ADAMTS10

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ADAM metallopeptidase with thrombospondin type 1 motif, 10
Identifiers
Symbol(s)	ADAMTS10; WMS; ADAM-TS10
External IDs	OMIM: 608990 MGI: 2449112 Homologene: 81940
Gene ontology Molecular Function: • molecular_function • metalloendopeptidase activity • zinc ion binding • metal ion binding Cellular Component: • proteinaceous extracellular matrix • extracellular matrix Biological Process: • proteolysis • integrin-mediated signaling pathway • biological_process
RNA expression pattern
More reference expression data
Orthologs
	Human	Mouse
Entrez	81794	224697
Ensembl	ENSG00000142303	ENSMUSG00000024299
Uniprot	Q9H324	P58459
Refseq	NM_030957 (mRNA) NP_112219 (protein)	XM_905505 (mRNA) XP_910598 (protein)
Location	Chr 19: 8.55 - 8.58 Mb	Chr 17: 33.13 - 33.16 Mb
Pubmed search	[1]	[2]

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Overview

ADAM metallopeptidase with thrombospondin type 1 motif, 10, also known as ADAMTS10, is a human gene.

This gene belongs to the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 motifs) family of zinc-dependent proteases. ADAMTS proteases are complex secreted enzymes containing a prometalloprotease domain of the reprolysin type attached to an ancillary domain with a highly conserved structure that includes at least one thrombospondin type 1 repeat. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. The product of this gene plays a major role in growth and in skin, lens, and heart development. It is also a candidate gene for autosomal recessive Weill-Marchesani syndrome.

Further reading

• Tang BL (2001). "ADAMTS: a novel family of extracellular matrix proteases.". Int. J. Biochem. Cell Biol. 33 (1): 33–44. PMID 11167130.
• Faivre L, Dollfus H, Lyonnet S, et al. (2004). "Clinical homogeneity and genetic heterogeneity in Weill-Marchesani syndrome.". Am. J. Med. Genet. A 123 (2): 204–7. doi:10.1002/ajmg.a.20289. PMID 14598350.
• Apte SS (2004). "A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family.". Int. J. Biochem. Cell Biol. 36 (6): 981–5. doi:10.1016/j.biocel.2004.01.014. PMID 15094112.
• Faivre L, Mégarbané A, Alswaid A, et al. (2002). "Homozygosity mapping of a Weill-Marchesani syndrome locus to chromosome 19p13.3-p13.2.". Hum. Genet. 110 (4): 366–70. doi:10.1007/s00439-002-0689-3. PMID 11941487.
• 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. PMID 12477932.
• Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
• Fu GK, Wang JT, Yang J, et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes.". Genomics 84 (1): 205–10. doi:10.1016/j.ygeno.2004.01.011. PMID 15203218.
• Somerville RP, Jungers KA, Apte SS (2005). "Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation.". J. Biol. Chem. 279 (49): 51208–17. doi:10.1074/jbc.M409036200. PMID 15355968.
• Charrier L, Yan Y, Driss A, et al. (2005). "ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers.". Am. J. Physiol. Gastrointest. Liver Physiol. 288 (2): G346–53. doi:10.1152/ajpgi.00262.2004. PMID 15358598.
• Dagoneau N, Benoist-Lasselin C, Huber C, et al. (2005). "ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome.". Am. J. Hum. Genet. 75 (5): 801–6. doi:10.1086/425231. PMID 15368195.