ADAMTS1

A disintegrin and metalloproteinase with thrombospondin motifs 1 is an enzyme that in humans is encoded by the ADAMTS1 gene.[5][6]

ADAMTS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2JIH, 2V4B, 3Q2G, 3Q2H
Identifiers
Aliases	ADAMTS1, C3-C5, METH1, ADAM metallopeptidase with thrombospondin type 1 motif 1
External IDs	OMIM: 605174 MGI: 109249 HomoloGene: 21381 GeneCards: ADAMTS1
Gene location (Human) Chr. Chromosome 21 (human)[1] Band 21q21.3 Start 26,835,755 bp[1] End 26,845,409 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16 C3.3|16 48.2 cM Start 85,793,827 bp[2] End 85,803,113 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • heparin binding • zinc ion binding • metal ion binding • peptidase activity • metalloendopeptidase activity • hydrolase activity • metallopeptidase activity Cellular component • extracellular region • basement membrane • cytoplasmic vesicle • extracellular matrix • collagen-containing extracellular matrix Biological process • ovulation from ovarian follicle • heart trabecula formation • kidney development • proteolysis • integrin-mediated signaling pathway • negative regulation of cell proliferation • positive regulation of G1/S transition of mitotic cell cycle • positive regulation of vascular smooth muscle cell proliferation • positive regulation of vascular associated smooth muscle cell migration Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9510	11504
Ensembl	ENSG00000154734	ENSMUSG00000022893
UniProt	Q9UHI8	P97857
RefSeq (mRNA)	NM_006988	NM_009621
RefSeq (protein)	NP_008919	NP_033751
Location (UCSC)	Chr 21: 26.84 – 26.85 Mb	Chr 16: 85.79 – 85.8 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) 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 contains two disintegrin loops and three C-terminal TS motifs and has anti-angiogenic activity. The expression of this gene may be associated with various inflammatory processes as well as development of cancer cachexia. This gene is likely to be necessary for normal growth, fertility, and organ morphology and function.[6]

Interactions

ADAMTS1 has been shown to interact with Vascular endothelial growth factor A.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000154734 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022893 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Vazquez F, Hastings G, Ortega MA, Lane TF, Oikemus S, Lombardo M, Iruela-Arispe ML (September 1999). "METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity". J Biol Chem. 274 (33): 23349–57. doi:10.1074/jbc.274.33.23349. PMID 10438512.
6. "Entrez Gene: ADAMTS1 ADAM metallopeptidase with thrombospondin type 1 motif, 1".
7. Luque A, Carpizo DR, Iruela-Arispe ML (June 2003). "ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165". J. Biol. Chem. 278 (26): 23656–65. doi:10.1074/jbc.M212964200. PMID 12716911.

Further reading

• Tang BL, Hong W (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. S2CID 37955930.
• Hirohata S (2002). "[ADAMTS family--new extracellular matrix degrading enzyme]". Seikagaku. 73 (11): 1333–7. PMID 11831030.
• Kuno K, Kanada N, Nakashima E, et al. (1997). "Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene". J. Biol. Chem. 272 (1): 556–62. doi:10.1074/jbc.272.1.556. PMID 8995297.
• Kuno K, Matsushima K (1998). "ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region". J. Biol. Chem. 273 (22): 13912–7. doi:10.1074/jbc.273.22.13912. PMID 9593739.
• Kuno K, Terashima Y, Matsushima K (1999). "ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix". J. Biol. Chem. 274 (26): 18821–6. doi:10.1074/jbc.274.26.18821. PMID 10373500.
• 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.
• Glienke J, Schmitt AO, Pilarsky C, et al. (2000). "Differential gene expression by endothelial cells in distinct angiogenic states". Eur. J. Biochem. 267 (9): 2820–30. doi:10.1046/j.1432-1327.2000.01325.x. PMID 10785405.
• Shindo T, Kurihara H, Kuno K, et al. (2000). "ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function". J. Clin. Invest. 105 (10): 1345–52. doi:10.1172/JCI8635. PMC 315464. PMID 10811842.
• Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21". Nature. 405 (6784): 311–9. Bibcode:2000Natur.405..311H. doi:10.1038/35012518. PMID 10830953.
• Kuno K, Okada Y, Kawashima H, et al. (2000). "ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan". FEBS Lett. 478 (3): 241–5. doi:10.1016/S0014-5793(00)01854-8. PMID 10930576. S2CID 32699689.
• Sandy JD, Westling J, Kenagy RD, et al. (2001). "Versican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4". J. Biol. Chem. 276 (16): 13372–8. doi:10.1074/jbc.M009737200. PMID 11278559.
• Wei P, Zhao YG, Zhuang L, et al. (2002). "Protein engineering and properties of human metalloproteinase and thrombospondin 1". Biochem. Biophys. Res. Commun. 293 (1): 478–88. doi:10.1016/S0006-291X(02)00255-3. PMID 12054626.
• Rodríguez-Manzaneque JC, Westling J, Thai SN, et al. (2002). "ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors". Biochem. Biophys. Res. Commun. 293 (1): 501–8. doi:10.1016/S0006-291X(02)00254-1. PMID 12054629.
• 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.
• Luque A, Carpizo DR, Iruela-Arispe ML (2003). "ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165". J. Biol. Chem. 278 (26): 23656–65. doi:10.1074/jbc.M212964200. PMID 12716911.
• Russell DL, Doyle KM, Ochsner SA, et al. (2004). "Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation". J. Biol. Chem. 278 (43): 42330–9. doi:10.1074/jbc.M300519200. PMID 12907688.
• 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.

External links

• The MEROPS online database for peptidases and their inhibitors: M12.222
• ADAMTS1 on the Atlas of Genetics and Oncology
• Human ADAMTS1 genome location and ADAMTS1 gene details page in the UCSC Genome Browser.
• Overview of all the structural information available in the PDB for UniProt: Q9UHI8 (A disintegrin and metalloproteinase with thrombospondin motifs 1) at the PDBe-KB.