Adamts18
entrez
208936
canonical
uniprot
Q4VC17
canonical
ensembl
ENSMUSG00000053399
resolver
ensp
ENSMUSP00000090801
resolver
enst
ENSMUST00000093113
resolver
genesymbol
Adamts18
resolver
uniprot
E9QNK0
resolver
uniprot
Q8BZD1
resolver
uniprot_entry
ATS18_MOUSE
resolver
uniprot_sec
E9QNK0
resolver
uniprot_sec
Q8BZD1
resolver
amino_acid_sequence
MECALLCLCALRAAGPGPPWGPAGLGRLAKALQLCCFCCASVAVALASDSGSSGGSGLNDDYVFVVPVEVDSGGSYISHDILHHRKRRSAHGASNSLHYRVSAFGQDLHLELKPSAILSSHFRVQVLGKDGASETREPEVPQCLYQGFIRNDSSSSVAVSTCAGLSGLIRTRDNEFLISPLPQLLAQEHNYSSPAGHHPHVLYKRTAEKRVRWYQDYPGSQRTYPGHSPSHTPPASQSQEPEYSHRRWQKRHFCGRRKKYAPKPPAEDAYLRFDEYGGTGRPRRSAGKSQNGLNVETLVVADAKMVEKHGKDDVTTYILTVMNMVSSLFKDGTIGSDINIVVVSLILLEEEPEGLLINHHADQSLNSFCQWQSALVGKNGKRHDHAILLTGFDICSWKNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMVHDGEGNPCRKAEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCLVDEPKQTGQYKYPDKLPGQIYDADMQCKWQFGAKAKLCSLGVMKDICKSLWCHRVGHRCETKFMPAAEGTACGLSMWCRQGQCVKLGELGPRPIHGQWSAWSKWSECSRTCGGGVKFQERHCSNPKPQYGGKYCPGSSRIYKLCNINPCPENSLDFRAQQCAEYNNKPFRGWLYRWKPYTKVEEEDRCKLYCKAENFEFFFAMSGKVKDGTPCSPHRNDVCIDGICELVGCDHELGSKAVSDACGVCKGDNSTCKFYKGLYLSQHKANEYYPVVTIPAGARSIEIQELQLSSSYLAVRSLSQKYYLTGGWSIDWPGDFTFAGTTFEYQRSFNRPERLYAPGPTNETLVFEILTQGKNPGIAWKYALPKVMNVTQPATKRYHHTWRTVQSDCSVTCGGGYISIKAICLRDQHTQVNSSFCSVRTKPATEPKICNAFSCPAYWLPGEWSACSKSCAGGQQSRKIRCVQKKPFQKEEAVLHSLCPVSTPTQVQVCNSHACPPEWSPSPWSQCSKTCGRGVRRREVLCKSPAAETLPESLCSSSPRPEAQEGCVLGRCPKNNRLQWIASAWSECSATCGLGVRKRELKCVEKTLQGKLITFPERRCRNIKKPSLELEEACNQRTCPVYSMAVASWYSSPWQQCTVTCGGGVQTRSVHCMQQGRPSSSCLLHQKPPVLRACNTNFCPAPEKKDDPSCVDFFSWCHLVPQHGVCNHKFYGKQCCRSCTRKS
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
mass_dalton
135244
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; 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
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
sequence_length
1219
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
uniprot
proteins