ADAMTS13
entrez
11093
canonical
uniprot
Q76LX8
canonical
ensembl
ENSG00000160323
resolver
ensembl
ENSG00000281244
resolver
ensp
ENSP00000347927
resolver
ensp
ENSP00000348997
resolver
ensp
ENSP00000360997
resolver
genesymbol
ADAMTS13
resolver
genesymbol_syn
C9orf8
resolver
hgnc
HGNC:1366
resolver
uniprot
Q6UY16
resolver
uniprot
Q710F6
resolver
uniprot
Q711T8
resolver
uniprot
Q96L37
resolver
uniprot
Q9H0G3
resolver
uniprot
Q9UGQ1
resolver
uniprot_entry
ATS13_HUMAN
resolver
uniprot_sec
Q6UY16
resolver
uniprot_sec
Q710F6
resolver
uniprot_sec
Q711T8
resolver
uniprot_sec
Q96L37
resolver
uniprot_sec
Q9H0G3
resolver
uniprot_sec
Q9UGQ1
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. {ECO:0000269|PubMed:12975358, ECO:0000269|PubMed:16286459, ECO:0000269|PubMed:19047683}.
uniprot
proteins
amino_acid_sequence
MHQRHPRARCPPLCVAGILACGFLLGCWGPSHFQQSCLQALEPQAVSSYLSPGAPLKGRPPSPGFQRQRQRQRRAAGGILHLELLVAVGPDVFQAHQEDTERYVLTNLNIGAELLRDPSLGAQFRVHLVKMVILTEPEGAPNITANLTSSLLSVCGWSQTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAPGSGCGPSGHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVWDPPRPQPGSAGHPPDAQPGLYYSANEQCRVAFGPKAVACTFAREHLDMCQALSCHTDPLDQSSCSRLLVPLLDGTECGVEKWCSKGRCRSLVELTPIAAVHGRWSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACEKTQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLSLCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTCSPRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVRIGGRYVVAGKMSISPNTTYPSLLEDGRVEYRVALTEDRLPRLEEIRIWGPLQEDADIQVYRRYGEEYGNLTRPDITFTYFQPKPRQAWVWAAVRGPCSVSCGAGLRWVNYSCLDQARKELVETVQCQGSQQPPAWPEACVLEPCPPYWAVGDFGPCSASCGGGLRERPVRCVEAQGSLLKTLPPARCRAGAQQPAVALETCNPQPCPARWEVSEPSSCTSAGGAGLALENETCVPGADGLEAPVTEGPGSVDEKLPAPEPCVGMSCPPGWGHLDATSAGEKAPSPWGSIRTGAQAAHVWTPAAGSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPGSRREVCQAVPCPARWQYKLAACSVSCGRGVVRRILYCARAHGEDDGEEILLDTQCQGLPRPEPQEACSLEPCPPRWKVMSLGPCSASCGLGTARRSVACVQLDQGQDVEVDEAACAALVRPEASVPCLIADCTYRWHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPCVGQGTPSLVPHEEAAAPGRTTATPAGASLEWSQARGLLFSPAPQPRRLLPGPQENSVQSSACGRQHLEPTGTIDMRGPGQADCAVAIGRPLGEVVTLRVLESSLNCSAGDMLLLWGRLTWRKMCRKLLDMTFSSKTNTLVVRQRCGRPGGGVLLRYGSQLAPETFYRECDMQLFGPWGEIVSPSLSPATSNAGGCRLFINVAPHARIAIHALATNMGAGTEGANASYILIRDTHSLRTTAFHGQQVLYWESESSQAEMEFSEGFLKAQASLRGQYWTLQSWVPEMQDPQSWKGKEGT
uniprot
proteins
disease_involvement
DISEASE: Thrombotic thrombocytopenic purpura, hereditary (TTP) [MIM:274150]: An autosomal recessive hematologic disease characterized by hemolytic anemia with fragmentation of erythrocytes, thrombocytopenia, diffuse and non-focal neurologic findings, decreased renal function and fever. {ECO:0000269|PubMed:11586351, ECO:0000269|PubMed:12181489, ECO:0000269|PubMed:12393505, ECO:0000269|PubMed:12614216, ECO:0000269|PubMed:12753286, ECO:0000269|PubMed:14512317, ECO:0000269|PubMed:14563640, ECO:0000269|PubMed:15009458, ECO:0000269|PubMed:15126318, ECO:0000269|PubMed:15327386, ECO:0000269|PubMed:16160007, ECO:0000269|PubMed:16449289, ECO:0000269|PubMed:16453338, ECO:0000269|PubMed:16796708, ECO:0000269|PubMed:16807643, ECO:0000269|PubMed:17003922, ECO:0000269|PubMed:18443791, ECO:0000269|PubMed:19055667, ECO:0000269|PubMed:19116307, ECO:0000269|PubMed:22075512}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:19880749}.
