ADAMTS12

ADAM metallopeptidase with thrombospondin type 1 motif, 12
Identifiers
Symbols	ADAMTS12 ; PRO4389
External IDs	OMIM: 606184 MGI: 2146046 HomoloGene: 12808 GeneCards: ADAMTS12 Gene
Gene ontology Molecular function • metalloendopeptidase activity • protein binding • zinc ion binding Cellular component • proteinaceous extracellular matrix • extracellular matrix Biological process • cell-matrix adhesion • cell migration • proteoglycan catabolic process • negative regulation of chondrocyte differentiation • regulation of inflammatory response • proteolysis involved in cellular protein catabolic process • cellular response to interleukin-1 • cellular response to tumor necrosis factor • cellular response to BMP stimulus • regulation of endothelial tube morphogenesis • negative regulation of hepatocyte growth factor receptor signaling pathway • negative regulation of cellular response to vascular endothelial growth factor stimulus • negative regulation of cellular response to hepatocyte growth factor stimulus Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	81792	239337
Ensembl	ENSG00000151388	ENSMUSG00000047497
UniProt	P58397	Q811B3
RefSeq (mRNA)	NM_030955	NM_175501
RefSeq (protein)	NP_112217	NP_780710
Location (UCSC)	Chr 5: 33.52 – 33.89 Mb	Chr 15: 11.06 – 11.35 Mb
PubMed search

A disintegrin and metalloproteinase with thrombospondin motifs 12 is an enzyme that in humans is encoded by the ADAMTS12 gene.^[1][2]

This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS-1) motif. Individual members of this family differ in the number of C-terminal TS-1 motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains eight TS-1 motifs. It may play roles in pulmonary cells during fetal development or in tumor processes through its proteolytic activity or as a molecule potentially involved in regulation of cell adhesion.^[2]

References

1. Cal S, Arguelles JM, Fernandez PL, Lopez-Otin C (May 2001). "Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats". J Biol Chem 276 (21): 17932–40. doi:10.1074/jbc.M100534200. PMID 11279086.
2. "Entrez Gene: ADAMTS12 ADAM metallopeptidase with thrombospondin type 1 motif, 12".

Further reading

• Tang BL (2001). "ADAMTS: a novel family of extracellular matrix proteases.". Int. J. Biochem. Cell Biol. 33 (1): 33–44. doi:10.1016/S1357-2725(00)00061-3. PMID 11167130.
• Llamazares M, Obaya AJ, Moncada-Pazos A; et al. (2008). "The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway.". J. Cell. Sci. 120 (Pt 20): 3544–52. doi:10.1242/jcs.005751. PMID 17895370.
• Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Liu CJ, Kong W, Xu K; et al. (2006). "ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein.". J. Biol. Chem. 281 (23): 15800–8. doi:10.1074/jbc.M513433200. PMC 1483932. PMID 16611630.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Clark HF, Gurney AL, Abaya E; et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• 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.
• Dias Neto E, Correa RG, Verjovski-Almeida S; et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.

External links

• The MEROPS online database for peptidases and their inhibitors: M12.237