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CD9 antigen (CD antigen CD9)

 CD9_MOUSE               Reviewed;         226 AA.
P40240; Q3U9W0;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 147.
RecName: Full=CD9 antigen;
AltName: CD_antigen=CD9;
Name=Cd9;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Kidney;
PubMed=8236164; DOI=10.1016/0049-3848(93)90162-H;
Rubinstein E., Billard M., Plaisance S., Prenant M., Boucheix C.;
"Molecular cloning of the mouse equivalent of CD9 antigen.";
Thromb. Res. 71:377-383(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
ROLE IN GAMETE FUSION.
PubMed=10700183; DOI=10.1038/73502;
Kaji K., Oda S., Shikano T., Ohnuki T., Uematsu Y., Sakagami J.,
Tada N., Miyazaki S., Kudo A.;
"The gamete fusion process is defective in eggs of Cd9-deficient
mice.";
Nat. Genet. 24:279-282(2000).
[5]
MUTAGENESIS OF PHE-174 AND 173-SER--GLN-175.
PubMed=11934865;
Zhu G.-Z., Miller B.J., Boucheix C., Rubinstein E., Liu C.C.,
Hynes R.O., Myles D.G., Primakoff P.;
"Residues SFQ (173-175) in the large extracellular loop of CD9 are
required for gamete fusion.";
Development 129:1995-2002(2002).
[6]
FUNCTION AS A RECEPTOR FOR PSG17, AND SUBCELLULAR LOCATION.
PubMed=11805154; DOI=10.1084/jem.20011741;
Waterhouse R., Ha C., Dveksler G.S.;
"Murine CD9 is the receptor for pregnancy-specific glycoprotein 17.";
J. Exp. Med. 195:277-282(2002).
[7]
ROLE IN PARANODAL FORMATION, AND TISSUE SPECIFICITY.
PubMed=14715942; DOI=10.1523/JNEUROSCI.1484-03.2004;
Ishibashi T., Ding L., Ikenaka K., Inoue Y., Miyado K., Mekada E.,
Baba H.;
"Tetraspanin protein CD9 is a novel paranodal component regulating
paranodal junctional formation.";
J. Neurosci. 24:96-102(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
SUBCELLULAR LOCATION.
TISSUE=Macrophage;
PubMed=26109643; DOI=10.4049/jimmunol.1402894;
Athman J.J., Wang Y., McDonald D.J., Boom W.H., Harding C.V.,
Wearsch P.A.;
"Bacterial membrane vesicles mediate the release of Mycobacterium
tuberculosis lipoglycans and lipoproteins from infected macrophages.";
J. Immunol. 195:1044-1053(2015).
-!- 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). Acts as a receptor for PSG17. {ECO:0000250,
ECO:0000269|PubMed:10700183, ECO:0000269|PubMed:11805154,
ECO:0000269|PubMed:14715942}.
-!- 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:11805154};
Multi-pass membrane protein {ECO:0000269|PubMed:11805154}. Cell
membrane {ECO:0000269|PubMed:11805154}; Multi-pass membrane
protein {ECO:0000269|PubMed:11805154}. Secreted, exosome
{ECO:0000269|PubMed:26109643}.
-!- TISSUE SPECIFICITY: Expressed predominantly in the peripheral
nervous system. {ECO:0000269|PubMed:14715942}.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L08115; AAA37405.1; -; mRNA.
EMBL; AK002251; BAB21965.1; -; mRNA.
EMBL; AK012793; BAB28473.1; -; mRNA.
EMBL; AK151443; BAE30405.1; -; mRNA.
EMBL; AK151619; BAE30556.1; -; mRNA.
EMBL; AK170310; BAE41707.1; -; mRNA.
EMBL; BC070474; AAH70474.1; -; mRNA.
CCDS; CCDS20551.1; -.
PIR; I49589; I49589.
RefSeq; NP_031683.1; NM_007657.3.
UniGene; Mm.210676; -.
UniGene; Mm.404614; -.
ProteinModelPortal; P40240; -.
IntAct; P40240; 1.
MINT; MINT-4090327; -.
STRING; 10090.ENSMUSP00000032492; -.
PhosphoSitePlus; P40240; -.
SwissPalm; P40240; -.
MaxQB; P40240; -.
PaxDb; P40240; -.
PeptideAtlas; P40240; -.
PRIDE; P40240; -.
Ensembl; ENSMUST00000032492; ENSMUSP00000032492; ENSMUSG00000030342.
GeneID; 12527; -.
KEGG; mmu:12527; -.
UCSC; uc009dun.1; mouse.
CTD; 928; -.
MGI; MGI:88348; Cd9.
eggNOG; KOG3882; Eukaryota.
eggNOG; ENOG4111IRY; LUCA.
GeneTree; ENSGT00880000137858; -.
HOGENOM; HOG000230651; -.
HOVERGEN; HBG002324; -.
InParanoid; P40240; -.
KO; K06460; -.
OMA; CCAIRKS; -.
OrthoDB; EOG091G0K9H; -.
PhylomeDB; P40240; -.
TreeFam; TF352895; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-1300652; Sperm:Oocyte Membrane Binding.
PRO; PR:P40240; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030342; -.
CleanEx; MM_CD9; -.
Genevisible; P40240; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:1903561; C:extracellular vesicle; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:MGI.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
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; IDA:UniProtKB.
GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IDA:UniProtKB.
GO; GO:0006928; P:movement of cell or subcellular component; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
GO; GO:0030913; P:paranodal junction assembly; IDA:UniProtKB.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IEA:Ensembl.
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.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
Fertilization; Glycoprotein; Lipoprotein; Membrane; Palmitate;
Reference proteome; Secreted; Transmembrane; Transmembrane helix.
CHAIN 1 226 CD9 antigen.
/FTId=PRO_0000219206.
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}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 173 175 SFQ->AAA: Sperm-egg fusion abolished.
{ECO:0000269|PubMed:11934865}.
MUTAGEN 174 174 F->A: 4-fold reduction of sperm-egg
fusion. {ECO:0000269|PubMed:11934865}.
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


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