ADAMTS3

ADAM metallopeptidase with thrombospondin type 1 motif, 3
Identifiers
Symbols	ADAMTS3 ; ADAMTS-4
External IDs	OMIM: 605011 MGI: 3045353 HomoloGene: 8596 GeneCards: ADAMTS3 Gene
EC number	3.4.24.-
Gene ontology Molecular function • endopeptidase activity • metalloendopeptidase activity • protein binding • heparin binding • zinc ion binding Cellular component • extracellular region • proteinaceous extracellular matrix • extracellular space • extracellular matrix • extracellular exosome Biological process • vascular endothelial growth factor production • protein processing • extracellular matrix organization • collagen fibril organization • collagen catabolic process • collagen biosynthetic process • extracellular fibril organization • positive regulation of vascular endothelial growth factor signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9508	330119
Ensembl	ENSG00000156140	ENSMUSG00000043635
UniProt	O15072	E9Q287
RefSeq (mRNA)	NM_014243	NM_001081401
RefSeq (protein)	NP_055058	NP_001074870
Location (UCSC)	Chr 4: 72.28 – 72.57 Mb	Chr 5: 89.68 – 89.88 Mb
PubMed search

A disintegrin and metalloproteinase with thrombospondin motifs 3 is an enzyme that in humans is encoded by the ADAMTS3 gene.^[1][2]

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. The protein encoded by this gene is the major procollagen II N-propeptidase. A deficiency of this protein may be responsible for dermatosparaxis, a genetic defect of connective tissues.^[2]

References

1. Tang BL, Hong W (Apr 1999). "ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats". FEBS Lett 445 (2–3): 223–5. doi:10.1016/S0014-5793(99)00119-2. PMID 10094461.
2. "Entrez Gene: ADAMTS3 ADAM metallopeptidase with thrombospondin type 1 motif, 3".

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.
• Martel-Pelletier J, Welsch DJ, Pelletier JP (2002). "Metalloproteases and inhibitors in arthritic diseases". Best practice & research. Clinical rheumatology 15 (5): 805–29. doi:10.1053/berh.2001.0195. PMID 11812023.
• Hirohata S (2002). "[ADAMTS family--new extracellular matrix degrading enzyme]". Seikagaku 73 (11): 1333–7. PMID 11831030.
• Nagase T, Ishikawa K, Nakajima D; et al. (1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 4 (2): 141–50. doi:10.1093/dnares/4.2.141. PMID 9205841.
• Hurskainen TL, Hirohata S, Seldin MF, Apte SS (1999). "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family". J. Biol. Chem. 274 (36): 25555–63. doi:10.1074/jbc.274.36.25555. PMID 10464288.
• Fernandes RJ, Hirohata S, Engle JM; et al. (2001). "Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis". J. Biol. Chem. 276 (34): 31502–9. doi:10.1074/jbc.M103466200. PMID 11408482.
• Colige A, Vandenberghe I, Thiry M; et al. (2002). "Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3". J. Biol. Chem. 277 (8): 5756–66. doi:10.1074/jbc.M105601200. PMID 11741898.
• 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.

External links

• The MEROPS online database for peptidases and their inhibitors: M12.220