D3YX90
uniprot
D3YX90
canonical
amino_acid_sequence
MCDGTLLPPLVLSLLLLVWGLDPGTAVGDAAADVEVVLPRRLRPEDVHLQLLPGAAGLRRWRRPRASPGGHRAGQGERALLLHLPAFGRDLYLQLHRDLRFLSPGFEVEEAGVSGRSGHPAELCFYSGRVLGHPGSLVSLSACGAAGGLVGLIQLEQEQVFIQPLNSSGGPFIGREHLIRRKWASTPSPATEVEGPRQRCKVVTEKKPRKDHLSRDWRERRNAIRLTNEHTVETLVVADADMVQYHGAEAAQRFILTVMNMVYNMFQHRSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQNEEYGGARYLGNNQVPGGKDDTPPVDAAVFVTRTDFCVHKDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHELGHNLGMNHDDDHSSCAGRSHIMSGEWVKGRNPSDLSWSSCSRDDLENFLKSKVSTCLLITDPRSQHALRLPHKLPGMHYSANEQCQILFGTNATFCKNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECVSKTPIPEHVDGDWSLWSAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCQGASVEHAACEKLPCPKGVPSFRDQQCQAHDRLSSKKRGLLTAVVVDDKPCELYCSPLGKESPLLVADRVLDGTPCGPYEADLCVYGRCQKIGCDGIIGSAAKEDRCGVCSGDGKTCRVVKGDFSHSRGTALKDSSKRSINSDWKIELPGEFQIAGTTVRYVRRGLWEKFSAKGPTTVPLHLMVLLFHDQNYGIHYEYTIPVNQSSENQSEPAKPQDALFLWTHSGWEGCSVQCGGGERRTIVSCTRIVNKTTTLVNDSDCPQASRPEPQVRRCNSHPCQSRWVTGQWSPCSATCEKGVQHREVTCVYQLQNGTHVTTRPIYCSEPRPTPVQSCEGQDCLSIWEASEWSECSANCGKGIQKRTVTCTNSQGKCDASTRPKAEEECEDYSGCYEWKTGDWSKCSSTCGKGLQSRVVQCMHKLTGRHGSECPTLSKPAAYRQCHQEVCNEKINVNTITSPRLAALTYKCTRDQWTVYCRVIREKNLCQDMRWYQRCCQTCRDFYADKMRQPPSPPSS
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Extracellular metalloprotease that regulates skeletal development by modulating BMP-Smad signaling and extracellular matrix microfibril organization, which controls chondrocyte differentiation and bone growth. {ECO:0000269|PubMed:31201465}.
uniprot
proteins
mass_dalton
121198
uniprot
proteins
post_translational_modification
PTM: The precursor is autoproteolytically processed upon secretion in trans that is independent of furin processing. {ECO:0000250|UniProtKB:Q8TE56}.; 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. {ECO:0000250|UniProtKB:Q8TE56}.
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21750661
uniprot
proteins
pubmed
31201465
uniprot
proteins
sequence_length
1095
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q8TE56}.
uniprot
proteins