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Protein

CD63 antigen

Gene

Cd63

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_307071. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
CD63 antigen
Alternative name(s):
CD_antigen: CD63
Gene namesi
Name:Cd63
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:99529. Cd63.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1110CytoplasmicSequence Analysis
Transmembranei12 – 3221HelicalSequence AnalysisAdd
BLAST
Topological domaini33 – 5119ExtracellularSequence AnalysisAdd
BLAST
Transmembranei52 – 7221HelicalSequence AnalysisAdd
BLAST
Topological domaini73 – 819CytoplasmicSequence Analysis
Transmembranei82 – 10221HelicalSequence AnalysisAdd
BLAST
Topological domaini103 – 203101ExtracellularSequence AnalysisAdd
BLAST
Transmembranei204 – 22421HelicalSequence AnalysisAdd
BLAST
Topological domaini225 – 23814CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Lysosome, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mutant mice are viable and fertile, but display impaired water homeostasis, with increased urinary flow, increased water intake, reduced urine osmolality and increased fecal water content. Mice display inclusions in the principal cells in the renal collecting duct (PubMed:19075008). Mutant mice display variable graying of their coat color and a dramatic reduction in the number of melanosomes in the retinal pigment epithelium (PubMed:21962903). According to PubMed:21803846, mutant mice display a defect in the Selp-dependent attachment of leukocytes to endothelial cells. According to PubMed:23945142, mast cells from mutant mice show decreased degranulation and decreased release of TNF in response to Ms4a2/FceRI stimulation, but no difference in mast cell degranulation in response to other stimuli and no change in the release of IL6 and leukotriene C4.5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 238237CD63 antigenPRO_0000219217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi130 – 1301N-linked (GlcNAc...)1 Publication
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Palmitoylated at a low, basal level in unstimulated platelets. The level of palmitoylation increases when platelets are activated by thrombin (in vitro) (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

MaxQBiP41731.
PaxDbiP41731.
PRIDEiP41731.

PTM databases

PhosphoSiteiP41731.

Expressioni

Tissue specificityi

Ubiquitous. Strongly expressed in kidney. Detected in spleen, bone marrow, peripheral blood mononuclear cells and macrophages.

Gene expression databases

BgeeiP41731.
CleanExiMM_CD63.
ExpressionAtlasiP41731. baseline and differential.

Interactioni

Subunit structurei

Interacts with TIMP1 and ITGB1 and recruits TIMP1 to ITGB1. Interacts with CD9. Identified in a complex with CD9 and ITGB3. Interacts with PMEL. Interacts with KDR/VEGFR2; identified in a complex with ITGB1 and KDR/VEGFR2 and is required to recruit KDR to ITGB1 complexes (By similarity).By similarity

Protein-protein interaction databases

IntActiP41731. 2 interactions.
STRINGi10090.ENSMUSP00000026407.

Structurei

3D structure databases

ProteinModelPortaliP41731.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tetraspanin (TM4SF) family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG268658.
HOVERGENiHBG107306.
InParanoidiP41731.
KOiK06497.
OMAiVTQGCGI.
OrthoDBiEOG73BVDM.
TreeFamiTF316345.

Family and domain databases

InterProiIPR000301. Tetraspanin.
IPR018499. Tetraspanin/Peripherin.
IPR018503. Tetraspanin_CS.
IPR008952. Tetraspanin_EC2.
[Graphical view]
PfamiPF00335. Tetraspannin. 1 hit.
[Graphical view]
PIRSFiPIRSF002419. Tetraspanin. 1 hit.
PRINTSiPR00259. TMFOUR.
SUPFAMiSSF48652. SSF48652. 1 hit.
PROSITEiPS00421. TM4_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P41731-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVEGGMKCV KFLLYVLLLA FCACAVGLIA IGVAVQVVLK QAITHETTAG
60 70 80 90 100
SLLPVVIIAV GAFLFLVAFV GCCGACKENY CLMITFAIFL SLIMLVEVAV
110 120 130 140 150
AIAGYVFRDQ VKSEFNKSFQ QQMQNYLKDN KTATILDKLQ KENNCCGASN
160 170 180 190 200
YTDWENIPGM AKDRVPDSCC INITVGCGND FKESTIHTQG CVETIAIWLR
210 220 230
KNILLVAAAA LGIAFVEVLG IIFSCCLVKS IRSGYEVM
Length:238
Mass (Da):25,767
Last modified:January 23, 2007 - v2
Checksum:iB57E47B31E13EED8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16432 mRNA. Translation: BAA03904.1.
BC008108 mRNA. Translation: AAH08108.1.
BC012212 mRNA. Translation: AAH12212.1.
BC083161 mRNA. Translation: AAH83161.1.
CCDSiCCDS24297.1.
PIRiS43511.
RefSeqiNP_001036045.1. NM_001042580.1.
NP_001269895.1. NM_001282966.1.
NP_031679.1. NM_007653.3.
UniGeneiMm.371552.
Mm.416079.

