ADAMTS5

ADAM metallopeptidase with thrombospondin type 1 motif, 5
250px PDB rendering based on 2rjq.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2RJQ, 3B8Z, 3HY7, 3HY9, 3HYG, 3LJT
Identifiers
Symbols	ADAMTS5 ; ADAM-TS 11; ADAM-TS 5; ADAM-TS5; ADAMTS-11; ADAMTS-5; ADAMTS11; ADMP-2
External IDs	OMIM: 605007 MGI: 1346321 HomoloGene: 5109 IUPHAR: 1678 ChEMBL: 2285 GeneCards: ADAMTS5 Gene
EC number	3.4.24.-
Gene ontology Molecular function • metalloendopeptidase activity • integrin binding • protein binding • metallopeptidase activity • zinc ion binding Cellular component • extracellular region • proteinaceous extracellular matrix • endoplasmic reticulum lumen Biological process • protein O-linked glycosylation • proteolysis • extracellular matrix disassembly • extracellular matrix organization • protein O-linked fucosylation • defense response to bacterium • post-translational protein modification • cellular protein metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11096	23794
Ensembl	ENSG00000154736	ENSMUSG00000022894
UniProt	Q9UNA0	Q9R001
RefSeq (mRNA)	NM_007038	NM_011782
RefSeq (protein)	NP_008969	NP_035912
Location (UCSC)	Chr 21: 26.92 – 26.97 Mb	Chr 16: 85.86 – 85.9 Mb
PubMed search	[1]	[2]

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

Function

ADAMTS5 is 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 enzyme encoded by this gene contains two C-terminal TS motifs and functions as aggrecanase to cleave aggrecan, a major proteoglycan of cartilage.

Clinical significance

Genetically modified mice in which the catalytic domain of ADAMTS5 was deleted are resistant to cartilage destruction in an experimental model of osteoarthritis. ADAMTS5 is the major aggrecanase in mouse cartilage in a mouse model of inflammatory arthritis.

Further reading

• 
• 

External links

• The MEROPS online database for peptidases and their inhibitors: M12.225
• Rat Genome Database