| IED ID | IndEnz0002004691 |
| Enzyme Type ID | protease004691 |
| Protein Name |
A disintegrin and metalloproteinase with thrombospondin motifs 13 ADAM-TS 13 ADAM-TS13 ADAMTS-13 EC 3.4.24.87 von Willebrand factor-cleaving protease vWF-CP vWF-cleaving protease |
| Gene Name | Adamts13 Gm710 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MSQLCLWLTCQPCYAVSVRGILTGAIFILGCWGLSDFQKSLLQDLEPKDVSSYFGHHAAPFTGHPPSHLQRLRRRRTLEDILHLELLVAVGPDVSRAHQEDTERYVLTNLNIGSELLRNPSLGVQFQVHLVKLITLSDSESTPNITANITSSLMSVCEWSQTINPHDDRDPSHADLILYITRFDLELPDGNQQVRGVTQLGGACSLSWSCLITEDTGFDLGVTIAHEIGHSFGLDHDGAPGSGSTCKASGHVMAADGATPTGGTLEWSACSQRQLQHLLSTGQMHCFQDPPGLQSGLTRHQLMAQPGLYYSADDQCRVAFGSGAVACTFSREGLDVCQALSCHTDPLDQSSCSRLLVPLLDGTECGVEKWCSKARCRSLAELAPVAAVHGHWSSWGPHSPCSRSCGGGVITRRRWCNNPRPAFGGRACVGEDLQAKMCNTQACEKTQLEFMSEQCAQTDRQPLQLSQGTASFYHWDAAVQYSQGDTLCRHMCWAVGESFIVSRGDRFLDGTRCVPSGPQDDGTLSLCLLGSCRTFGCDGRMDSQKVWDACQVCGGDNSTCSSRNGSFTAGRAREYVTFLIVTPNMTNAHIVNRRPLFTHLAVRIQGHYIVAGKTSISPNTTYPSLLEDYRVEYRVTLTEDQLPHLEEIHIRGPVRDDIEIQVYRRYGGEYGDLTHPDITFSYFQLKQQAAWVWTAKRGPCSVSCGAGLRWVTYSCQDQAQDKWVKNAQCQGSPQPPAWQEPCVSAPCSPYWVAGDFSPCSVSCGGGLRERSLRCVETQDGFLKTLPPARCRAVAQQPAAEVENCNSQPCPTRWEVSDPGPCMSSACEAGLDSRNVTCVSRAGDPEKPETAGPCRTDEMSAMLEPCSRSLCSPGLGQVDNTMSLGEEAPSPVGSDKPGAQAEHVWTPLVGLCSISCGRGLKELYFLCMDSVLKMPVQEELCGLASKPPSRWEVCRARPCPARWETQVLAPCPVTCGGGRVPLSVRCVQLDRGHPISVPHSKCSPVPKPGSFEDCSPEPCPARWKVLSLGPCSASCGLGTATQMVACMQLDQGHDNEVNETFCKALVRPQASVPCLIADCAFRWHISAWTECSVSCGDGIQRRHDTCLGPQAQVPVPANFCQHLPKPMTVRGCWAGPCAGQETSSSLPHKEATLPSQTQAAATVASLQWSQPRARTPTLFSASQSLGLQENLEEHGACGRQYLEPTGTIHMRDQGRLDCVVAIGRPLGEVVTLQILESSLKCSAGEQLLLWGRFTWRKTCRKMPGMTFSTKTNTVVVKQHRVLPGGGVLLRYWSQPAPGTFYKECDRQLFGPRGEIVSPSLSPDGRKAGTCRVFISVAPQARIAIRALASDMGTASEGTNANYVSIRDIHSLRTTTFWGQQVLYWESEGSEAELEFSPGFLEAHASLQGEYWTISPRTSEQDDSLALS |
| Enzyme Length | 1426 |
| Uniprot Accession Number | Q769J6 |
| Absorption | |
| Active Site | ACT_SITE 227; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| 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}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=The enzyme cleaves the von Willebrand factor at bond 842-Tyr-|-Met-843 within the A2 domain.; EC=3.4.24.87; Evidence={ECO:0000269|PubMed:15869605}; |
| DNA Binding | |
| EC Number | 3.4.24.87 |
| Enzyme Function | FUNCTION: Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation. {ECO:0000269|PubMed:15869605}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (14); Domain (12); Glycosylation (14); Metal binding (11); Motif (1); Natural variant (2); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1) |
| Keywords | Blood coagulation;Calcium;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hemostasis;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15136581}. Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats. {ECO:0000250}. |
| Modified Residue | |
| 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}. |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14610273; 15806136; 16141072; 16200209; 16368888; 16533881; 17414218; 17414219; 17426255; 17509843; 18006046; 18083848; 18263586; 18695007; 19109562; 19141866; 19541819; 19687510; 19965676; 20047094; 20200350; 20637190; 20644116; 20695979; 20704649; 21266777; 21494805; 21677750; 21720563; 21799176; 22123843; 22192156; 22212812; 22232208; 22529289; 22652598; 22712744; 22721582; 22915644; 22983446; 23051932; 23144461; 23515928; 23878316; 24115559; 24261607; 24357063; 24713928; 25442981; 25770910; 25800050; 25813552; 25835743; 25849793; 25855507; 25977583; 26542631; 26929275; 27444201; 27479501; 27507004; 27602496; 27604194; 27626380; 28011677; 28254814; 28428179; 28495930; 29348121; 29729651; 29941674; 29976618; 31185010; 31340669; 31409673; 32135568; 32196558; |
| Motif | MOTIF 503..505; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 155,357 |
| Kinetics | |
| Metal Binding | METAL 85; /note=Calcium; /evidence=ECO:0000250; METAL 175; /note=Calcium; /evidence=ECO:0000250; METAL 184; /note=Calcium; high affinity; /evidence=ECO:0000250|UniProtKB:Q76LX8; METAL 186; /note=Calcium; high affinity; /evidence=ECO:0000250|UniProtKB:Q76LX8; METAL 189; /note=Calcium; high affinity; /evidence=ECO:0000250|UniProtKB:Q76LX8; METAL 214; /note=Calcium; high affinity; /evidence=ECO:0000250|UniProtKB:Q76LX8; METAL 226; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UNA0; METAL 230; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UNA0; METAL 236; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9UNA0; METAL 281; /note=Calcium; /evidence=ECO:0000250; METAL 289; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.87; |