Genome annotation databases

EnsembliENSMUST00000026407; ENSMUSP00000026407; ENSMUSG00000025351.
ENSMUST00000105229; ENSMUSP00000100862; ENSMUSG00000025351.
GeneIDi12512.
KEGGimmu:12512.
UCSCiuc007hou.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16432 mRNA. Translation: BAA03904.1.
BC008108 mRNA. Translation: AAH08108.1.
BC012212 mRNA. Translation: AAH12212.1.
BC083161 mRNA. Translation: AAH83161.1.
CCDSiCCDS24297.1.
PIRiS43511.
RefSeqiNP_001036045.1. NM_001042580.1.
NP_001269895.1. NM_001282966.1.
NP_031679.1. NM_007653.3.
UniGeneiMm.371552.
Mm.416079.

3D structure databases

ProteinModelPortaliP41731.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP41731. 2 interactions.
STRINGi10090.ENSMUSP00000026407.

PTM databases

PhosphoSiteiP41731.

Proteomic databases

MaxQBiP41731.
PaxDbiP41731.
PRIDEiP41731.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026407; ENSMUSP00000026407; ENSMUSG00000025351.
ENSMUST00000105229; ENSMUSP00000100862; ENSMUSG00000025351.
GeneIDi12512.
KEGGimmu:12512.
UCSCiuc007hou.1. mouse.

Organism-specific databases

CTDi967.
MGIiMGI:99529. Cd63.

Phylogenomic databases

eggNOGiNOG268658.
HOVERGENiHBG107306.
InParanoidiP41731.
KOiK06497.
OMAiVTQGCGI.
OrthoDBiEOG73BVDM.
TreeFamiTF316345.

Enzyme and pathway databases

ReactomeiREACT_307071. Platelet degranulation.

Miscellaneous databases

NextBioi281496.
PROiP41731.
SOURCEiSearch...

Gene expression databases

BgeeiP41731.
CleanExiMM_CD63.
ExpressionAtlasiP41731. baseline and differential.

Family and domain databases

InterProiIPR000301. Tetraspanin.
IPR018499. Tetraspanin/Peripherin.
IPR018503. Tetraspanin_CS.
IPR008952. Tetraspanin_EC2.
[Graphical view]
PfamiPF00335. Tetraspannin. 1 hit.
[Graphical view]
PIRSFiPIRSF002419. Tetraspanin. 1 hit.
PRINTSiPR00259. TMFOUR.
SUPFAMiSSF48652. SSF48652. 1 hit.
PROSITEiPS00421. TM4_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the murine homologue of CD63/ME491 and detection of its strong expression in the kidney and activated macrophages."
    Miyamoto M., Homma M., Hotta H.
    Biochim. Biophys. Acta 1217:312-316(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon and Mammary gland.
  3. "Deficiency of the tetraspanin CD63 associated with kidney pathology but normal lysosomal function."
    Schroder J., Lullmann-Rauch R., Himmerkus N., Pleines I., Nieswandt B., Orinska Z., Koch-Nolte F., Schroder B., Bleich M., Saftig P.
    Mol. Cell. Biol. 29:1083-1094(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION.
  4. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130.
  5. "CD63 is an essential cofactor to leukocyte recruitment by endothelial P-selectin."
    Doyle E.L., Ridger V., Ferraro F., Turmaine M., Saftig P., Cutler D.F.
    Blood 118:4265-4273(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  6. "The tetraspanin CD63 regulates ESCRT-independent and -dependent endosomal sorting during melanogenesis."
    van Niel G., Charrin S., Simoes S., Romao M., Rochin L., Saftig P., Marks M.S., Rubinstein E., Raposo G.
    Dev. Cell 21:708-721(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MELANOCYTE DEVELOPMENT, DISRUPTION PHENOTYPE.
  7. "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."
    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.
    J. Biol. Chem. 288:19060-19071(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "The tetraspanin CD63 is required for efficient IgE-mediated mast cell degranulation and anaphylaxis."
    Kraft S., Jouvin M.H., Kulkarni N., Kissing S., Morgan E.S., Dvorak A.M., Schroder B., Saftig P., Kinet J.P.
    J. Immunol. 191:2871-2878(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCD63_MOUSE
AccessioniPrimary (citable) accession number: P41731
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.