CD9_MOUSE
ID CD9_MOUSE Reviewed; 226 AA.
AC P40240; Q3U9W0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=CD9 antigen {ECO:0000303|PubMed:8236164};
DE AltName: CD_antigen=CD9 {ECO:0000303|PubMed:8236164};
GN Name=Cd9 {ECO:0000303|PubMed:8236164, ECO:0000312|MGI:MGI:88348};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=8236164; DOI=10.1016/0049-3848(93)90162-h;
RA Rubinstein E., Billard M., Plaisance S., Prenant M., Boucheix C.;
RT "Molecular cloning of the mouse equivalent of CD9 antigen.";
RL Thromb. Res. 71:377-383(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION IN GAMETE FUSION.
RX PubMed=10700183; DOI=10.1038/73502;
RA Kaji K., Oda S., Shikano T., Ohnuki T., Uematsu Y., Sakagami J., Tada N.,
RA Miyazaki S., Kudo A.;
RT "The gamete fusion process is defective in eggs of Cd9-deficient mice.";
RL Nat. Genet. 24:279-282(2000).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10518536; DOI=10.1073/pnas.96.21.11830;
RA Chen M.S., Tung K.S., Coonrod S.A., Takahashi Y., Bigler D., Chang A.,
RA Yamashita Y., Kincade P.W., Herr J.C., White J.M.;
RT "Role of the integrin-associated protein CD9 in binding between sperm ADAM
RT 2 and the egg integrin alpha6beta1: implications for murine
RT fertilization.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11830-11835(1999).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10634790; DOI=10.1126/science.287.5451.319;
RA Le Naour F., Rubinstein E., Jasmin C., Prenant M., Boucheix C.;
RT "Severely reduced female fertility in CD9-deficient mice.";
RL Science 287:319-321(2000).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND INTERACTION WITH ITGA6 AND ITGB1.
RX PubMed=10634791; DOI=10.1126/science.287.5451.321;
RA Miyado K., Yamada G., Yamada S., Hasuwa H., Nakamura Y., Ryu F., Suzuki K.,
RA Kosai K., Inoue K., Ogura A., Okabe M., Mekada E.;
RT "Requirement of CD9 on the egg plasma membrane for fertilization.";
RL Science 287:321-324(2000).
RN [8]
RP MUTAGENESIS OF PHE-174 AND 173-SER--GLN-175.
RX PubMed=11934865; DOI=10.1242/dev.129.8.1995;
RA Zhu G.-Z., Miller B.J., Boucheix C., Rubinstein E., Liu C.C., Hynes R.O.,
RA Myles D.G., Primakoff P.;
RT "Residues SFQ (173-175) in the large extracellular loop of CD9 are required
RT for gamete fusion.";
RL Development 129:1995-2002(2002).
RN [9]
RP FUNCTION AS A RECEPTOR FOR PSG17, AND SUBCELLULAR LOCATION.
RX PubMed=11805154; DOI=10.1084/jem.20011741;
RA Waterhouse R., Ha C., Dveksler G.S.;
RT "Murine CD9 is the receptor for pregnancy-specific glycoprotein 17.";
RL J. Exp. Med. 195:277-282(2002).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12796480; DOI=10.1083/jcb.200212031;
RA Takeda Y., Tachibana I., Miyado K., Kobayashi M., Miyazaki T.,
RA Funakoshi T., Kimura H., Yamane H., Saito Y., Goto H., Yoneda T.,
RA Yoshida M., Kumagai T., Osaki T., Hayashi S., Kawase I., Mekada E.;
RT "Tetraspanins CD9 and CD81 function to prevent the fusion of mononuclear
RT phagocytes.";
RL J. Cell Biol. 161:945-956(2003).
RN [11]
RP FUNCTION IN PARANODAL FORMATION, AND TISSUE SPECIFICITY.
