ADAMTS12

A disintegrin and metalloproteinase with thrombospondin motifs 12 is an enzyme that in humans is encoded by the ADAMTS12 gene.[5]

ADAMTS12
Identifiers
Aliases	ADAMTS12, PRO4389, ADAM metallopeptidase with thrombospondin type 1 motif 12
External IDs	OMIM: 606184 MGI: 2146046 HomoloGene: 12808 GeneCards: ADAMTS12
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5p13.3-p13.2 Start 33,523,535 bp[1] End 33,892,019 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 A1 Start 11,064,790 bp[2] End 11,349,231 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • metal ion binding • peptidase activity • GO:0001948 protein binding • metalloendopeptidase activity • hydrolase activity • metallopeptidase activity • zinc ion binding Cellular component • extracellular region • extracellular matrix • collagen-containing extracellular matrix Biological process • regulation of endothelial tube morphogenesis • proteoglycan catabolic process • negative regulation of hepatocyte growth factor receptor signaling pathway • negative regulation of cellular response to vascular endothelial growth factor stimulus • cellular response to tumor necrosis factor • cellular response to BMP stimulus • negative regulation of cellular response to hepatocyte growth factor stimulus • proteolysis • negative regulation of chondrocyte differentiation • cellular response to interleukin-1 • regulation of inflammatory response • proteolysis involved in cellular protein catabolic process • cell-matrix adhesion • cell migration Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	81792	239337
Ensembl	ENSG00000151388 ENSG00000281690	ENSMUSG00000047497
UniProt	P58397	Q811B3
RefSeq (mRNA)	NM_030955 NM_001324511 NM_001324512	NM_175501
RefSeq (protein)	NP_001311440 NP_001311441 NP_112217	NP_780710
Location (UCSC)	Chr 5: 33.52 – 33.89 Mb	Chr 15: 11.06 – 11.35 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[5]

References

1. ENSG00000281690 GRCh38: Ensembl release 89: ENSG00000151388, ENSG00000281690 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000047497 - 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. "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
• Human ADAMTS12 genome location and ADAMTS12 gene details page in the UCSC Genome Browser.