CD9_RAT
ID CD9_RAT Reviewed; 226 AA.
AC P40241;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=CD9 antigen {ECO:0000303|PubMed:7823164};
DE AltName: CD_antigen=CD9 {ECO:0000303|PubMed:7823164};
GN Name=Cd9 {ECO:0000303|PubMed:7823164};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Sciatic nerve;
RX PubMed=7823164; DOI=10.1523/jneurosci.15-01-00562.1995;
RA Kaprielian Z., Cho K.O., Hadjiargyrou M., Patterson P.H.;
RT "CD9, a major platelet cell surface glycoprotein, is a ROCA antigen and is
RT expressed in the nervous system.";
RL J. Neurosci. 15:562-573(1995).
RN [2]
RP PROTEIN SEQUENCE OF 118-131 AND 143-190, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
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: Expressed in the peripheral nervous system.
CC {ECO:0000269|PubMed:7823164}.
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; X76489; CAA54027.1; -; mRNA.
DR PIR; I56562; S39262.
DR RefSeq; NP_444177.1; NM_053018.1.
DR AlphaFoldDB; P40241; -.
DR SMR; P40241; -.
DR BioGRID; 247041; 1.
DR IntAct; P40241; 1.
DR MINT; P40241; -.
DR STRING; 10116.ENSRNOP00000026633; -.
DR GlyGen; P40241; 1 site.
DR iPTMnet; P40241; -.
DR PhosphoSitePlus; P40241; -.
DR PaxDb; P40241; -.
DR PRIDE; P40241; -.
DR Ensembl; ENSRNOT00000026633; ENSRNOP00000026633; ENSRNOG00000019556.
DR GeneID; 24936; -.
DR KEGG; rno:24936; -.
DR UCSC; RGD:2318; rat.
DR CTD; 928; -.
DR RGD; 2318; Cd9.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000155083; -.
DR HOGENOM; CLU_055524_10_1_1; -.
DR InParanoid; P40241; -.
DR OMA; CGAGCES; -.
DR OrthoDB; 1205716at2759; -.
DR PhylomeDB; P40241; -.
DR TreeFam; TF352895; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-1300645; Acrosome Reaction and Sperm:Oocyte Membrane Binding.
DR PRO; PR:P40241; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000019556; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; P40241; baseline and differential.
DR Genevisible; P40241; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; IPI:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
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:0008347; P:glial cell migration; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
DR GO; GO:0030913; P:paranodal junction assembly; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:1905521; P:regulation of macrophage migration; ISO:RGD.
DR GO; GO:0009414; P:response to water deprivation; IEP:RGD.
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 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Fertilization; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Secreted; Transmembrane; Transmembrane helix.
FT CHAIN 1..226
FT /note="CD9 antigen"
FT /id="PRO_0000219208"
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; 25215 MW; 55E56BA0C595CF98 CRC64;
MPVKGGSKCI KYLLFGFNFI FWLAGIAVLA IGLWLRFDSQ TKSIFEQETN HSSFYTGVYI
LIGAGALMML VGFLGCCGAV QESQCMLGLF FGFLLVIFAI EIAAAVWGYT HKDEVIKELQ
EFYKDTYQKL RNKDEPQRET LKAIHMALNC CGIAGGVEQF ISDICPKKQV LESFQVKSCP
DAIDEVFHSK FHIIGAVGIG IAVVMIFGMI FSMILCCAIR RSREMV
