CD9_BOVIN
ID CD9_BOVIN Reviewed; 226 AA.
AC P30932; A6QLK0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=CD9 antigen {ECO:0000303|PubMed:1339429};
DE AltName: CD_antigen=CD9 {ECO:0000303|PubMed:1339429};
GN Name=CD9 {ECO:0000303|PubMed:1339429};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Ocular ciliary epithelium;
RX PubMed=1339429; DOI=10.1093/oxfordjournals.jbchem.a123866;
RA Martin-Alonso J.M., Hernando N., Ghosh S., Coca-Prados M.;
RT "Molecular cloning of the bovine CD9 antigen from ocular ciliary epithelial
RT cells.";
RL J. Biochem. 112:63-67(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Integral membrane protein associated with integrins, which
CC regulates different processes, such as sperm-egg fusion, platelet
CC activation and aggregation, and cell adhesion (By similarity). Present
CC at the cell surface of oocytes and plays a key role in sperm-egg
CC fusion, possibly by organizing multiprotein complexes and the
CC morphology of the membrane required for the fusion (By similarity). In
CC myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion
CC during muscle regeneration (By similarity). In macrophages, associates
CC with CD81 and beta-1 and beta-2 integrins, and prevents macrophage
CC fusion into multinucleated giant cells specialized in ingesting
CC complement-opsonized large particles (By similarity). Also prevents the
CC fusion between mononuclear cell progenitors into osteoclasts in charge
CC of bone resorption (By similarity). Acts as a receptor for PSG17 (By
CC similarity). Involved in platelet activation and aggregation (By
CC similarity). Regulates paranodal junction formation (By similarity).
CC Involved in cell adhesion, cell motility and tumor metastasis (By
CC similarity). {ECO:0000250|UniProtKB:P21926,
CC ECO:0000250|UniProtKB:P40240}.
CC -!- SUBUNIT: Forms both disulfide-linked homodimers and higher
CC homooligomers as well as heterooligomers with other members of the
CC tetraspanin family. Interacts (via the second extracellular domain)
CC with integrin ITGAV:ITGB3 (By similarity). Interacts with integrin
CC ITGA6:ITGB1; interaction takes place in oocytes and is involved in
CC sperm-egg fusion (By similarity). Part of integrin-tetraspanin
CC complexes composed of CD81, beta-1 and beta-2 integrins in the membrane
CC of monocyte/macrophages (By similarity). Interacts with CD63;
CC identified in a complex with CD63 and ITGB3. Associates with CR2/CD21
CC and with PTGFRN/CD9P1. Part of a complex composed of CD9, CD81, PTGFRN
CC and IGSF8 (By similarity). Interacts directly with IGSF8. Interacts
CC with PDPN; this interaction is homophilic and attenuates platelet
CC aggregation and pulmonary metastasis induced by PDPN. Interacts (on T
CC cell side) with CD81 at immunological synapses between antigen-
CC presenting cells and T cells (By similarity).
CC {ECO:0000250|UniProtKB:P21926, ECO:0000250|UniProtKB:P40240}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P40240};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P40240}. Membrane
CC {ECO:0000250|UniProtKB:P40240}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P40240}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P40240}. Note=Present at the cell surface of
CC oocytes. Accumulates in the adhesion area between the sperm and egg
CC following interaction between IZUMO1 and its receptor IZUMO1R/JUNO.
CC {ECO:0000250|UniProtKB:P40240}.
CC -!- TISSUE SPECIFICITY: Detected in cornea, and at low levels in
CC neuroretina and ciliary epithelium cells. {ECO:0000269|PubMed:1339429}.
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). The protein exists in three forms with molecular
CC masses between 22 and 27 kDa, and is known to carry covalently linked
CC fatty acids. Palmitoylation by ZDHHC2 regulates CD9 expression,
CC association with other tetraspanin family proteins and function in cell
CC adhesion. {ECO:0000250|UniProtKB:P21926}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; M81720; AAA30439.1; -; mRNA.
DR EMBL; BC147992; AAI47993.1; -; mRNA.
DR PIR; JX0221; JX0221.
DR RefSeq; NP_776325.1; NM_173900.2.
DR AlphaFoldDB; P30932; -.
DR SMR; P30932; -.
DR STRING; 9913.ENSBTAP00000019643; -.
DR CarbonylDB; P30932; -.
DR PaxDb; P30932; -.
DR PeptideAtlas; P30932; -.
DR PRIDE; P30932; -.
DR Ensembl; ENSBTAT00000019643; ENSBTAP00000019643; ENSBTAG00000014764.
DR GeneID; 280746; -.
DR KEGG; bta:280746; -.
DR CTD; 928; -.
DR VEuPathDB; HostDB:ENSBTAG00000014764; -.
DR VGNC; VGNC:27053; CD9.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000155083; -.
DR HOGENOM; CLU_055524_10_1_1; -.
DR InParanoid; P30932; -.
DR OMA; CGAGCES; -.
DR OrthoDB; 1205716at2759; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000014764; Expressed in prostate gland and 102 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:AgBase.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; ISS:AgBase.
DR GO; GO:0008347; P:glial cell migration; IEA:Ensembl.
DR GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0030913; P:paranodal junction assembly; ISS:AgBase.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:1905521; P:regulation of macrophage migration; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
DR GO; GO:0035036; P:sperm-egg recognition; ISS:UniProtKB.
DR CDD; cd03152; CD9_LEL; 1.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR042055; CD9_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 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Fertilization; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Secreted;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..226
FT /note="CD9 antigen"
FT /id="PRO_0000219202"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 9
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21926"
FT LIPID 76
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21926"
FT LIPID 77
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21926"
FT LIPID 85
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21926"
FT LIPID 216
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21926"
FT LIPID 217
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21926"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 151..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 226 AA; 25258 MW; C18A778646380BE2 CRC64;
MPVKGGTKCI KYLLFGFNFI FWLAGIAVLS VGLWLRFDSQ TKSIFEQENN DSSFYTGVYI
LIGAGALMML VGFLGCCGAV QESQCMLGLF FSFLLVIFAI EVAAAIWGYS HKEEVIKEVQ
KFYEDTYNKL KNKDEPQRET LKAIHIALDC CGLTGVPEQF LTDTCPPKNL IDSLKTRPCP
EAIDEIFRSK FHIIGAVGIG IAVVMIFGMV FSMILCCAIR RNRDMV
