Adamts15
entrez
235130
canonical
uniprot
P59384
canonical
ensembl
ENSMUSG00000033453
resolver
ensp
ENSMUSP00000067022
resolver
enst
ENSMUST00000065112
resolver
genesymbol
Adamts15
resolver
uniprot
Q504Z2
resolver
uniprot
Q91Z56
resolver
uniprot_entry
ATS15_MOUSE
resolver
uniprot_sec
Q504Z2
resolver
uniprot_sec
Q91Z56
resolver
amino_acid_sequence
MLLLGISILALAWRPAGSSEPEWEVVVPIRRDPDINGRHYYRRGTEDSGDQGLIFQITAFQQDFYLHLTPDAQFLAPAFATEYLGVPLQRLTGSSLDLRRCFYSGYVNAEPDSFAAVSLCGGLRGAFGYRGAEYVISPLPNTSAPEAQRHSQGAHLLQRRGAPVGPSGDPTSRCGVASGWNPAILRALDPYKPRRTGAGESHNRRRSGRAKRFVSIPRYVETLVVADESMVKFHGADLEHYLLTLLATAARLYRHPSILNPINIVVVKVLLLGDRDTGPKVTGNAALTLRNFCAWQKKLNKVSDKHPEYWDTAILFTRQDLCGATTCDTLGMADVGTMCDPKRSCSVIEDDGLPSAFTTAHELGHVFNMPHDNVKVCEEVFGKLRANHMMSPTLIQIDRANPWSACSAAIITDFLDSGHGDCLLDQPSKPITLPEDLPGTSYSLSQQCELAFGVGSKPCPYMQYCTKLWCTGKAKGQMVCQTRHFPWADGTSCGEGKFCLKGACVERHNPNKYRVDGSWAKWEPYGSCSRTCGGGVQLARRQCSNPTPANGGKYCEGVRVKYRSCNLEPCPSSASGKSFREEQCEAFNGYNHSTNRLTLAVAWVPKYSGVSPRDKCKLICRANGTGYFYVLAPKVVDGTLCTPDSTSVCVQGKCIKAGCDGNLGSKKKFDKCGVCGGDNKSCKRVTGLFTKPMHGYNFVVAIPAGASSIDIRQRGYKGLIGDDNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSVLRYSGTGTAVESLQASRPILEPLTVEVLSVGKMTPPRVRYSFYLPKEPREDKSTRPKDPRGSPVLRNSVLSLSNQVEQPDNRPPARWVAGSWGPCSVSCGSGLQKRAVDCRDSPGQQGASACDVDHRPLEKRACGEPCPTWELGNWSPCSKSCGRGFKRRPLKCVGHGGRLLARDQCDLRRKPQELDFCVLRPC
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Metalloprotease which has proteolytic activity against the proteoglycan VCAN, cleaving it at the 'Glu-1401-|-1402-Ala' site (PubMed:24220035). Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration (PubMed:23233679). {ECO:0000269|PubMed:23233679, ECO:0000269|PubMed:24220035}.
uniprot
proteins
mass_dalton
103938
uniprot
proteins
mutagenesis
MUTAGEN 141; /note="N->Q: Reduced glycosylation."; /evidence="ECO:0000269|PubMed:24220035"; MUTAGEN 212; /note="R->A: Reduced propeptide cleavage."; /evidence="ECO:0000269|PubMed:24220035
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000269|PubMed:24220035}.; PTM: Glycosylated (PubMed:24220035). 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 (By similarity). Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL (By similarity). Fucosylation mediates the efficient secretion of ADAMTS family members (By similarity). Can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs (By similarity). Also N-glycosylated (PubMed:24220035). These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250|UniProtKB:Q76LX8, ECO:0000269|PubMed:24220035}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
23233679
uniprot
proteins
pubmed
24220035
uniprot
proteins
pubmed
35962790
uniprot
proteins
pubmed
36853234
uniprot
proteins
sequence_length
950
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:24220035}. Cell surface {ECO:0000269|PubMed:24220035}.
uniprot
proteins