ADAMTS9

ADAMTS9
Identifiers
Aliases	ADAMTS9, ADAM metallopeptidase with thrombospondin type 1 motif 9
External IDs	OMIM: 605421; MGI: 1916320; HomoloGene: 18821; GeneCards: ADAMTS9; OMA:ADAMTS9 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3p14.1 Start 64,515,654 bp End 64,688,000 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 D1 Start 92,749,680 bp End 92,920,473 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve endometrium parietal pleura body of uterus right ventricle pericardium upper lobe of left lung left uterine tube left coronary artery ascending aorta Top expressed in renal corpuscle gastrula molar external carotid artery cumulus cell vas deferens left lung lobe dermis Gonadal ridge efferent ductule More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding peptidase activity metalloendopeptidase activity endopeptidase activity hydrolase activity metallopeptidase activity metal ion binding Cellular component extracellular region cell surface extracellular space extracellular matrix endoplasmic reticulum intracellular membrane-bounded organelle collagen-containing extracellular matrix Biological process multicellular organism development protein transport regulation of developmental pigmentation vesicle-mediated transport positive regulation of melanocyte differentiation proteolysis glycoprotein catabolic process heart valve morphogenesis ventricular cardiac muscle tissue development negative regulation of endothelial cell migration extracellular matrix organization aorta morphogenesis endothelial cell-matrix adhesion negative regulation of sprouting angiogenesis response to bacterium Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 56999 101401 Ensembl ENSG00000163638 ENSMUSG00000030022 UniProt Q9P2N4 n/a RefSeq (mRNA) NM_182920 NM_001318781 NM_020249 NM_182921 NM_175314 RefSeq (protein) NP_001305710 NP_891550 n/a Location (UCSC) Chr 3: 64.52 – 64.69 Mb Chr 6: 92.75 – 92.92 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

A disintegrin and metalloproteinase with thrombospondin motifs 9 is an enzyme that in humans is encoded by the ADAMTS9 gene.

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) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. Members of the ADAMTS family have been implicated in the cleavage of proteoglycans, the control of organ shape during development, and the inhibition of angiogenesis. This gene is localized to chromosome 3p14.3-p14.2, an area known to be lost in hereditary renal tumors.

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.
• Nagase T, Kikuno R, Ishikawa KI, et al. (2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
• 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.
• Somerville RP, Longpre JM, Jungers KA, et al. (2003). "Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1". J. Biol. Chem. 278 (11): 9503–13. doi:10.1074/jbc.M211009200. PMID 12514189.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Cross NA, Chandrasekharan S, Jokonya N, et al. (2005). "The expression and regulation of ADAMTS-1, -4, -5, -9, and -15, and TIMP-3 by TGFbeta1 in prostate cells: relevance to the accumulation of versican". Prostate. 63 (3): 269–75. doi:10.1002/pros.20182. PMID 15599946. S2CID 24137815.
• Zeng W, Corcoran C, Collins-Racie LA, et al. (2006). "Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: comparative analyses with ADAMTS-5, -9, -16 and -18". Biochim. Biophys. Acta. 1760 (3): 517–24. doi:10.1016/j.bbagen.2006.01.013. PMID 16507336.
• Koo BH, Longpré JM, Somerville RP, et al. (2006). "Cell-surface processing of pro-ADAMTS9 by furin". J. Biol. Chem. 281 (18): 12485–94. doi:10.1074/jbc.M511083200. PMID 16537537.
• Lo PH, Leung AC, Kwok CY, et al. (2007). "Identification of a tumor suppressive critical region mapping to 3p14.2 in esophageal squamous cell carcinoma and studies of a candidate tumor suppressor gene, ADAMTS9". Oncogene. 26 (1): 148–57. doi:10.1038/sj.onc.1209767. PMID 16799631.

External links

• The MEROPS online database for peptidases and their inhibitors: M12.021
• Human ADAMTS9 genome location and ADAMTS9 gene details page in the UCSC Genome Browser.