Adamts1
entrez
11504
canonical
uniprot
P97857
canonical
ensembl
ENSMUSG00000022893
resolver
ensp
ENSMUSP00000023610
resolver
enst
ENSMUST00000023610
resolver
genesymbol
Adamts1
resolver
uniprot
E9QMN9
resolver
uniprot
O54768
resolver
uniprot
Q3TQF7
resolver
uniprot
Q3TTE6
resolver
uniprot_entry
ATS1_MOUSE
resolver
uniprot_entry
Q3TQF7_MOUSE
resolver
uniprot_entry
Q3TTE6_MOUSE
resolver
uniprot_sec
E9QMN9
resolver
uniprot_sec
O54768
resolver
amino_acid_sequence
MQPKVPLGSRKQKPCSDMGDVQRAARSRGSLSAHMLLLLLASITMLLCARGAHGRPTEEDEELVLPSLERAPGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSPGSEAQHLDPTGDLAHCFYSGTVNGDPGSAAALSLCEGVRGAFYLQGEEFFIQPAPGVATERLAPAVPEEESSARPQFHILRRRRRGSGGAKCGVMDDETLPTSDSRPESQNTRNQWPVRDPTPQDAGKPSGPGSIRKKRFVSSPRYVETMLVADQSMADFHGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQKQHNSPSDRDPEHYDTAILFTRQDLCGSHTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKHCASLNGVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECLMDKPQNPIKLPSDLPGTLYDANRQCQFTFGEESKHCPDAASTCTTLWCTGTSGGLLVCQTKHFPWADGTSCGEGKWCVSGKCVNKTDMKHFATPVHGSWGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCPDNNGKTFREEQCEAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCKLTCEAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKMSGIVTSTRPGYHDIVTIPAGATNIEVKHRNQRGSRNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGSSAALERIRSFSPLKEPLTIQVLMVGHALRPKIKFTYFMKKKTESFNAIPTFSEWVIEEWGECSKTCGSGWQRRVVQCRDINGHPASECAKEVKPASTRPCADLPCPHWQVGDWSPCSKTCGKGYKKRTLKCVSHDGGVLSNESCDPLKKPKHYIDFCTLTQCS
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Metalloprotease which cleaves aggrecan, a cartilage proteoglycan, at the '1691-Glu-|-Leu-1692' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover (PubMed:10930576, PubMed:9441751). Also cleaves COMP (By similarity). Has angiogenic inhibitor activity (By similarity). May play a critical role in follicular rupture (PubMed:10781075). {ECO:0000250|UniProtKB:Q9UHI8, ECO:0000269|PubMed:10781075, ECO:0000269|PubMed:10930576, ECO:0000269|PubMed:9441751}.
uniprot
proteins
mass_dalton
105801
uniprot
proteins
mutagenesis
MUTAGEN 403; /note="E->Q: Loss of activity."; /evidence="ECO:0000269|PubMed:10373500
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
10373500
uniprot
proteins
pubmed
10781075
uniprot
proteins
pubmed
10930576
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
23233679
uniprot
proteins
pubmed
8995297
uniprot
proteins
pubmed
9441751
uniprot
proteins
sequence_length
968
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix.
uniprot
proteins