RX PubMed=14715942; DOI=10.1523/jneurosci.1484-03.2004;
RA Ishibashi T., Ding L., Ikenaka K., Inoue Y., Miyado K., Mekada E., Baba H.;
RT "Tetraspanin protein CD9 is a novel paranodal component regulating
RT paranodal junctional formation.";
RL J. Neurosci. 24:96-102(2004).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18662991; DOI=10.1074/jbc.m801902200;
RA Takeda Y., He P., Tachibana I., Zhou B., Miyado K., Kaneko H., Suzuki M.,
RA Minami S., Iwasaki T., Goya S., Kijima T., Kumagai T., Yoshida M.,
RA Osaki T., Komori T., Mekada E., Kawase I.;
RT "Double deficiency of tetraspanins CD9 and CD81 alters cell motility and
RT protease production of macrophages and causes chronic obstructive pulmonary
RT disease-like phenotype in mice.";
RL J. Biol. Chem. 283:26089-26097(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21690351; DOI=10.1073/pnas.1017400108;
RA Jegou A., Ziyyat A., Barraud-Lange V., Perez E., Wolf J.P., Pincet F.,
RA Gourier C.;
RT "CD9 tetraspanin generates fusion competent sites on the egg membrane for
RT mammalian fertilization.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10946-10951(2011).
RN [15]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23213457; DOI=10.1242/bio.20121420;
RA Ohnami N., Nakamura A., Miyado M., Sato M., Kawano N., Yoshida K.,
RA Harada Y., Takezawa Y., Kanai S., Ono C., Takahashi Y., Kimura K.,
RA Shida T., Miyado K., Umezawa A.;
RT "CD81 and CD9 work independently as extracellular components upon fusion of
RT sperm and oocyte.";
RL Biol. Open 1:640-647(2012).
RN [16]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH CD81,
RP INTERACTION WITH PTGFRN, AND INTERACTION WITH IGSF8.
RX PubMed=23575678; DOI=10.1038/ncomms2675;
RA Charrin S., Latil M., Soave S., Polesskaya A., Chretien F., Boucheix C.,
RA Rubinstein E.;
RT "Normal muscle regeneration requires tight control of muscle cell fusion by
RT tetraspanins CD9 and CD81.";
RL Nat. Commun. 4:1674-1674(2013).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=25209248; DOI=10.1242/dev.111534;
RA Chalbi M., Barraud-Lange V., Ravaux B., Howan K., Rodriguez N., Soule P.,
RA Ndzoudi A., Boucheix C., Rubinstein E., Wolf J.P., Ziyyat A., Perez E.,
RA Pincet F., Gourier C.;
RT "Binding of sperm protein Izumo1 and its egg receptor Juno drives Cd9
RT accumulation in the intercellular contact area prior to fusion during
RT mammalian fertilization.";
RL Development 141:3732-3739(2014).
RN [18]
RP SUBCELLULAR LOCATION.
RC TISSUE=Macrophage;
RX PubMed=26109643; DOI=10.4049/jimmunol.1402894;
RA Athman J.J., Wang Y., McDonald D.J., Boom W.H., Harding C.V., Wearsch P.A.;
RT "Bacterial membrane vesicles mediate the release of Mycobacterium
RT tuberculosis lipoglycans and lipoproteins from infected macrophages.";
RL J. Immunol. 195:1044-1053(2015).
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 (PubMed:10700183,
CC PubMed:10634790, PubMed:10634791, PubMed:14715942). Present at the cell
CC surface of oocytes and plays a key role in sperm-egg fusion, possibly
CC by organizing multiprotein complexes and the morphology of the membrane
CC required for the fusion (PubMed:10700183, PubMed:10634790,
CC PubMed:10634791, PubMed:21690351). In myoblasts, associates with CD81
CC and PTGFRN and inhibits myotube fusion during muscle regeneration
CC (PubMed:23575678). In macrophages, associates with CD9 and beta-1 and
CC beta-2 integrins, and prevents macrophage fusion into multinucleated
CC giant cells specialized in ingesting complement-opsonized large
CC particles. Also prevents the fusion between mononuclear cell
CC progenitors into osteoclasts in charge of bone resorption
CC (PubMed:12796480). Acts as a receptor for PSG17 (PubMed:11805154).
CC Involved in platelet activation and aggregation (PubMed:14715942).
CC Regulates paranodal junction formation (PubMed:14715942). Involved in
CC cell adhesion, cell motility and tumor metastasis (By similarity). Also
CC regulates integrin-dependent migration of macrophages, particularly
CC relevant for inflammatory response in the lung (PubMed:18662991).
