ADAMTS3

ADAMTS3
Identifiers
AliasesADAMTS3, ADAMTS-4, ADAM metallopeptidase with thrombospondin type 1 motif 3
External IDsMGI: 3045353 HomoloGene: 8596 GeneCards: ADAMTS3
Gene location (Human)
Chr.Chromosome 4 (human)[1]
Band4q13.3Start72,280,969 bp[1]
End72,569,386 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

9508

330119

Ensembl

ENSG00000156140

ENSMUSG00000043635

UniProt

O15072

n/a

RefSeq (mRNA)

NM_014243

NM_001081401
NM_177872

RefSeq (protein)

NP_055058

n/a

Location (UCSC)Chr 4: 72.28 – 72.57 MbChr 5: 89.68 – 89.88 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

A disintegrin and metalloproteinase with thrombospondin motifs 3 is an enzyme that in humans is encoded by the ADAMTS3 gene.[5][6]

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.[6]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000156140 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000043635 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ 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.
  6. 1 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.


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