CD9 antigen

Details

Name
CD9 antigen
Synonyms
  • 5H9 antigen
  • Cell growth-inhibiting gene 2 protein
  • Leukocyte antigen MIC3
  • MIC3
  • Motility-related protein
  • MRP-1
  • p24
  • Tetraspanin-29
  • Tspan-29
  • TSPAN29
Gene Name
CD9
Organism
Humans
Amino acid sequence
>lcl|BSEQ0012360|CD9 antigen
MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGV
YILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKE
VQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKS
CPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV
Number of residues
228
Molecular Weight
25415.835
Theoretical pI
7.19
GO Classification
Processes
blood coagulation / brain development / cell adhesion / cell surface receptor signaling pathway / cellular response to low-density lipoprotein particle stimulus / fusion of sperm to egg plasma membrane / movement of cell or subcellular component / multicellular organism reproduction / negative regulation of cell proliferation / oligodendrocyte development / paranodal junction assembly / platelet activation / platelet degranulation / receptor internalization / response to water deprivation / single fertilization
Components
apical plasma membrane / clathrin-coated endocytic vesicle membrane / endocytic vesicle membrane / external side of plasma membrane / extracellular exosome / extracellular space / extracellular vesicle / focal adhesion / integral component of plasma membrane / membrane / plasma membrane / platelet alpha granule membrane
General Function
Not Available
Specific 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.
Pfam Domain Function
Transmembrane Regions
13-33 56-76 88-111 196-221
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0012361|CD9 antigen (CD9)
ATGCCGGTCAAAGGAGGCACCAAGTGCATCAAATACCTGCTGTTCGGATTTAACTTCATC
TTCTGGCTTGCCGGGATTGCTGTCCTTGCCATTGGACTATGGCTCCGATTCGACTCTCAG
ACCAAGAGCATCTTCGAGCAAGAAACTAATAATAATAATTCCAGCTTCTACACAGGAGTC
TATATTCTGATCGGAGCCGGCGCCCTCATGATGCTGGTGGGCTTCCTGGGCTGCTGCGGG
GCTGTGCAGGAGTCCCAGTGCATGCTGGGACTGTTCTTCGGCTTCCTCTTGGTGATATTC
GCCATTGAAATAGCTGCGGCCATCTGGGGATATTCCCACAAGGATGAGGTGATTAAGGAA
GTCCAGGAGTTTTACAAGGACACCTACAACAAGCTGAAAACCAAGGATGAGCCCCAGCGG
GAAACGCTGAAAGCCATCCACTATGCGTTGAACTGCTGTGGTTTGGCTGGGGGCGTGGAA
CAGTTTATCTCAGACATCTGCCCCAAGAAGGACGTACTCGAAACCTTCACCGTGAAGTCC
TGTCCTGATGCCATCAAAGAGGTCTTCGACAATAAATTCCACATCATCGGCGCAGTGGGC
ATCGGCATTGCCGTGGTCATGATATTTGGCATGATCTTCAGTATGATCTTGTGCTGTGCT
ATCCGCAGGAACCGCGAGATGGTCTAG
Chromosome Location
12
Locus
12p13.3
External Identifiers
ResourceLink
UniProtKB IDP21926
UniProtKB Entry NameCD9_HUMAN
GenBank Gene IDS60489
GenAtlas IDCD9
HGNC IDHGNC:1709
General References
  1. Boucheix C, Benoit P, Frachet P, Billard M, Worthington RE, Gagnon J, Uzan G: Molecular cloning of the CD9 antigen. A new family of cell surface proteins. J Biol Chem. 1991 Jan 5;266(1):117-22. [Article]
  2. Lanza F, Wolf D, Fox CF, Kieffer N, Seyer JM, Fried VA, Coughlin SR, Phillips DR, Jennings LK: cDNA cloning and expression of platelet p24/CD9. Evidence for a new family of multiple membrane-spanning proteins. J Biol Chem. 1991 Jun 5;266(16):10638-45. [Article]
  3. Miyake M, Koyama M, Seno M, Ikeyama S: Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility. J Exp Med. 1991 Dec 1;174(6):1347-54. [Article]
  4. Rubinstein E, Benoit P, Billard M, Plaisance S, Prenant M, Uzan G, Boucheix C: Organization of the human CD9 gene. Genomics. 1993 Apr;16(1):132-8. [Article]
  5. Kobayashi H, Hosono O, Iwata S, Kawasaki H, Kuwana M, Tanaka H, Dang NH, Morimoto C: The tetraspanin CD9 is preferentially expressed on the human CD4(+)CD45RA+ naive T cell population and is involved in T cell activation. Clin Exp Immunol. 2004 Jul;137(1):101-8. [Article]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  7. Higashihara M, Takahata K, Yatomi Y, Nakahara K, Kurokawa K: Purification and partial characterization of CD9 antigen of human platelets. FEBS Lett. 1990 May 21;264(2):270-4. [Article]
  8. Ikeyama S, Koyama M, Yamaoko M, Sasada R, Miyake M: Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA. J Exp Med. 1993 May 1;177(5):1231-7. [Article]
  9. Masellis-Smith A, Shaw AR: CD9-regulated adhesion. Anti-CD9 monoclonal antibody induce pre-B cell adhesion to bone marrow fibroblasts through de novo recognition of fibronectin. J Immunol. 1994 Mar 15;152(6):2768-77. [Article]
  10. Higginbottom A, Takahashi Y, Bolling L, Coonrod SA, White JM, Partridge LJ, Monk PN: Structural requirements for the inhibitory action of the CD9 large extracellular domain in sperm/oocyte binding and fusion. Biochem Biophys Res Commun. 2003 Nov 7;311(1):208-14. [Article]
  11. Kovalenko OV, Yang X, Kolesnikova TV, Hemler ME: Evidence for specific tetraspanin homodimers: inhibition of palmitoylation makes cysteine residues available for cross-linking. Biochem J. 2004 Jan 15;377(Pt 2):407-17. [Article]
  12. Charrin S, Manie S, Oualid M, Billard M, Boucheix C, Rubinstein E: Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation. FEBS Lett. 2002 Apr 10;516(1-3):139-44. [Article]
  13. Charrin S, Le Naour F, Oualid M, Billard M, Faure G, Hanash SM, Boucheix C, Rubinstein E: The major CD9 and CD81 molecular partner. Identification and characterization of the complexes. J Biol Chem. 2001 Apr 27;276(17):14329-37. Epub 2001 Jan 18. [Article]
  14. Stipp CS, Kolesnikova TV, Hemler ME: EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily. J Biol Chem. 2001 Nov 2;276(44):40545-54. Epub 2001 Aug 14. [Article]
  15. Israels SJ, McMillan-Ward EM: Palmitoylation supports the association of tetraspanin CD63 with CD9 and integrin alphaIIbbeta3 in activated platelets. Thromb Res. 2010 Feb;125(2):152-8. doi: 10.1016/j.thromres.2009.07.005. Epub 2009 Jul 29. [Article]
  16. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB05398C31GinvestigationalunknownDetails