29186; -.
DR UCSC; RGD:62080; rat.
DR CTD; 967; -.
DR RGD; 62080; Cd63.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000156832; -.
DR HOGENOM; CLU_055524_6_1_1; -.
DR InParanoid; P28648; -.
DR PhylomeDB; P28648; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P28648; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007650; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; P28648; baseline and differential.
DR Genevisible; P28648; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031904; C:endosome lumen; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
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:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
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:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
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:0030855; P:epithelial cell differentiation; IMP:RGD.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:RGD.
DR GO; GO:0050931; P:pigment cell differentiation; ISO:RGD.
DR GO; GO:0048757; P:pigment granule maturation; ISS:UniProtKB.
DR GO; GO:0043473; P:pigmentation; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
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:1901379; P:regulation of potassium ion transmembrane transport; ISO:RGD.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Endosome; Glycoprotein;
KW Lipoprotein; Lysosome; Membrane; Palmitate; Protein transport;
KW Reference proteome; Secreted; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1703158"
FT CHAIN 2..238
FT /note="CD63 antigen"
FT /id="PRO_0000219219"
FT TOPO_DOM 2..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 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; 25699 MW; B6F8C8B69E766690 CRC64;
MAVEGGMKCV KFLLYVLLLA FCACAVGLIA IGVAVQVVLK QAITHETTAG SLLPVVIIAV
GAFLFLVAFV GCCGACKENY CLMITFAIFL SLIMLVEVAV AIAGYVFRDQ VKSEFSKSFQ
KQMQNYLTDN KTATILDKLQ KENKCCGASN YTDWERIPGM AKDRVPDSCC INITVGCGND
FKESTIHTQG CVETIAAWLR KNVLLVAGAA LGIAFVEVLG IIFSCCLVKS IRSGYEVM