CC {ECO:0000250|UniProtKB:P21926, ECO:0000269|PubMed:10634790,
CC ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:10700183,
CC ECO:0000269|PubMed:11805154, ECO:0000269|PubMed:12796480,
CC ECO:0000269|PubMed:14715942, ECO:0000269|PubMed:18662991,
CC ECO:0000269|PubMed:21690351, ECO:0000269|PubMed:23575678}.
CC -!- SUBUNIT: Forms both disulfide-linked homodimers and higher
CC homooligomers as well as heterooligomers with other members of the
CC tetraspanin family (By similarity). Interacts (via the second
CC extracellular domain) with integrin ITGAV:ITGB3 (By similarity).
CC Interacts with integrin ITGA6:ITGB1; interaction takes place in oocytes
CC and is involved in sperm-egg fusion (PubMed:10634791). Part of
CC integrin-tetraspanin complexes composed of CD81, beta-1 and beta-2
CC integrins in the membrane of monocyte/macrophages (By similarity).
CC Interacts with CD63; identified in a complex with CD63 and ITGB3 (By
CC similarity). Associates with CR2/CD21 and with PTGFRN/CD9P1 (By
CC similarity). Part of a complex composed of CD9, CD81, PTGFRN and IGSF8
CC (PubMed:23575678). Interacts directly with IGSF8 (By similarity).
CC Interacts with PDPN; this interaction is homophilic and attenuates
CC platelet aggregation and pulmonary metastasis induced by PDPN (By
CC similarity). {ECO:0000250|UniProtKB:P21926,
CC ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:23575678}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10518536,
CC ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:11805154,
CC ECO:0000269|PubMed:23213457}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11805154}. Membrane {ECO:0000269|PubMed:11805154};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11805154}. Secreted,
CC extracellular exosome {ECO:0000269|PubMed:26109643}. Note=Present at
CC the cell surface of oocytes (PubMed:10518536, PubMed:10634791,
CC PubMed:23213457). Accumulates in the adhesion area between the sperm
CC and egg following interaction between IZUMO1 and its receptor
CC IZUMO1R/JUNO (PubMed:25209248). {ECO:0000269|PubMed:10518536,
CC ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:23213457,
CC ECO:0000269|PubMed:25209248}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the peripheral nervous
CC system (PubMed:14715942). Highly expressed in oocytes and blastocysts
CC (at protein level) (PubMed:10518536, PubMed:10634790, PubMed:10634791,
CC PubMed:23213457). Expression is also observed on follicular oocytes in
CC the ovary, whereas no expression is found on follicular cells (at
CC protein level) (PubMed:10518536, PubMed:10634790). Expressed in
CC skeletal muscle mainly in endothelial cells of endomysial capillaries,
CC in satellite cells and myoblasts (at protein level).
CC {ECO:0000269|PubMed:10518536, ECO:0000269|PubMed:10634790,
CC ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:14715942,
CC ECO:0000269|PubMed:23213457, ECO:0000269|PubMed:23575678}.
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 -!- DISRUPTION PHENOTYPE: Knockout mice are healthy, but females display
CC severely reduced fertility (PubMed:10634790, PubMed:10634791). Oocyte
CC maturation and ovulation are normal and female infertility is caused by
CC defects in sperm-egg fusion (PubMed:10634790, PubMed:10634791). Wild
CC type sperm penetrates the zona pellucida, binds to the oolema but the
CC membranes fail to fuse (PubMed:10634790, PubMed:10634791). The
CC infertility is overcome by intracytoplasmic sperm injection, and
CC embryos develop normally (PubMed:10634790, PubMed:10634791). Eggs show
CC reduced ability for strong sperm adhesion, and sperm accumulate in the
CC perivitelline space, only transiently binding to the egg surface
CC (PubMed:21690351). In response to notexin-induced acute myoinjury,
CC mutant mice display abnormal muscle regeneration characterized by
CC typical giant distrophic myofibres (PubMed:23575678). These mice
CC spontaneously develop multinucleated giant cells (MGCs) and show
CC enhanced osteoclastogenesis when compared to wild-type littermates
CC (PubMed:12796480). CD81 and CD9 double knockout mice develop pulmonary
CC emphysema, reminiscent of chronic obstructive pulmonary disease in
CC human (PubMed:18662991). {ECO:0000269|PubMed:10634790,
CC ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:12796480,
CC ECO:0000269|PubMed:18662991, ECO:0000269|PubMed:21690351,
CC ECO:0000269|PubMed:23575678}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; L08115; AAA37405.1; -; mRNA.
