THC Science

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; OMA:ADAM9 - orthologs
Gene location (Human)
Chr.	Chromosome 8 (human)
End	39,105,445 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	25,506,943 bp
RNA expression pattern
	Top expressed in
	Top expressed in
	More reference expression data
	n/a
Gene ontology
Molecular function
Cellular component
Biological process
	Sources:Amigo / QuickGO
Orthologs
	8754
	11502
	ENSG00000168615; ENSG00000282230
	ENSMUSG00000031555
	Q13443
	Q61072
	NM_001005845; NM_003816
	NM_001270996; NM_007404
	NP_003807
	NP_001257925; NP_031430
	Wikidata
View/Edit Human	View/Edit Mouse

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.

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

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

[refGRCh38Ensembl-1] ENSG00000282230 GRCh38: Ensembl release 89: ENSG00000168615, ENSG00000282230 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid8647900-5] 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.

[entrez-6] "Entrez Gene: ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma)".

[pmid10527948-7] 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.

[pmid10531379-8] 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.

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Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

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