ADAMTS17
entrez
170691
canonical
uniprot
Q8TE56
canonical
ensembl
ENSG00000140470
resolver
ensp
ENSP00000268070
resolver
ensp
ENSP00000456161
resolver
ensp
ENSP00000631157
resolver
ensp
ENSP00000778629
resolver
enst
ENST00000568565
resolver
genesymbol
ADAMTS17
resolver
hgnc
HGNC:17109
resolver
uniprot
H3BRA9
resolver
uniprot
Q2I7G4
resolver
uniprot
Q6ZN75
resolver
uniprot_entry
ATS17_HUMAN
resolver
uniprot_entry
H3BRA9_HUMAN
resolver
uniprot_sec
Q2I7G4
resolver
uniprot_sec
Q6ZN75
resolver
amino_acid_sequence
MCDGALLPPLVLPVLLLLVWGLDPGTAVGDAAADVEVVLPWRVRPDDVHLPPLPAAPGPRRRRRPRTPPAAPRARPGERALLLHLPAFGRDLYLQLRRDLRFLSRGFEVEEAGAARRRGRPAELCFYSGRVLGHPGSLVSLSACGAAGGLVGLIQLGQEQVLIQPLNNSQGPFSGREHLIRRKWSLTPSPSAEAQRPEQLCKVLTEKKKPTWGRPSRDWRERRNAIRLTSEHTVETLVVADADMVQYHGAEAAQRFILTVMNMVYNMFQHQSLGIKINIQVTKLVLLRQRPAKLSIGHHGERSLESFCHWQNEEYGGARYLGNNQVPGGKDDPPLVDAAVFVTRTDFCVHKDEPCDTVGIAYLGGVCSAKRKCVLAEDNGLNLAFTIAHELGHNLGMNHDDDHSSCAGRSHIMSGEWVKGRNPSDLSWSSCSRDDLENFLKSKVSTCLLVTDPRSQHTVRLPHKLPGMHYSANEQCQILFGMNATFCRNMEHLMCAGLWCLVEGDTSCKTKLDPPLDGTECGADKWCRAGECVSKTPIPEHVDGDWSPWGAWSMCSRTCGTGARFRQRKCDNPPPGPGGTHCPGASVEHAVCENLPCPKGLPSFRDQQCQAHDRLSPKKKGLLTAVVVDDKPCELYCSPLGKESPLLVADRVLDGTPCGPYETDLCVHGKCQKIGCDGIIGSAAKEDRCGVCSGDGKTCHLVKGDFSHARGTALKDSGKGSINSDWKIELPGEFQIAGTTVRYVRRGLWEKISAKGPTKLPLHLMVLLFHDQDYGIHYEYTVPVNRTAENQSEPEKPQDSLFIWTHSGWEGCSVQCGGGERRTIVSCTRIVNKTTTLVNDSDCPQASRPEPQVRRCNLHPCQSRWVAGPWSPCSATCEKGFQHREVTCVYQLQNGTHVATRPLYCPGPRPAAVQSCEGQDCLSIWEASEWSQCSASCGKGVWKRTVACTNSQGKCDASTRPRAEEACEDYSGCYEWKTGDWSTCSSTCGKGLQSRVVQCMHKVTGRHGSECPALSKPAPYRQCYQEVCNDRINANTITSPRLAALTYKCTRDQWTVYCRVIREKNLCQDMRWYQRCCQTCRDFYANKMRQPPPNS
uniprot
proteins
disease_involvement
DISEASE: Weill-Marchesani syndrome 4 (WMS4) [MIM:613195]: An autosomal recessive syndrome characterized by lenticular myopia, ectopia lentis, glaucoma, spherophakia and short stature. Brachydactyly and decreased joint flexibility are present in some patients. {ECO:0000269|PubMed:19836009, ECO:0000269|PubMed:22486325, ECO:0000269|PubMed:24940034}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:0000250|UniProtKB:D3YX90}.
uniprot
proteins
mass_dalton
121127
uniprot
proteins
mutagenesis
MUTAGEN 390; /note="E->A: Loss of autocatalysis."; /evidence="ECO:0000269|PubMed:28176809
uniprot
proteins
post_translational_modification
PTM: The precursor is autoproteolytically processed upon secretion in trans that is independent of furin processing. {ECO:0000269|PubMed:28176809}.; 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:0000269|PubMed:28176809}.
uniprot
proteins
pubmed
11867212
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
19836009
uniprot
proteins
pubmed
22486325
uniprot
proteins
pubmed
24940034
uniprot
proteins
pubmed
28176809
uniprot
proteins
sequence_length
1095
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:28176809}.
uniprot
proteins