ADAMTS10

ADAMTS10
Identifiers
Aliases	ADAMTS10, ADAM-TS10, ADAMTS-10, WMS, WMS1, ADAM metallopeptidase with thrombospondin type 1 motif 10
External IDs	OMIM: 608990 MGI: 2449112 HomoloGene: 81940 GeneCards: ADAMTS10
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.2 Start 8,580,240 bp End 8,610,735 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 B1 Start 33,743,178 bp End 33,772,756 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right coronary artery ascending aorta cerebellar vermis vena cava parotid gland popliteal artery left coronary artery left uterine tube canal of the cervix body of tongue Top expressed in ascending aorta aortic valve left lung left lung lobe external carotid artery internal carotid artery cerebellar cortex body of femur right lung molar More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activity metalloendopeptidase activity protein binding hydrolase activity metallopeptidase activity metal ion binding molecular function Cellular component microfibril extracellular region extracellular matrix collagen-containing extracellular matrix Biological process proteolysis biological process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 81794 224697 Ensembl ENSG00000142303 ENSMUSG00000024299 UniProt Q9H324 P58459 RefSeq (mRNA) NM_001282352 NM_030957 NM_172619 NM_001329143 NM_001329147 NM_001329151 NM_001329152 NM_001329153 NM_001329154 NM_001329202 NM_001329203 RefSeq (protein) NP_001269281 NP_112219 NP_001316072 NP_001316076 NP_001316080 NP_001316081 NP_001316082 NP_001316083 NP_001316131 NP_001316132 NP_766207 Location (UCSC) Chr 19: 8.58 – 8.61 Mb Chr 17: 33.74 – 33.77 Mb PubMed search
Wikidata
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A disintegrin and metalloproteinase with thrombospondin motifs 10 is an enzyme that in humans is encoded by the ADAMTS10 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. 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. S2CID 13600027.
• 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. S2CID 10463979.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID 27764390.
• 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
• Human ADAMTS10 genome location and ADAMTS10 gene details page in the UCSC Genome Browser.