DR EMBL; AK002251; BAB21965.1; -; mRNA.
DR EMBL; AK012793; BAB28473.1; -; mRNA.
DR EMBL; AK151443; BAE30405.1; -; mRNA.
DR EMBL; AK151619; BAE30556.1; -; mRNA.
DR EMBL; AK170310; BAE41707.1; -; mRNA.
DR EMBL; BC070474; AAH70474.1; -; mRNA.
DR CCDS; CCDS20551.1; -.
DR PIR; I49589; I49589.
DR RefSeq; NP_031683.1; NM_007657.3.
DR AlphaFoldDB; P40240; -.
DR SMR; P40240; -.
DR BioGRID; 198620; 1.
DR STRING; 10090.ENSMUSP00000032492; -.
DR GlyGen; P40240; 1 site.
DR PhosphoSitePlus; P40240; -.
DR SwissPalm; P40240; -.
DR EPD; P40240; -.
DR jPOST; P40240; -.
DR MaxQB; P40240; -.
DR PaxDb; P40240; -.
DR PeptideAtlas; P40240; -.
DR PRIDE; P40240; -.
DR ProteomicsDB; 281272; -.
DR Antibodypedia; 3733; 1806 antibodies from 49 providers.
DR DNASU; 12527; -.
DR Ensembl; ENSMUST00000032492; ENSMUSP00000032492; ENSMUSG00000030342.
DR GeneID; 12527; -.
DR KEGG; mmu:12527; -.
DR UCSC; uc009dun.1; mouse.
DR CTD; 928; -.
DR MGI; MGI:88348; Cd9.
DR VEuPathDB; HostDB:ENSMUSG00000030342; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000155083; -.
DR HOGENOM; CLU_055524_10_1_1; -.
DR InParanoid; P40240; -.
DR OMA; CGAGCES; -.
DR OrthoDB; 1205716at2759; -.
DR PhylomeDB; P40240; -.
DR TreeFam; TF352895; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-1300645; Acrosome Reaction and Sperm:Oocyte Membrane Binding.
DR BioGRID-ORCS; 12527; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cd9; mouse.
DR PRO; PR:P40240; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P40240; protein.
DR Bgee; ENSMUSG00000030342; Expressed in skin of external ear and 268 other tissues.
DR Genevisible; P40240; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:UniProtKB.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IDA:UniProtKB.
DR GO; GO:0008347; P:glial cell migration; ISO:MGI.
DR GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0030913; P:paranodal junction assembly; IDA:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR GO; GO:1905521; P:regulation of macrophage migration; IDA:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IDA:UniProtKB.
DR GO; GO:0035036; P:sperm-egg recognition; IDA: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; 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_0000219206"
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"
FT MUTAGEN 173..175
FT /note="SFQ->AAA: Sperm-egg fusion abolished."
FT /evidence="ECO:0000269|PubMed:11934865"
FT MUTAGEN 174
FT /note="F->A: 4-fold reduction of sperm-egg fusion."
FT /evidence="ECO:0000269|PubMed:11934865"
SQ SEQUENCE 226 AA; 25258 MW; 06D24A878BF348C5 CRC64;
MPVKGGSKCI KYLLFGFNFI FWLAGIAVLA IGLWLRFDSQ TKSIFEQENN HSSFYTGVYI
LIGAGALMML VGFLGCCGAV QESQCMLGLF FGFLLVIFAI EIAAAVWGYT HKDEVIKELQ
EFYKDTYQKL RSKDEPQRET LKAIHMALDC CGIAGPLEQF ISDTCPKKQL LESFQVKPCP
EAISEVFNNK FHIIGAVGIG IAVVMIFGMI FSMILCCAIR RSREMV
