ADAMTS17

ADAMTS17
Identifiers
Aliases	ADAMTS17 , ADAM metallopeptidase with thrombospondin type 1 motif 17, WMS4
External IDs	OMIM: 607511 MGI: 3588195 HomoloGene: 16373 GeneCards: ADAMTS17
Gene location (Human)
Chr.	Chromosome 15 (human)
End	100,342,005 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	67,153,171 bp
Gene ontology
Molecular function	• peptidase activity ; • metalloendopeptidase activity ; • hydrolase activity ; • metallopeptidase activity ; • metal ion binding ; • nucleic acid binding ;
Cellular component	• extracellular region ;
Biological process	• proteolysis ;
	Sources:Amigo / QuickGO
Orthologs
	170691
	233332
	ENSG00000140470
	ENSMUSG00000058145
	Q8TE56
	n/a
	NM_139057
	NM_001033877
	NP_620688
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 03, 2021

ADAM metallopeptidase with thrombospondin type 1 motif, 17 is a protein that in humans is encoded by the ADAMTS17 gene.^[5]

Function

This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. ADAMTS family members 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 has a high sequence similarity to the protein encoded by ADAMTS19, another family member. The function of this protein has not been determined. [provided by RefSeq, Jul 2008].

Clinical significance

Mutations in ADAMTS17 are associated with Weill-Marchesani syndrome.^[6]

Related Research Articles

A disintegrin and metalloproteinase with thrombospondin motifs 5 also known as ADAMTS5 is an enzyme that in humans is encoded by the ADAMTS5 gene.

A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS2) also known as procollagen I N-proteinase is an enzyme that in humans is encoded by the ADAMTS2 gene.

ADAMs are a family of single-pass transmembrane and secreted metalloendopeptidases. All ADAMs are characterized by a particular domain organization featuring a pro-domain, a metalloprotease, a disintegrin, a cysteine-rich, an epidermal-growth factor like and a transmembrane domain, as well as a C-terminal cytoplasmic tail. Nonetheless, not all human ADAMs have a functional protease domain, which indicates that their biological function mainly depends on protein–protein interactions. Those ADAMs which are active proteases are classified as sheddases because they cut off or shed extracellular portions of transmembrane proteins. For example, ADAM10 can cut off part of the HER2 receptor, thereby activating it. ADAM genes are found in animals, choanoflagellates, fungi and some groups of green algae. Most green algae and all land plants likely lost ADAM proteins.

A disintegrin and metalloproteinase with thrombospondin motifs 4 is an enzyme that in humans is encoded by the ADAMTS4 gene.

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

Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.

ADAMTS-like protein 4 is a protein that in humans is encoded by the ADAMTSL4 gene.

ADAMTS is a family of multidomain extracellular protease enzymes. 19 members of this family have been identified in humans, the first of which, ADAMTS1, was described in 1997. Known functions of the ADAMTS proteases include processing of procollagens and von Willebrand factor as well as cleavage of aggrecan, versican, brevican and neurocan, making them key remodeling enzymes of the extracellular matrix. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. Homologous subfamily of ADAMTSL (ADAMTS-like) proteins, which lack enzymatic activity, has also been described. Most cases of thrombotic thrombocytopenic purpura arise from autoantibody-mediated inhibition of ADAMTS13.

A disintegrin and metalloproteinase with thrombospondin motifs 8 is an enzyme that in humans is encoded by the ADAMTS8 gene.

A disintegrin and metalloproteinase with thrombospondin motifs 9 is an enzyme that in humans is encoded by the ADAMTS9 gene.

A disintegrin and metalloproteinase with thrombospondin motifs 10 is an enzyme that in humans is encoded by the ADAMTS10 gene.

ADAMTS-like protein 1 is a protein that in humans is encoded by the ADAMTSL1 gene.

Disintegrin and metalloproteinase domain-containing protein 28 is an enzyme that in humans is encoded by the ADAM28 gene.

Disintegrin and metalloproteinase domain-containing protein 11 is an enzyme that in humans is encoded by the ADAM11 gene.

A disintegrin and metalloproteinase with thrombospondin motifs 3 is an enzyme that in humans is encoded by the ADAMTS3 gene. The protein encoded by this gene is the major procollagen II N-propeptidase.

A disintegrin and metalloproteinase with thrombospondin motifs 12 is an enzyme that in humans is encoded by the ADAMTS12 gene.

Disintegrin and metalloproteinase domain-containing protein 18 is an enzyme that in humans is encoded by the ADAM18 gene.

Papilin is a protein that in humans is encoded by the PAPLN gene. Papilin is an extracellular matrix glycoprotein.

A disintegrin and metalloproteinase with thrombospondin motifs 7 (ADAMTS7) is an enzyme that in humans is encoded by the ADAMTS7 gene on chromosome 15. It is ubiquitously expressed in many tissues and cell types. This enzyme catalyzes the degradation of cartilage oligomeric matrix protein (COMP) degradation. ADAMTS7 has been associated with cancer and arthritis in multiple tissue types. The ADAMTS7 gene also contains one of 27 SNPs associated with increased risk of coronary artery disease.

