ADAMTS5
entrez
11096
canonical
uniprot
Q9UNA0
canonical
ensembl
ENSG00000154736
resolver
ensp
ENSP00000284987
resolver
ensp
ENSP00000640405
resolver
enst
ENST00000284987
resolver
genesymbol
ADAMTS5
resolver
genesymbol_syn
ADAMTS11
resolver
genesymbol_syn
ADMP2
resolver
hgnc
HGNC:221
resolver
uniprot
Q52LV4
resolver
uniprot
Q9UKP2
resolver
uniprot_entry
ATS5_HUMAN
resolver
uniprot_sec
Q52LV4
resolver
uniprot_sec
Q9UKP2
resolver
amino_acid_sequence
MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGHPHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGTSAPWRHRSHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGRVYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLDQSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYDAAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQILGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVLPADVCKLTCRAKGTGYYVVFSPKVTDGTECRLYSNSVCVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPTKPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTVQCQDGNRKLAKGCPLSQRPSAFKQCLLKKC
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN (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 VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration (By similarity). Participates in development of brown adipose tissue and browning of white adipose tissue (By similarity). 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}.
uniprot
proteins
mass_dalton
101718
uniprot
proteins
mutagenesis
MUTAGEN 411; /note="E->A: Complete loss of catalytic activity."; /evidence="ECO:0000269|PubMed:18992360
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by furin and PCSK7 outside of the cell. {ECO:0000269|PubMed:18992360}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Can also be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
10438522
uniprot
proteins
pubmed
10464288
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16133547
uniprot
proteins
pubmed
18042673
uniprot
proteins
pubmed
18992360
uniprot
proteins
pubmed
19671700
uniprot
proteins
sequence_length
930
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18992360}.
uniprot
proteins