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CD9 antigen (CD antigen CD9)

 CD9_FELCA               Reviewed;         226 AA.
P40239;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 105.
RecName: Full=CD9 antigen;
AltName: CD_antigen=CD9;
Name=CD9;
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=7753050; DOI=10.1016/0161-5890(95)00008-3;
Willett B.J., Neil J.C.;
"cDNA cloning and eukaryotic expression of feline CD9.";
Mol. Immunol. 32:417-423(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Morikawa S.;
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in platelet activation and aggregation.
Regulates paranodal junction formation. Involved in cell adhesion,
cell motility and tumor metastasis. Required for sperm-egg fusion
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Forms both disulfide-linked homodimers and higher
homooligomers as well as heterooligomers with other members of the
tetraspanin family. Interacts with CD63. Identified in a complex
with CD63 and ITGB3. Associates with CR2/CD21 and with
PTGFRN/CD9P1. Interacts directly with IGSF8 (By similarity).
Interacts with PDPN; this interaction is homophilic and attenuates
platelet aggregation and pulmonary metastasis induced by PDPN (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P21926}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7753050};
Multi-pass membrane protein {ECO:0000269|PubMed:7753050}. Cell
membrane {ECO:0000269|PubMed:7753050}; Multi-pass membrane protein
{ECO:0000269|PubMed:7753050}.
-!- 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}.
-!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
{ECO:0000305}.
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EMBL; L35275; AAA92867.1; -; mRNA.
EMBL; D30786; BAA06452.1; -; mRNA.
RefSeq; NP_001009305.1; NM_001009305.1.
ProteinModelPortal; P40239; -.
STRING; 9685.ENSFCAP00000006372; -.
GeneID; 493874; -.
KEGG; fca:493874; -.
CTD; 928; -.
eggNOG; KOG3882; Eukaryota.
eggNOG; ENOG4111IRY; LUCA.
HOGENOM; HOG000230651; -.
HOVERGEN; HBG002324; -.
InParanoid; P40239; -.
KO; K06460; -.
TreeFam; TF352895; -.
Proteomes; UP000011712; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; ISS:UniProtKB.
GO; GO:0006928; P:movement of cell or subcellular component; ISS:UniProtKB.
GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0030913; P:paranodal junction assembly; ISS:UniProtKB.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
Gene3D; 1.10.1450.10; -; 1.
InterPro; IPR000301; Tetraspanin.
InterPro; IPR018499; Tetraspanin/Peripherin.
InterPro; IPR018503; Tetraspanin_CS.
InterPro; IPR008952; Tetraspanin_EC2_sf.
Pfam; PF00335; Tetraspannin; 1.
PIRSF; PIRSF002419; Tetraspanin; 1.
PRINTS; PR00259; TMFOUR.
SUPFAM; SSF48652; SSF48652; 1.
PROSITE; PS00421; TM4_1; 1.
2: Evidence at transcript level;
Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
Fertilization; Lipoprotein; Membrane; Palmitate; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 226 CD9 antigen.
/FTId=PRO_0000219204.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 33 Helical. {ECO:0000255}.
TOPO_DOM 34 53 Extracellular. {ECO:0000255}.
TRANSMEM 54 74 Helical. {ECO:0000255}.
TOPO_DOM 75 85 Cytoplasmic. {ECO:0000255}.
TRANSMEM 86 109 Helical. {ECO:0000255}.
TOPO_DOM 110 193 Extracellular. {ECO:0000255}.
TRANSMEM 194 219 Helical. {ECO:0000255}.
TOPO_DOM 220 226 Cytoplasmic. {ECO:0000255}.
LIPID 9 9 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 76 76 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 77 77 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 85 85 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 216 216 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 217 217 S-palmitoyl cysteine. {ECO:0000250}.
CONFLICT 83 83 S -> Y (in Ref. 2; BAA06452).
{ECO:0000305}.
SEQUENCE 226 AA; 25059 MW; 77689D4B0C2B50B6 CRC64;
MPVKGGTKCI KYLLFGFNFI FWLAGIAVLA VGLWLRFDSQ TKSIFEQDSQ PSSFYTGVYI
LIGAGALMML VGFLGCCGAV QESQCMLGLF FGFLLVIFAI EIAAAIWGYS HKDEVIQEVQ
EFYKDTYNKL KSKDEPQRDT LKAIHYALDC CGLAGGVEQF ISDICPQKDI LSSITVKPCP
EAIKEVFHNK FHIIGAVGIG IAVVMIFGMI FSMILCCAIR RSREMV


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