ADAM metallopeptidase with thrombospondin type 1 motif 6 is a protein that in humans is encoded by the ADAMTS6 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000140470 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000058145 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Entrez Gene: ADAM metallopeptidase with thrombospondin type 1 motif, 17".
↑ Shah MH, Bhat V, Shetty JS, Kumar A (2014). "Whole exome sequencing identifies a novel splice-site mutation in ADAMTS17 in an Indian family with Weill-Marchesani syndrome". Molecular Vision. 20: 790–796. PMC 4057248 . PMID 24940034.

External links

Human ADAMTS17 genome location and ADAMTS17 gene details page in the UCSC Genome Browser .

Peters BJ, Rodin AS, Klungel OH, Stricker BH, de Boer A, Maitland-van der Zee AH (December 2010). "Variants of ADAMTS1 modify the effectiveness of statins in reducing the risk of myocardial infarction". Pharmacogenetics and Genomics. 20 (12): 766–774. doi:10.1097/FPC.0b013e328340aded. PMID 21037509. S2CID 23007611.
Sovio, U; Bennett, AJ; Millwood, IY; Molitor, J; O'Reilly, PF; Timpson, NJ; Kaakinen, M; Laitinen, J; Haukka, J; Pillas, D; Tzoulaki, I; Molitor, J; Hoggart, C; Coin, LJ; Whittaker, J; Pouta, A; Hartikainen, AL; Freimer, NB; Widen, E; Peltonen, L; Elliott, P; McCarthy, MI; Jarvelin, MR (March 2009). "Genetic determinants of height growth assessed longitudinally from infancy to adulthood in the northern Finland birth cohort 1966". PLOS Genetics. 5 (3): e1000409. doi:10.1371/journal.pgen.1000409. PMC 2646138 . PMID 19266077.
Ichikawa S, Koller DL, Padgett LR, Lai D, Hui SL, Peacock M, Foroud T, Econs MJ (August 2010). "Replication of previous genome-wide association studies of bone mineral density in premenopausal American women". Journal of Bone and Mineral Research. 25 (8): 1821–1829. doi:10.1002/jbmr.62. PMC 3153352 . PMID 20200978.
Warnatz HJ, Schmidt D, Manke T, Piccini I, Sultan M, Borodina T, Balzereit D, Wruck W, Soldatov A, Vingron M, Lehrach H, Yaspo ML (July 2011). "The BTB and CNC homology 1 (BACH1) target genes are involved in the oxidative stress response and in control of the cell cycle". The Journal of Biological Chemistry. 286 (26): 23521–23532. doi: 10.1074/jbc.M111.220178 . PMC 3123115 . PMID 21555518.
Zhao J, Li M, Bradfield JP, Zhang H, Mentch FD, Wang K, Sleiman PM, Kim CE, Glessner JT, Hou C, Keating BJ, Thomas KA, Garris ML, Deliard S, Frackelton EC, Otieno FG, Chiavacci RM, Berkowitz RI, Hakonarson H, Grant SF (June 2010). "The role of height-associated loci identified in genome wide association studies in the determination of pediatric stature". BMC Medical Genetics. 11: 96. doi:10.1186/1471-2350-11-96. PMC 2894790 . PMID 20546612.
Cal S, Obaya AJ, Llamazares M, Garabaya C, Quesada V, López-Otín C (January 2002). "Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains". Gene. 283 (1–2): 49–62. doi:10.1016/s0378-1119(01)00861-7. PMID 11867212.
Khan AO, Aldahmesh MA, Al-Ghadeer H, Mohamed JY, Alkuraya FS (December 2012). "Familial spherophakia with short stature caused by a novel homozygous ADAMTS17 mutation". Ophthalmic Genetics. 33 (4): 235–239. doi:10.3109/13816810.2012.666708. PMID 22486325. S2CID 37291964.
Morales J, Al-Sharif L, Khalil DS, Shinwari JM, Bavi P, Al-Mahrouqi RA, Al-Rajhi A, Alkuraya FS, Meyer BF, Al Tassan N (November 2009). "Homozygous mutations in ADAMTS10 and ADAMTS17 cause lenticular myopia, ectopia lentis, glaucoma, spherophakia, and short stature". American Journal of Human Genetics. 85 (5): 558–568. doi:10.1016/j.ajhg.2009.09.011. PMC 2775842 . PMID 19836009.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000140470 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000058145 - 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.

[entrez-5] "Entrez Gene: ADAM metallopeptidase with thrombospondin type 1 motif, 17".

[6] Shah MH, Bhat V, Shetty JS, Kumar A (2014). "Whole exome sequencing identifies a novel splice-site mutation in ADAMTS17 in an Indian family with Weill-Marchesani syndrome". Molecular Vision. 20: 790–796. PMC 4057248 . PMID 24940034.

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