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{{Infobox_gene}}
{{PBB_Controls
'''A disintegrin and metalloproteinase with thrombospondin motifs 1''' is an [[enzyme]] that in humans is encoded by the ''ADAMTS1'' [[gene]].<ref name="pmid10438512">{{cite journal | vauthors = Vazquez F, Hastings G, Ortega MA, Lane TF, Oikemus S, Lombardo M, Iruela-Arispe ML | title = METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity | journal = J Biol Chem | volume = 274 | issue = 33 | pages = 23349–57 |date=September 1999| pmid = 10438512 | pmc =  | doi =10.1074/jbc.274.33.23349  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ADAMTS1 ADAM metallopeptidase with thrombospondin type 1 motif, 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9510| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ADAM metallopeptidase with thrombospondin type 1 motif, 1
| HGNCid = 217
| Symbol = ADAMTS1
| AltSymbols =; C3-C5; KIAA1346; METH1
| OMIM = 605174
| ECnumber = 
| Homologene = 21381
| MGIid = 109249
| GeneAtlas_image1 = PBB_GE_ADAMTS1_222162_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0031410 |text = cytoplasmic vesicle}}
| Process = {{GNF_GO|id=GO:0001542 |text = ovulation (sensu Mammalia)}} {{GNF_GO|id=GO:0001822 |text = kidney development}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9510
    | Hs_Ensembl = ENSG00000154734
    | Hs_RefseqProtein = NP_008919
    | Hs_RefseqmRNA = NM_006988
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 21
    | Hs_GenLoc_start = 27130479
    | Hs_GenLoc_end = 27139599
    | Hs_Uniprot = Q9UHI8
    | Mm_EntrezGene = 11504
    | Mm_Ensembl = ENSMUSG00000022893
    | Mm_RefseqmRNA = NM_009621
    | Mm_RefseqProtein = NP_033751
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 85683023
    | Mm_GenLoc_end = 85692295
    | Mm_Uniprot = Q05DU9
  }}
}}
'''ADAM metallopeptidase with thrombospondin type 1 motif, 1''', also known as '''METH-1'''<ref>[http://clincancerres.aacrjournals.org/cgi/content/abstract/7/11/3437 Expression of METH-1 and METH-2 in Pancreatic Cancer -- Masui et ...]</ref> or '''ADAMTS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADAMTS1 ADAM metallopeptidase with thrombospondin type 1 motif, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9510| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez" />
{{PBB_Summary
 
| section_title =
== Interactions ==
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ADAMTS1 ADAM metallopeptidase with thrombospondin type 1 motif, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9510| accessdate = }}</ref>
 
