ADAM metallopeptidase with thrombospondin type 1 motif 10
Last updated 18 Aug 2020
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The ADAMTS10 gene provides instructions for making an enzyme that is found in many of the body's cells and tissues. This enzyme is part of a family of metalloproteases, which are zinc-containing enzymes that cut apart other proteins. Although the function of the ADAMTS10 enzyme is unknown, it is critical for growth before and after birth. Researchers believe that it may be involved in the development of structures including the skin, eyes, heart, and skeleton.
Normal function
The ADAMTS10 gene provides instructions for making an enzyme that is found in many of the body's cells and tissues. This enzyme is part of a family of metalloproteases, which are zinc-containing enzymes that cut apart other proteins. Although the function of the ADAMTS10 enzyme is unknown, it is critical for growth before and after birth. Researchers believe that it may be involved in the development of structures including the skin, eyes, heart, and skeleton.
Conditions referring to this gene or chromosome
Other names
a disintegrin and metalloproteinase with thrombospondin motifs 10
a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 10
a disintegrin-like and metalloprotease domain with thrombospondin type I repeats 10
ADAM metallopeptidase with thrombospondin type 1 motif, 10
ADAM-TS10
ADAMTS-10
ATS10_HUMAN
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Further reading and references
- ADAM metallopeptidase with thrombospondin type 1 motif 10; MedlinePlus, National Library of Medicine.
- Dagoneau N, Benoist-Lasselin C, Huber C, Faivre L, Megarbane A, Alswaid A, Dollfus H, Alembik Y, Munnich A, Legeai-Mallet L, Cormier-Daire V. ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome. Am J Hum Genet. 2004 Nov;75(5):801-6. doi: 10.1086/425231. Epub 2004 Sep 13.
- Kutz WE, Wang LW, Dagoneau N, Odrcic KJ, Cormier-Daire V, Traboulsi EI, Apte SS. Functional analysis of an ADAMTS10 signal peptide mutation in Weill-Marchesani syndrome demonstrates a long-range effect on secretion of the full-length enzyme. Hum Mutat. 2008 Dec;29(12):1425-34. doi: 10.1002/humu.20797.
- Nicholson AC, Malik SB, Logsdon JM Jr, Van Meir EG. Functional evolution of ADAMTS genes: evidence from analyses of phylogeny and gene organization. BMC Evol Biol. 2005 Feb 4;5:11. doi: 10.1186/1471-2148-5-11.
- Somerville RP, Jungers KA, Apte SS. Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation. J Biol Chem. 2004 Dec 3;279(49):51208-17. doi: 10.1074/jbc.M409036200. Epub 2004 Sep 7.
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