uniprot
proteins
mass_dalton
153604
uniprot
proteins
mutagenesis
MUTAGEN 71; /note="R->K: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with D-73."; /evidence="ECO:0000269|PubMed:12975358"; MUTAGEN 73; /note="R->D: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with K-71."; /evidence="ECO:0000269|PubMed:12975358"; MUTAGEN 83; /note="E->A: No change in calcium dependence for proteolysis."; /evidence="ECO:0000269|PubMed:19047683"; MUTAGEN 173; /note="D->A: No change in calcium dependence for proteolysis."; /evidence="ECO:0000269|PubMed:19047683"; MUTAGEN 184; /note="E->A: Dramatically reduced affinity for calcium."; /evidence="ECO:0000269|PubMed:19047683"; MUTAGEN 187; /note="D->A: Dramatically reduced affinity for calcium."; /evidence="ECO:0000269|PubMed:19047683"; MUTAGEN 212; /note="E->A: Dramatically reduced affinity for calcium."; /evidence="ECO:0000269|PubMed:19047683"; MUTAGEN 399; /note="S->A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-698."; /evidence="ECO:0000269|PubMed:17395589"; MUTAGEN 698; /note="S->A: No effect on cleavage of VWF and greatly reduced secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-399."; /evidence="ECO:0000269|PubMed:17395589"; MUTAGEN 757; /note="S->A: No effect on cleavage of VWF and little change in secretion of ADAMTS13."; /evidence="ECO:0000269|PubMed:17395589"; MUTAGEN 907; /note="S->A: No effect on cleavage of VWF and greatly reduced secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-965."; /evidence="ECO:0000269|PubMed:17395589"; MUTAGEN 965; /note="S->A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-907."; /evidence="ECO:0000269|PubMed:17395589"; MUTAGEN 1027; /note="S->A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-1087."; /evidence="ECO:0000269|PubMed:17395589"; MUTAGEN 1087; /note="S->A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-1027."; /evidence="ECO:0000269|PubMed:17395589
uniprot
proteins
post_translational_modification
PTM: Glycosylated. 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. {ECO:0000269|PubMed:11557746, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17395589, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19880749}.; PTM: The precursor is processed by a furin endopeptidase which cleaves off the pro-domain.
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11535494
uniprot
proteins
pubmed
11535495
uniprot
proteins
pubmed
11557746
uniprot
proteins
pubmed
11574066
uniprot
proteins
pubmed
11586351
uniprot
proteins
pubmed
11867212
uniprot
proteins
pubmed
12181489
uniprot
proteins
pubmed
12393505
uniprot
proteins
pubmed
12614216
uniprot
proteins
pubmed
12753286
uniprot
proteins
pubmed
12791682
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
12975358
uniprot
proteins
pubmed
14512317
uniprot
proteins
pubmed
14563640
uniprot
proteins
pubmed
15009458
uniprot
proteins
pubmed
15126318
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15327386
uniprot
proteins
pubmed
16160007
uniprot
proteins
pubmed
16286459
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16449289
uniprot
proteins
pubmed
16453338
uniprot
proteins
pubmed
16468327
uniprot
proteins
pubmed
16796708
uniprot
proteins
pubmed
16807643
uniprot
proteins
pubmed
17003922
uniprot
proteins
pubmed
17395589
uniprot
proteins
pubmed
18443791
uniprot
proteins
pubmed
19047683
uniprot
proteins
pubmed
19055667
uniprot
proteins
pubmed
19116307
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19847791
uniprot
proteins
pubmed
19880749
uniprot
proteins
pubmed
21488199
uniprot
proteins
pubmed
22075512
uniprot
proteins
sequence_length
1427
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12791682}. Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats.
uniprot
proteins