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CD9 information


Crystal structure of human CD9
CD9
Identifiers
AliasesCD9, BTCC-1, DRAP-27, MIC3, MRP-1, TSPAN-29, TSPAN29, CD9 molecule
External IDsOMIM: 143030; MGI: 88348; HomoloGene: 20420; GeneCards: CD9; OMA:CD9 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001769
NM_001330312

NM_007657

RefSeq (protein)

NP_001317241
NP_001760

NP_031683

Location (UCSC)Chr 12: 6.2 – 6.24 MbChr 6: 125.44 – 125.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

CD9 is a gene encoding a protein that is a member of the transmembrane 4 superfamily also known as the tetraspanin family. It is a cell surface glycoprotein that consists of four transmembrane regions and has two extracellular loops that contain disulfide bonds which are conserved throughout the tetraspanin family.[5][6][7] Also containing distinct palmitoylation sites that allows CD9 to interact with lipids and other proteins.[5][8][9]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000010278 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030342 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Andreu Z, Yáñez-Mó M (2014). "Tetraspanins in extracellular vesicle formation and function". Frontiers in Immunology. 8: 342. doi:10.3389/fimmu.2014.00442. PMC 4165315. PMID 25278937.
  6. ^ "CD9 CD9 molecule [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2019-12-04.
  7. ^ "CD9 Gene - GeneCards | CD9 Protein | CD9 Antibody". www.genecards.org. Retrieved 2019-12-04.
  8. ^ Yáñez-Mó M, Barreiro O, Gordon-Alonso M, Sala-Valdés M, Sánchez-Madrid F (September 2009). "Tetraspanin-enriched microdomains: a functional unit in cell plasma membranes". Trends in Cell Biology. 19 (9): 434–46. doi:10.1016/j.tcb.2009.06.004. PMID 19709882.
  9. ^ Yang XH, Kovalenko OV, Kolesnikova TV, Andzelm MM, Rubinstein E, Strominger JL, Hemler ME (May 2006). "Contrasting effects of EWI proteins, integrins, and protein palmitoylation on cell surface CD9 organization". The Journal of Biological Chemistry. 281 (18): 12976–85. doi:10.1074/jbc.M510617200. PMID 16537545.

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the flagellum, but not the mitochondria, to enter the oocyte. The protein CD9 likely mediates this fusion in mice (the binding homolog). The egg "activates"...

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