CD9_PIG
ID CD9_PIG Reviewed; 226 AA.
AC Q8WMQ3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=CD9 antigen {ECO:0000303|PubMed:14610355};
DE AltName: CD_antigen=CD9 {ECO:0000303|PubMed:14610355};
GN Name=CD9 {ECO:0000303|PubMed:14610355};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Smooth muscle;
RX PubMed=14610355; DOI=10.1159/000074170;
RA Yubero N., Jimenez-Marin A., Yerle M., Morera L., Barbancho M.J.,
RA Llanes D., Garrido J.J.;
RT "Molecular cloning, expression pattern and chromosomal mapping of pig CD9
RT antigen.";
RL Cytogenet. Genome Res. 101:143-146(2003).
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: Ubiquitous. {ECO:0000269|PubMed:14610355}.
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; AY072785; AAL68966.1; -; mRNA.
DR RefSeq; NP_999171.1; NM_214006.1.
DR AlphaFoldDB; Q8WMQ3; -.
DR SMR; Q8WMQ3; -.
DR STRING; 9823.ENSSSCP00000026090; -.
DR PaxDb; Q8WMQ3; -.
DR PeptideAtlas; Q8WMQ3; -.
DR GeneID; 397067; -.
DR KEGG; ssc:397067; -.
DR CTD; 928; -.
DR eggNOG; KOG3882; Eukaryota.
DR InParanoid; Q8WMQ3; -.
DR OrthoDB; 1205716at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
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:UniProtKB.
DR GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; ISS:UniProtKB.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0030913; P:paranodal junction assembly; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
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_0000219207"
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 CARBOHYD 51
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; 25201 MW; D24405DCC7F14640 CRC64;
MPVKGGTKCI KYLLFGFNFI FWLAGIAVLA IGLWLRFDSQ TKSIFEQENN NSSFYTGVYI
LIGAGALMMV VGFLGCCGAV QESQCMLGLF FGFLLVIFAI EIAAAIWGYS HKDQVIKEVQ
DFYRDTYNKL KGKDDPQRET LKAIHYALDC CGLMGEVEQL LADICPQRDV LSSLPMKPCP
EAIKEVFQNK FHIIGAVGIG IAVVMIFGMI FSMILCCAIR RSREMV
