ADAMTS4
entrez
9507
canonical
uniprot
O75173
canonical
ensembl
ENSG00000158859
resolver
ensp
ENSP00000356975
resolver
ensp
ENSP00000717041
resolver
genesymbol
ADAMTS4
resolver
genesymbol_syn
KIAA0688
resolver
hgnc
HGNC:220
resolver
uniprot
Q2HYD0
resolver
uniprot
Q5VTW2
resolver
uniprot
Q6P4Q8
resolver
uniprot
Q6UWA8
resolver
uniprot
Q9UN83
resolver
uniprot_entry
ATS4_HUMAN
resolver
uniprot_sec
Q2HYD0
resolver
uniprot_sec
Q5VTW2
resolver
uniprot_sec
Q6P4Q8
resolver
uniprot_sec
Q6UWA8
resolver
uniprot_sec
Q9UN83
resolver
amino_acid_sequence
MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK
uniprot
proteins
ec_number
3.4.24.82
uniprot
proteins
function
FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, at the '392-Glu-|-Ala-393' site and may be involved in its turnover (PubMed:10356395, PubMed:10827174). Also cleaves COMP (PubMed:39672391). May play an important role in the destruction of aggrecan in arthritic diseases. Could be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. {ECO:0000269|PubMed:10356395, ECO:0000269|PubMed:10827174, ECO:0000269|PubMed:39672391}.
uniprot
proteins
mass_dalton
90197
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by a furin endopeptidase.; 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
10356395
uniprot
proteins
pubmed
10827174
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16723216
uniprot
proteins
pubmed
18042673
uniprot
proteins
pubmed
18718938
uniprot
proteins
pubmed
23897278
uniprot
proteins
pubmed
39672391
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
837
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
uniprot
proteins