ADAMTS9

ADAM metallopeptidase with thrombospondin type 1 motif, 9
Identifiers
Symbols	ADAMTS9; FLJ42955; KIAA1312
External IDs	OMIM: 605421 HomoloGene: 18821 GeneCards: ADAMTS9 Gene
Gene Ontology Molecular function • metalloendopeptidase activity • peptidase activity • metallopeptidase activity • zinc ion binding • metal ion binding Cellular component • extracellular region • proteinaceous extracellular matrix Biological process • proteolysis • glycoprotein catabolic process • multicellular organismal development Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	56999	n/a
Ensembl	ENSG00000163638	n/a
UniProt	Q9P2N4	n/a
RefSeq (mRNA)	NM_182920	n/a
RefSeq (protein)	NP_891550	n/a
Location (UCSC)	Chr 3: 64.5 – 64.67 Mb	n/a
PubMed search	[1]	n/a

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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. 
• 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