Adamts13
entrez
279028
canonical
uniprot
Q769J6
canonical
ensembl
ENSMUSG00000014852
resolver
ensp
ENSMUSP00000014996
resolver
ensp
ENSMUSP00000099955
resolver
enst
ENSMUST00000014996
resolver
enst
ENSMUST00000102891
resolver
genesymbol
Adamts13
resolver
genesymbol_syn
Gm710
resolver
uniprot
A2ALB3
resolver
uniprot
A2ALB4
resolver
uniprot
A7LM19
resolver
uniprot
Q76LW1
resolver
uniprot_entry
A2ALB3_MOUSE
resolver
uniprot_entry
A7LM19_MOUSE
resolver
uniprot_entry
ATS13_MOUSE
resolver
uniprot_sec
A2ALB4
resolver
uniprot_sec
Q76LW1
resolver
activity_regulation
ACTIVITY REGULATION: Zinc and calcium ions cooperatively modulate enzyme activity. The cleavage of the pro-domain is not required for protease activity. Dependence on calcium for proteolytic activity is mediated by the high affinity site (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MSQLCLWLTCQPCYAVSVRGILTGAIFILGCWGLSDFQKSLLQDLEPKDVSSYFGHHAAPFTGHPPSHLQRLRRRRTLEDILHLELLVAVGPDVSRAHQEDTERYVLTNLNIGSELLRNPSLGVQFQVHLVKLITLSDSESTPNITANITSSLMSVCEWSQTINPHDDRDPSHADLILYITRFDLELPDGNQQVRGVTQLGGACSLSWSCLITEDTGFDLGVTIAHEIGHSFGLDHDGAPGSGSTCKASGHVMAADGATPTGGTLEWSACSQRQLQHLLSTGQMHCFQDPPGLQSGLTRHQLMAQPGLYYSADDQCRVAFGSGAVACTFSREGLDVCQALSCHTDPLDQSSCSRLLVPLLDGTECGVEKWCSKARCRSLAELAPVAAVHGHWSSWGPHSPCSRSCGGGVITRRRWCNNPRPAFGGRACVGEDLQAKMCNTQACEKTQLEFMSEQCAQTDRQPLQLSQGTASFYHWDAAVQYSQGDTLCRHMCWAVGESFIVSRGDRFLDGTRCVPSGPQDDGTLSLCLLGSCRTFGCDGRMDSQKVWDACQVCGGDNSTCSSRNGSFTAGRAREYVTFLIVTPNMTNAHIVNRRPLFTHLAVRIQGHYIVAGKTSISPNTTYPSLLEDYRVEYRVTLTEDQLPHLEEIHIRGPVRDDIEIQVYRRYGGEYGDLTHPDITFSYFQLKQQAAWVWTAKRGPCSVSCGAGLRWVTYSCQDQAQDKWVKNAQCQGSPQPPAWQEPCVSAPCSPYWVAGDFSPCSVSCGGGLRERSLRCVETQDGFLKTLPPARCRAVAQQPAAEVENCNSQPCPTRWEVSDPGPCMSSACEAGLDSRNVTCVSRAGDPEKPETAGPCRTDEMSAMLEPCSRSLCSPGLGQVDNTMSLGEEAPSPVGSDKPGAQAEHVWTPLVGLCSISCGRGLKELYFLCMDSVLKMPVQEELCGLASKPPSRWEVCRARPCPARWETQVLAPCPVTCGGGRVPLSVRCVQLDRGHPISVPHSKCSPVPKPGSFEDCSPEPCPARWKVLSLGPCSASCGLGTATQMVACMQLDQGHDNEVNETFCKALVRPQASVPCLIADCAFRWHISAWTECSVSCGDGIQRRHDTCLGPQAQVPVPANFCQHLPKPMTVRGCWAGPCAGQETSSSLPHKEATLPSQTQAAATVASLQWSQPRARTPTLFSASQSLGLQENLEEHGACGRQYLEPTGTIHMRDQGRLDCVVAIGRPLGEVVTLQILESSLKCSAGEQLLLWGRFTWRKTCRKMPGMTFSTKTNTVVVKQHRVLPGGGVLLRYWSQPAPGTFYKECDRQLFGPRGEIVSPSLSPDGRKAGTCRVFISVAPQARIAIRALASDMGTASEGTNANYVSIRDIHSLRTTTFWGQQVLYWESEGSEAELEFSPGFLEAHASLQGEYWTISPRTSEQDDSLALS
uniprot
proteins
ec_number
3.4.24.87
uniprot
proteins
function
FUNCTION: Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation. {ECO:0000269|PubMed:15869605}.
uniprot
proteins
mass_dalton
155357
uniprot
proteins
post_translational_modification
PTM: The precursor is processed by a furin endopeptidase which cleaves off the pro-domain. {ECO:0000250}.; PTM: O-glycosylated (By similarity). 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 ADAMTS13. May also be C-glycosylated on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and also N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
15136581
uniprot
proteins
pubmed
15869605
uniprot
proteins
pubmed
19468303
uniprot
proteins
sequence_length
1426
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15136581}. Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats. {ECO:0000250}.
uniprot
proteins