ADAM9

Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.[5][6]

ADAM9
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1M1V
Identifiers
Aliases	ADAM9, CORD9, MCMP, MDC9, Mltng, ADAM metallopeptidase domain 9
External IDs	OMIM: 602713 MGI: 105376 HomoloGene: 20824 GeneCards: ADAM9
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8p11.22 Start 38,996,869 bp[1] End 39,105,261 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8 A2|8 13.7 cM Start 24,949,611 bp[2] End 25,016,927 bp[2]
Gene ontology Molecular function • collagen binding • SH3 domain binding • metal ion binding • integrin binding • peptidase activity • GO:0001948 protein binding • metalloendopeptidase activity • laminin binding • hydrolase activity • metallopeptidase activity • protein kinase C binding Cellular component • integral component of membrane • membrane • focal adhesion • intrinsic component of external side of plasma membrane • cell membrane • extracellular region • extracellular exosome • cell surface • basolateral plasma membrane • extracellular Biological process • activation of MAPKK activity • positive regulation of membrane protein ectodomain proteolysis • response to glucocorticoid • positive regulation of macrophage fusion • cell-cell adhesion mediated by integrin • keratinocyte differentiation • proteolysis • monocyte activation • response to calcium ion • response to tumor necrosis factor • positive regulation of keratinocyte migration • cell adhesion • response to manganese ion • membrane protein ectodomain proteolysis • positive regulation of protein secretion • integrin-mediated signaling pathway • positive regulation of cell adhesion mediated by integrin • cell-matrix adhesion • cellular response to lipopolysaccharide • transforming growth factor beta receptor signaling pathway • response to hydrogen peroxide • cell migration • cell adhesion mediated by integrin • response to laminar fluid shear stress • response to antineoplastic agent Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8754	11502
Ensembl	ENSG00000168615 ENSG00000282230	ENSMUSG00000031555
UniProt	Q13443	Q61072
RefSeq (mRNA)	NM_001005845 NM_003816	NM_001270996 NM_007404
RefSeq (protein)	NP_003807	NP_001257925 NP_031430
Location (UCSC)	Chr 8: 39 – 39.11 Mb	Chr 8: 24.95 – 25.02 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene interacts with SH3 domain-containing proteins, binds mitotic arrest deficient 2 beta protein, and is also involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. Two alternative splice variants have been identified, encoding distinct isoforms.[6]

Interactions

ADAM9 has been shown to interact with:

• MAD2L2,[7]
• SH3GL2,[8] and
• SNX9[8]

References

1. ENSG00000282230 GRCh38: Ensembl release 89: ENSG00000168615, ENSG00000282230 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031555 - 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. Weskamp G, Kratzschmar J, Reid MS, Blobel CP (Jul 1996). "MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains". J Cell Biol. 132 (4): 717–26. doi:10.1083/jcb.132.4.717. PMC 2199860. PMID 8647900.
6. "Entrez Gene: ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma)".
7. Nelson KK, Schlöndorff J, Blobel CP (Nov 1999). "Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta". Biochem. J. 343 (Pt 3): 673–80. doi:10.1042/0264-6021:3430673. PMC 1220601. PMID 10527948.
8. Howard L, Nelson KK, Maciewicz RA, Blobel CP (Oct 1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1". J. Biol. Chem. 274 (44): 31693–9. doi:10.1074/jbc.274.44.31693. PMID 10531379.

