Cd63
entrez
12512
canonical
uniprot
P41731
canonical
ensembl
ENSMUSG00000025351
resolver
ensp
ENSMUSP00000026407
resolver
ensp
ENSMUSP00000100862
resolver
ensp
ENSMUSP00000151313
resolver
ensp
ENSMUSP00000205840
resolver
ensp
ENSMUSP00000205843
resolver
ensp
ENSMUSP00000205844
resolver
ensp
ENSMUSP00000345768
resolver
enst
ENSMUST00000026407
resolver
enst
ENSMUST00000105229
resolver
enst
ENSMUST00000219317
resolver
genesymbol
Cd63
resolver
uniprot
Q549D0
resolver
uniprot_entry
CD63_MOUSE
resolver
uniprot_entry
Q549D0_MOUSE
resolver
amino_acid_sequence
MAVEGGMKCVKFLLYVLLLAFCACAVGLIAIGVAVQVVLKQAITHETTAGSLLPVVIIAVGAFLFLVAFVGCCGACKENYCLMITFAIFLSLIMLVEVAVAIAGYVFRDQVKSEFNKSFQQQMQNYLKDNKTATILDKLQKENNCCGASNYTDWENIPGMAKDRVPDSCCINITVGCGNDFKESTIHTQGCVETIAIWLRKNILLVAAAALGIAFVEVLGIIFSCCLVKSIRSGYEVM
uniprot
proteins
function
FUNCTION: Functions as a 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:19075008, ECO:0000269|PubMed:21803846, ECO:0000269|PubMed:21962903, ECO:0000269|PubMed:23632027, ECO:0000269|PubMed:23945142}.
uniprot
proteins
mass_dalton
25767
uniprot
proteins
mutagenesis
MUTAGEN 235; /note="Y->A: Abolishes localization to lysosomes."; /evidence="ECO:0000269|PubMed:21041449
uniprot
proteins
post_translational_modification
PTM: Palmitoylated at a low, basal level in unstimulated platelets. The level of palmitoylation increases when platelets are activated by thrombin (in vitro) (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
Tetraspanin (TM4SF) family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19075008
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
21041449
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21803846
uniprot
proteins
pubmed
21962903
uniprot
proteins
pubmed
23632027
uniprot
proteins
pubmed
23945142
uniprot
proteins
pubmed
26109643
uniprot
proteins
pubmed
8148377
uniprot
proteins
sequence_length
238
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08962}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19075008, ECO:0000269|PubMed:21041449, ECO:0000269|PubMed:23945142}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:23945142}; Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P08962}. Melanosome {ECO:0000250|UniProtKB:P08962}. Secreted, extracellular exosome {ECO:0000269|PubMed:26109643}. Cell surface {ECO:0000250|UniProtKB:P08962}. Note=Also found in Weibel-Palade bodies of endothelial cells. Located in platelet dense granules. Detected in a subset of pre-melanosomes. Detected on intralumenal vesicles (ILVs) within multivesicular bodies. {ECO:0000250|UniProtKB:P08962}.
uniprot
proteins
transmembrane_region
TRANSMEM 12..32; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 52..72; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 82..102; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 204..224; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins