UniProt Summary: Metalloproteinase that plays an important role in connective tissue organization, development, inflammation, arthritis, and cell migration. ADAMTS5 is an extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including aggrecan, versican, brevican and neurocan (PubMed:16133547, PubMed:18992360). Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its versican remodeling properties. Participates in development of brown adipose tissue and browning of white adipose tissue. Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection. {ECO:0000250|UniProtKB:Q9R001, ECO:0000269|PubMed:16133547, ECO:0000269|PubMed:18992360}.
Pfam DomainsGO Terms
Pfam Domains
TSP 1
Reprolysin
ADAM spacer1
Pep M12B propep
GO Terms
tooth eruption
extracellular matrix binding
negative regulation of cold-induced thermogenesis
metallopeptidase activity
extracellular matrix disassembly
metalloendopeptidase activity
odontogenesis
integrin binding
regulation of cold-induced thermogenesis
heparin binding
extracellular matrix
endoplasmic reticulum lumen
defense response to bacterium
extracellular matrix organization
collagen-containing extracellular matrix
extracellular structure organization
cellular component disassembly
response to bacterium
zinc ion binding
defense response to other organism
animal organ morphogenesis
negative regulation of multicellular organismal process
proteolysis
response to other organism
response to external biotic stimulus
response to biotic stimulus
defense response
extracellular space
extracellular region
CRISPR Data
Compound HitMost Correlated Genes in ChemogenomicsTissues where Essential in the Avana Dataset (DepMap 20Q1)