Further reading

• Mazzocca A, Coppari R, De Franco R, Cho JY, Libermann TA, Pinzani M, Toker A (June 2005). "A secreted form of ADAM9 promotes carcinoma invasion through tumor-stromal interactions". Cancer Res. 65 (11): 4728–38. doi:10.1158/0008-5472.CAN-04-4449. PMID 15930291.
• Nomura N, Miyajima N, Sazuka T, et al. (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1". DNA Res. 1 (1): 27–35. doi:10.1093/dnares/1.1.27. PMID 7584026.
• Nomura N, Miyajima N, Sazuka T, et al. (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement)". DNA Res. 1 (1): 47–56. doi:10.1093/dnares/1.1.47. PMID 7584028.
• McKie N, Dallas DJ, Edwards T, et al. (1996). "Cloning of a novel membrane-linked metalloproteinase from human myeloma cells". Biochem. J. 318 (2): 459–62. doi:10.1042/bj3180459. PMC 1217643. PMID 8809033.
• McKie N, Edwards T, Dallas DJ, et al. (1997). "Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes". Biochem. Biophys. Res. Commun. 230 (2): 335–9. doi:10.1006/bbrc.1996.5957. PMID 9016778.
• Izumi Y, Hirata M, Hasuwa H, et al. (1999). "A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor". EMBO J. 17 (24): 7260–72. doi:10.1093/emboj/17.24.7260. PMC 1171072. PMID 9857183.
• Roghani M, Becherer JD, Moss ML, et al. (1999). "Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity". J. Biol. Chem. 274 (6): 3531–40. doi:10.1074/jbc.274.6.3531. PMID 9920899.
• Nelson KK, Schlöndorff J, Blobel CP (2000). "Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta". Biochem. J. 343 (3): 673–80. doi:10.1042/0264-6021:3430673. PMC 1220601. PMID 10527948.
• Howard L, Nelson KK, Maciewicz RA, Blobel CP (1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1". J. Biol. Chem. 274 (44): 31693–9. doi:10.1074/jbc.274.44.31693. PMID 10531379.
• Zhou M, Graham R, Russell G, Croucher PI (2001). "MDC-9 (ADAM-9/Meltrin gamma) functions as an adhesion molecule by binding the alpha(v)beta(5) integrin". Biochem. Biophys. Res. Commun. 280 (2): 574–80. doi:10.1006/bbrc.2000.4155. PMID 11162558.
• Namba K, Nishio M, Mori K, et al. (2002). "Involvement of ADAM9 in multinucleated giant cell formation of blood monocytes". Cell. Immunol. 213 (2): 104–13. doi:10.1006/cimm.2001.1873. PMID 11831872.
• Eto K, Huet C, Tarui T, et al. (2002). "Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions". J. Biol. Chem. 277 (20): 17804–10. doi:10.1074/jbc.M200086200. PMID 11882657.
• Lim JM, Lee JH, Wee WR, Joo CK (2002). "Downregulated expression of ADAM9 in anterior polar cataracts". Journal of Cataract and Refractive Surgery. 28 (4): 697–702. doi:10.1016/S0886-3350(01)01236-6. PMID 11955914. S2CID 21982654.
• Hotoda N, Koike H, Sasagawa N, Ishiura S (2002). "A secreted form of human ADAM9 has an alpha-secretase activity for APP". Biochem. Biophys. Res. Commun. 293 (2): 800–5. doi:10.1016/S0006-291X(02)00302-9. PMID 12054541.
• Amour A, Knight CG, English WR, et al. (2002). "The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs". FEBS Lett. 524 (1–3): 154–8. doi:10.1016/S0014-5793(02)03047-8. PMID 12135759. S2CID 37423323.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Mohan S, Thompson GR, Amaar YG, et al. (2003). "ADAM-9 is an insulin-like growth factor binding protein-5 protease produced and secreted by human osteoblasts". Biochemistry. 41 (51): 15394–403. doi:10.1021/bi026458q. PMID 12484779.
• Asai M, Hattori C, Szabó B, et al. (2003). "Putative function of ADAM9, ADAM10, and ADAM17 as APP alpha-secretase". Biochem. Biophys. Res. Commun. 301 (1): 231–5. doi:10.1016/S0006-291X(02)02999-6. PMID 12535668.
• O'Shea C, McKie N, Buggy Y, et al. (2003). "Expression of ADAM-9 mRNA and protein in human breast cancer". Int. J. Cancer. 105 (6): 754–61. doi:10.1002/ijc.11161. PMID 12767059. S2CID 19284959.
• Grützmann R, Lüttges J, Sipos B, et al. (2004). "ADAM9 expression in pancreatic cancer is associated with tumour type and is a prognostic factor in ductal adenocarcinoma". Br. J. Cancer. 90 (5): 1053–8. doi:10.1038/sj.bjc.6601645. PMC 2409625. PMID 14997207.

External links

• ADAM9 on the Atlas of Genetics and Oncology
• Human ADAM9 genome location and ADAM9 gene details page in the UCSC Genome Browser.