ADAMTS10
| ADAM metallopeptidase with thrombospondin type 1 motif, 10 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | ADAMTS10 ; ADAM-TS10; ADAMTS-10; WMS; WMS1 | ||||||||||||
| External IDs | OMIM: 608990 MGI: 2449112 HomoloGene: 81940 GeneCards: ADAMTS10 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 81794 | 224697 | |||||||||||
| Ensembl | ENSG00000142303 | ENSMUSG00000024299 | |||||||||||
| UniProt | Q9H324 | P58459 | |||||||||||
| RefSeq (mRNA) | NM_001282352 | NM_172619 | |||||||||||
| RefSeq (protein) | NP_001269281 | NP_766207 | |||||||||||
| Location (UCSC) |
Chr 19: 8.58 – 8.61 Mb |
Chr 17: 33.52 – 33.55 Mb | |||||||||||
| PubMed search | |||||||||||||
A disintegrin and metalloproteinase with thrombospondin motifs 10 is an enzyme that in humans is encoded by the ADAMTS10 gene.[1]
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.[1]
References
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.
- 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. PMC 139241. 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. PMC 1182109. PMID 15368195.
External links
- GeneReviews/NIH/NCBI/UW entry on Weill-Marchesani Syndrome
- The MEROPS online database for peptidases and their inhibitors: M12.235
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