Adamts20
entrez
223838
canonical
uniprot
P59511
canonical
ensembl
ENSMUSG00000022449
resolver
ensp
ENSMUSP00000036330
resolver
ensp
ENSMUSP00000121696
resolver
ensp
ENSMUSP00000266644
resolver
genesymbol
Adamts20
resolver
uniprot
E9QLA1
resolver
uniprot
Q3UQW9
resolver
uniprot_entry
ATS20_MOUSE
resolver
uniprot_entry
Q3UQW9_MOUSE
resolver
uniprot_sec
E9QLA1
resolver
amino_acid_sequence
MRVAKWLTGLLCPISLLLTGSWEVRFHPRQEALVKTLASYEVVTPTRVNEFGDVFPQNRHFSRKKRSSGVPEPPPFRTHYRISAYGQLFQLNLSADAAFLAAGYTEVHLGTPVPGPGGRSTESPDLRHCFYRGQVNAREDHTAVFSLCGGLMGTFKANDGEYFLEPVLRADGSAHDDDHNKPHLIYRQELKRNSFARSHKPCEVSENQMEKTALPSQSSRNTTGDVDIEEEAVFRLEGERSQLHSRNKRFLSYPRYVEVMVTADAKMVHHHGQNLQHYVLTLMSIVAAIYKDSSIGNLINIVIVKLVVIHSEQEGPVISFNAATTLRNFCLWQQSQNVPDDAHPSHHDTAVLITREDICGAKEKCDTLGLAELGTLCDPSRSCSISEENGLSAAFTIAHELGHVFNVPHDDSFKCKEAGIKHQYHVMAPTLNYHTSPWTWSACSQKHITEFLDTGHGECLLDKPNGRTYDLSPQLPGSVYDGNRQCELMFGPGSQVCPYLKHCRRLWCTSAEGVHKGCRTQHMPLADGTSCGPGMHCHRGLCVTRDMETRPVDGEWGPWGPYSSCSRTCGGGIKSTARLCDRPEPRNGGRYCVGRRMKFRSCNTDSCPKGKRDFREKQCSDFDGKHFDINGLPPNVRWLPKYSGIAVKDRCKLYCRVAGTTSFYQLKDRVADGTPCGTETNDICVQGLCRQAGCDHVLNSKAKRDKCGVCGGDNSSCQTLAGVFNSAHYGYNVVVKIPAGATNIEILQHSYSGRPEDDNYLALSDTQGNFLLNGNFVVSMAKKEINIQGAVFEYSGSNNSIERINSTDRLEAELVLQVLCVGNLYNPDVRYSFNIPIEERSNLFSWDPYGPWQDCTKMCQGLHRRKIACVRKSDHAVVSDHNCGHLPMPLFVTEKCNMDCELRWHIIGKSDCSSQCGQGYRTLDVHCMKYSVHKGQAVPVGDQYCGDQLKPPSREPCHGSCVLTRWHYSEWSQCSRSCGGGDKTRESYCVNGFGHRLAESECRELPRVVLENCNEFPCPSWATSEWSECPVTCGKGMKQRQVWCQLSEDPMRDGFCNASTKPESLRPCELRACASWHVGPWGSCTATCGHGYQMRAVKCISEIFGTMLDDRECPQASRPSDRQDCILAPCLAIPEVGATSLPAIPLGRAAQWRHGSWTPCSVSCGRGSQARYVSCRDAHDEVADESNCAHLPRPAAVSLCFSPCGEWQAGDWSPCSASCGHGKTTRRVLCVNYHQLVDESYCDPEGRPVTEQECSLAACPPLYSRAPSSSEQPSHVPSRNVPLTHKPGENQDQGAQLSIRGNQWRTGPWGACSRSCAGGLQHRAVVCQDEDGRSATSCDGSSKPPESRHCGSGPCPHWNYGDWGECTQTCGGGVKSRFVICQFPNGQMTQEHSCELPKPPSMMQCHLHACPEDVSWYRGPWKSCSASCGKGVKYREVLCIDQFQRKLEEKYCSHLHKPRTHKACRSGRCPSWKANKWKECSVTCGSGVQQREVYCRLRGTGRVSEDMCDPSTRPQGQRQCWRQDCMRYQWTTGDWLDCSTSCKKKETYRLVKCVNEQNVQANESLCDPLTKPLSIKKCRNPHCKYSVVTGDSSQCAGNCGFTSPQKITYCTKIQSSKKHTFHQLRPVVYGECPVIPSPQAYKCDLRSCLHVATWKVGKWSKCSVTCGIGIMERRVACRTENGWPSDLCLKRLKPDAQKKCYANDCKLLTTCKELQVTNNVTKDGDYDLNVRGRILKIHCSGMQLENPREYLPLVKSEDNFSEIYGLRLQNPYECPFNGSRRPDCACENDYLPAGYTVFSKVRVDLESMQIKTADLLFSQTLSGKAVPFATAGDCYSAARCPQGQFSINLAGTGMKISNTAKWLAQGRYASVIIHRSQDGTKVYGRCGGFCGKCIPHMATGLSIQVL
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Cleaves peptide bond of the large aggregating proteoglycan, versican (at the '1428-Glu-|-Ala-1429' site) (PubMed:12562771, PubMed:18454205). In addition, catalyzes the shedding of the endopeptidase MMP14 (at the '314-Tyr-|-Gly-315' site), releasing the catalytic domain from the cell surface thereby preventing the downstream pro-MMP2 activation (PubMed:37169079). Is involved in extracellular matrix proteolysis and ciliogenesis (PubMed:18454205, PubMed:30814516). May have a protease-independent function in promoting the transport from the endoplasmic reticulum to the Golgi apparatus of a variety of secretory cargos (By similarity). {ECO:0000250|UniProtKB:Q9P2N4, ECO:0000269|PubMed:12562771, ECO:0000269|PubMed:18454205, ECO:0000269|PubMed:30814516, ECO:0000269|PubMed:37169079}.
uniprot
proteins
mass_dalton
212068
uniprot
proteins
mutagenesis
MUTAGEN 400; /note="E->A: Loss of metalloendopeptidase activity toward MMP14."; /evidence="ECO:0000269|PubMed:37169079"; MUTAGEN 761; /note="L->F: In belted (bt); causes white spotting of the dorsal and ventral torso. Does not affect melanoblasts distribution at E12.5 embryos. Specifically reduces melanoblasts distribution in the trunk of E13.5 embryos. Reduces versican processing in skin of the embryonic trunk. Severe developmental defects. Impairs ciliogenesis. Affects proteoglycan-hyaluronan distribution in the neural tube."; /evidence="ECO:0000269|PubMed:18454205, ECO:0000269|PubMed:30814516
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250|UniProtKB:Q9P2N4}.; PTM: Glycosylated (By similarity). 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|UniProtKB:Q76LX8, ECO:0000250|UniProtKB:Q9P2N4}.
uniprot
proteins
pubmed
12562771
uniprot
proteins
pubmed
12925592
uniprot
proteins
pubmed
18454205
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
30814516
uniprot
proteins
pubmed
37169079
uniprot
proteins
sequence_length
1906
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9P2N4}. Cell projection, cilium {ECO:0000269|PubMed:30814516}. Note=Localized adjacent to the basal body. {ECO:0000269|PubMed:30814516}.
uniprot
proteins