Protein-coding gene in the species Homo sapiens
| ADAM9 |
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| Available structures |
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| PDB | Ortholog search: PDBe RCSB |
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| Identifiers |
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| Aliases | ADAM9, CORD9, MCMP, MDC9, Mltng, ADAM metallopeptidase domain 9 |
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| External IDs | OMIM: 602713; MGI: 105376; HomoloGene: 20824; GeneCards: ADAM9; OMA:ADAM9 - orthologs |
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| Gene location (Human) |
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 | | Chr. | Chromosome 8 (human)[1] |
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| | Band | 8p11.22 | Start | 38,996,754 bp[1] |
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| End | 39,105,445 bp[1] |
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| Gene location (Mouse) |
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 | | Chr. | Chromosome 8 (mouse)[2] |
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| | Band | 8 A2|8 13.7 cM | Start | 25,439,627 bp[2] |
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| End | 25,506,943 bp[2] |
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| RNA expression pattern |
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| Bgee | | Human | Mouse (ortholog) |
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| Top expressed in | - stromal cell of endometrium
- islet of Langerhans
- gallbladder
- smooth muscle tissue
- right lung
- Descending thoracic aorta
- Achilles tendon
- ascending aorta
- upper lobe of left lung
- rectum
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| | Top expressed in | - endothelial cell of lymphatic vessel
- stroma of bone marrow
- seminal vesicula
- retinal pigment epithelium
- epithelium of lens
- left lung lobe
- Paneth cell
- right lung
- parotid gland
- gastric mucosa
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| | More reference expression data |
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| BioGPS | |
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| Gene ontology |
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| Molecular function | - collagen binding
- SH3 domain binding
- metal ion binding
- integrin binding
- peptidase activity
- 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
- plasma membrane
- extracellular region
- extracellular exosome
- cell surface
- basolateral plasma membrane
- extracellular space
| | Biological process | - 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 |
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| Orthologs |
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| Species | Human | Mouse |
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| Entrez | | |
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| Ensembl | |
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ENSG00000168615
ENSG00000282230 |
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| UniProt | | |
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| RefSeq (mRNA) | | |
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| RefSeq (protein) | | |
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| Location (UCSC) | Chr 8: 39 – 39.11 Mb | Chr 8: 25.44 – 25.51 Mb |
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| PubMed search | [3] | [4] |
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| Wikidata |
| View/Edit Human | View/Edit Mouse |
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Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.[5][6]
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:
References
- ^ a b c ENSG00000282230 GRCh38: Ensembl release 89: ENSG00000168615, ENSG00000282230 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031555 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ 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.
- ^ a b "Entrez Gene: ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma)".
- ^ 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.
- ^ a b 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. Bibcode:2002PNAS...9916899M. 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
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