ADAMTS2

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ADAMTS2
Identifiers
AliasesADAMTS2, ADAM-TS2, ADAMTS-2, ADAMTS-3, NPI, PC I-NP, PCI-NP, PCINP, PCPNI, PNPI, ADAM metallopeptidase with thrombospondin type 1 motif 2, EDSDERMS
External IDsOMIM: 604539 MGI: 1347356 HomoloGene: 8597 GeneCards: ADAMTS2
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for ADAMTS2
Genomic location for ADAMTS2
Band5q35.3Start179,110,853 bp[1]
End179,345,461 bp[1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_021599
NM_014244

NM_001277305
NM_175643

RefSeq (protein)

NP_055059
NP_067610

NP_783574

Location (UCSC)Chr 5: 179.11 – 179.35 MbChr 11: 50.6 – 50.81 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS2) also known as procollagen I N-proteinase (PC I-NP) is an enzyme[5] that in humans is encoded by the ADAMTS2 gene.[6][7]

Gene[edit]

The ADAMTS2 gene is located on the long (q) arm of chromosome 5 at the end (terminus) of the arm, from base pair 178,473,473 to base pair 178,704,934.

Function[edit]

ADAMTS2 is responsible for processing several types of procollagen proteins. Procollagens are the precursors of collagens, the proteins that add strength and support to many body tissues. Specifically, this enzyme clips a short chain of amino acids off one end of the procollagen. This clipping step is necessary for collagen molecules to function normally and assemble into fibrils outside cells.

Clinical significance[edit]

Ehlers-Danlos syndrome, dermatosparaxis type is caused by mutations in the ADAMTS2 gene.[7] Several mutations in the ADAMTS2 gene have been identified in people with this syndrome. These mutations greatly reduce the production of the enzyme made by the ADAMTS2 gene. Procollagen cannot be processed correctly without this enzyme. As a result, collagen fibrils are not assembled properly; they appear ribbon-like and disorganized under the microscope. Cross-links, or chemical interactions, between collagen fibrils are also affected. These defects weaken connective tissue (the tissue that binds and supports the body's muscles, ligaments, organs, and skin), which causes the signs and symptoms of the disorder.

See also[edit]

References[edit]

  1. ^ a b c ENSG00000283802 GRCh38: Ensembl release 89: ENSG00000087116, ENSG00000283802 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036545 - 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. ^ Tang BL, Hong W (February 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. ^ "Entrez Gene: ADAM metallopeptidase with thrombospondin type 1 motif".
  7. ^ a b Colige A, Nuytinck L, Hausser I, van Essen AJ, Thiry M, Herens C, Adès LC, Malfait F, Paepe AD, Franck P, Wolff G, Oosterwijk JC, Smitt JH, Lapière CM, Nusgens BV (October 2004). "Novel types of mutation responsible for the dermatosparactic type of Ehlers-Danlos syndrome (Type VIIC) and common polymorphisms in the ADAMTS2 gene". J. Invest. Dermatol. 123 (4): 656–63. doi:10.1111/j.0022-202X.2004.23406.x. PMID 15373769.

Further reading[edit]

External links[edit]