A Disintegrin And Metalloprotease 9 (ADAM9)

MCMP; MDC9; Mltng; Meltrin Gamma; Metalloprotease/disintegrin/cysteine-rich protein 9; Myeloma cell metalloproteinase; Cellular disintegrin-related protein

SPN	V012
HGNC	216
MGI	105376
PubMed	14997207
RGD	621473
UniProt	Q13443
Wiki	ADAM9

Disintegrin and metalloproteinase domain-containing protein 9 is 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.

Reference

"MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains."
J. Cell Biol. 132:717-726(1996) [PubMed] [Europe PMC] [Abstract]

"Cloning of a novel membrane-linked metalloproteinase from human myeloma cells."
Biochem. J. 318:459-462(1996) [PubMed] [Europe PMC] [Abstract]

"A secreted form of human ADAM9 has an alpha-secretase activity for APP."
Biochem. Biophys. Res. Commun. 293:800-805(2002) [PubMed] [Europe PMC] [Abstract]

"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. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes."
Biochem. Biophys. Res. Commun. 230:335-339(1997) [PubMed] [Europe PMC] [Abstract]

"Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1."
J. Biol. Chem. 274:31693-31699(1999) [PubMed] [Europe PMC] [Abstract]

"A quantitative atlas of mitotic phosphorylation."
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]

"Loss of the metalloprotease ADAM9 leads to cone-rod dystrophy in humans and retinal degeneration in mice."
Am. J. Hum. Genet. 84:683-691(2009) [PubMed] [Europe PMC] [Abstract]

"Exploring the substrate affinities of MMP-3, ADAM-9 and ADAM-10 using molecular modelling and dynamics simulations."
Submitted (JUN-2002) to the PDB data bank