}}
ADAMTS1 has been shown to [[Protein-protein interaction|interact]] with [[Vascular endothelial growth factor A]].<ref name="pmid12716911">{{cite journal | vauthors = Luque A, Carpizo DR, Iruela-Arispe ML | title = ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165 | journal = J. Biol. Chem. | volume = 278 | issue = 26 | pages = 23656–65 | year = June 2003 | pmid = 12716911 | doi = 10.1074/jbc.M212964200 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Tang BL, Hong W |title=ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats |journal=FEBS Lett. |volume=445 |issue= 2–3 |pages= 223–5 |year= 1999 |pmid= 10094461 |doi=10.1016/S0014-5793(99)00119-2 }}
| citations =
*{{cite journal  | author=Hirohata S |title=[ADAMTS family--new extracellular matrix degrading enzyme] |journal=Seikagaku |volume=73 |issue= 11 |pages= 1333–7 |year= 2002 |pmid= 11831030 |doi=  }}
*{{cite journal  | author=Tang BL, Hong W |title=ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats. |journal=FEBS Lett. |volume=445 |issue= 2-3 |pages= 223-5 |year= 1999 |pmid= 10094461 |doi=  }}
*{{cite journal  | vauthors=Kuno K, Kanada N, Nakashima E |title=Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene |journal=J. Biol. Chem. |volume=272 |issue= 1 |pages= 556–62 |year= 1997 |pmid= 8995297 |doi=10.1074/jbc.272.1.556 |display-authors=etal}}
*{{cite journal  | author=Hirohata S |title=[ADAMTS family--new extracellular matrix degrading enzyme] |journal=Seikagaku |volume=73 |issue= 11 |pages= 1333-7 |year= 2002 |pmid= 11831030 |doi=  }}
*{{cite journal  | vauthors=Kuno K, Matsushima K |title=ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region |journal=J. Biol. Chem. |volume=273 |issue= 22 |pages= 13912–7 |year= 1998 |pmid= 9593739 |doi=10.1074/jbc.273.22.13912 }}
*{{cite journal  | author=Kuno K, Kanada N, Nakashima E, ''et al.'' |title=Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. |journal=J. Biol. Chem. |volume=272 |issue= 1 |pages= 556-62 |year= 1997 |pmid= 8995297 |doi=  }}
*{{cite journal  | vauthors=Kuno K, Terashima Y, Matsushima K |title=ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18821–6 |year= 1999 |pmid= 10373500 |doi=10.1074/jbc.274.26.18821 }}
*{{cite journal  | author=Kuno K, Matsushima K |title=ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region. |journal=J. Biol. Chem. |volume=273 |issue= 22 |pages= 13912-7 |year= 1998 |pmid= 9593739 |doi=  }}
*{{cite journal  | vauthors=Nagase T, Kikuno R, Ishikawa KI |title=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 |journal=DNA Res. |volume=7 |issue= 1 |pages= 65–73 |year= 2000 |pmid= 10718198 |doi=10.1093/dnares/7.1.65 |display-authors=etal}}
*{{cite journal  | author=Kuno K, Terashima Y, Matsushima K |title=ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix. |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18821-6 |year= 1999 |pmid= 10373500 |doi= }}
*{{cite journal  | vauthors=Glienke J, Schmitt AO, Pilarsky C |title=Differential gene expression by endothelial cells in distinct angiogenic states |journal=Eur. J. Biochem. |volume=267 |issue= 9 |pages= 2820–30 |year= 2000 |pmid= 10785405 |doi=10.1046/j.1432-1327.2000.01325.x |display-authors=etal}}
*{{cite journal  | author=Vázquez F, Hastings G, Ortega MA, ''et al.'' |title=METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23349-57 |year= 1999 |pmid= 10438512 |doi= }}
*{{cite journal  | vauthors=Shindo T, Kurihara H, Kuno K |title=ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function |journal=J. Clin. Invest. |volume=105 |issue= 10 |pages= 1345–52 |year= 2000 |pmid= 10811842 |doi=10.1172/JCI8635 | pmc=315464  |display-authors=etal}}
*{{cite journal  | author=Nagase T, Kikuno R, Ishikawa KI, ''et al.'' |title=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. |journal=DNA Res. |volume=7 |issue= 1 |pages= 65-73 |year= 2000 |pmid= 10718198 |doi=  }}
*{{cite journal  | vauthors=Hattori M, Fujiyama A, Taylor TD |title=The DNA sequence of human chromosome 21 |journal=Nature |volume=405 |issue= 6784 |pages= 311–9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 |display-authors=etal}}
*{{cite journal  | author=Glienke J, Schmitt AO, Pilarsky C, ''et al.'' |title=Differential gene expression by endothelial cells in distinct angiogenic states. |journal=Eur. J. Biochem. |volume=267 |issue= 9 |pages= 2820-30 |year= 2000 |pmid= 10785405 |doi=  }}
*{{cite journal  | vauthors=Kuno K, Okada Y, Kawashima H |title=ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan |journal=FEBS Lett. |volume=478 |issue= 3 |pages= 241–5 |year= 2000 |pmid= 10930576 |doi=10.1016/S0014-5793(00)01854-8 |display-authors=etal}}
*{{cite journal  | author=Shindo T, Kurihara H, Kuno K, ''et al.'' |title=ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function. |journal=J. Clin. Invest. |volume=105 |issue= 10 |pages= 1345-52 |year= 2000 |pmid= 10811842 |doi=  }}
*{{cite journal  | vauthors=Sandy JD, Westling J, Kenagy RD |title=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 |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 13372–8 |year= 2001 |pmid= 11278559 |doi= 10.1074/jbc.M009737200 |display-authors=etal}}
*{{cite journal  | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal  | vauthors=Wei P, Zhao YG, Zhuang L |title=Protein engineering and properties of human metalloproteinase and thrombospondin 1 |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 478–88 |year= 2002 |pmid= 12054626 |doi= 10.1016/S0006-291X(02)00255-3 |display-authors=etal}}
*{{cite journal  | author=Kuno K, Okada Y, Kawashima H, ''et al.'' |title=ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan. |journal=FEBS Lett. |volume=478 |issue= 3 |pages= 241-5 |year= 2000 |pmid= 10930576 |doi=  }}
*{{cite journal  | vauthors=Rodríguez-Manzaneque JC, Westling J, Thai SN |title=ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 501–8 |year= 2002 |pmid= 12054629 |doi= 10.1016/S0006-291X(02)00254-1 |display-authors=etal}}
*{{cite journal  | author=Sandy JD, Westling J, Kenagy RD, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 13372-8 |year= 2001 |pmid= 11278559 |doi= 10.1074/jbc.M009737200 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Wei P, Zhao YG, Zhuang L, ''et al.'' |title=Protein engineering and properties of human metalloproteinase and thrombospondin 1. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 478-88 |year= 2002 |pmid= 12054626 |doi= 10.1016/S0006-291X(02)00255-3 }}
*{{cite journal  | vauthors=Luque A, Carpizo DR, Iruela-Arispe ML |title=ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165 |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 23656–65 |year= 2003 |pmid= 12716911 |doi= 10.1074/jbc.M212964200 }}
*{{cite journal  | author=Rodríguez-Manzaneque JC, Westling J, Thai SN, ''et al.'' |title=ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 501-8 |year= 2002 |pmid= 12054629 |doi= 10.1016/S0006-291X(02)00254-1 }}
*{{cite journal  | vauthors=Russell DL, Doyle KM, Ochsner SA |title=Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 42330–9 |year= 2004 |pmid= 12907688 |doi= 10.1074/jbc.M300519200 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Luque A, Carpizo DR, Iruela-Arispe ML |title=ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 23656-65 |year= 2003 |pmid= 12716911 |doi= 10.1074/jbc.M212964200 }}
*{{cite journal  | author=Russell DL, Doyle KM, Ochsner SA, ''et al.'' |title=Processing and localization of ADAMTS-1 and proteolytic cleavage of versican during cumulus matrix expansion and ovulation. |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 42330-9 |year= 2004 |pmid= 12907688 |doi= 10.1074/jbc.M300519200 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
}}
{{refend}}
{{refend}}
==External links==
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M12.222 M12.222]
* [http://AtlasGeneticsOncology.org/Genes/ADAMTS1ID574ch21q21.html ADAMTS1] on the [[Atlas of Genetics and Cytogenetics in Oncology and Haematology|Atlas of Genetics and Oncology]]
* {{UCSC gene info|ADAMTS1}}
{{Metalloproteinases}}
[[Category:ADAMTS]]


{{gene-21-stub}}
{{gene-21-stub}}
{{WikiDoc Sources}}

Latest revision as of 17:48, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

A disintegrin and metalloproteinase with thrombospondin motifs 1 is an enzyme that in humans is encoded by the ADAMTS1 gene.[1][2]

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.[2]

Interactions

ADAMTS1 has been shown to interact with Vascular endothelial growth factor A.[3]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: ADAMTS1 ADAM metallopeptidase with thrombospondin type 1 motif, 1".
  3. ↑ 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

External links


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