| IED ID | IndEnz0002006053 |
| Enzyme Type ID | protease006053 |
| Protein Name |
Coagulation factor XI FXI EC 3.4.21.27 Plasma thromboplastin antecedent PTA Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain |
| Gene Name | F11 |
| Organism | Bos taurus (Bovine) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MTLLYQMVHFALFASVAGECVTTLFQDACFKGGDITVAFAPNAKHCQIICTHHPRCLLFTFMTESSSEDPTKWYTCILKDSVTETLPMVNMTGAISGYSSKQCLHHISACSKDMYVDLNMKGMNYNSSLAQSARECQQRCTDDTHCHFFTFATRHFPSIKDRNTCLLKNTQTGTPTSITKLHEVVSGFSLKSCGLSNLACIRDIFPRTAFVDITIDTVMAPDPFVCRSICTHHPSCLFFTFLSEEWPTASERNLCLLKTSSSGLPSARFRKNRAFSGFSLQHCQHSVPVFCHSSFYRNTDFLGEELDIVDADSHEACQKTCTNSIRCQFFTYSPSQESCNGGKGKCYLKLSANGSPTKILHGTGSISGYTLRLCKMDNVCTTKIKTRIVGGTQSVHGEWPWQITLHVTSPTQRHLCGGAIIGNQWILTAAHCFNEVKSPNVLRVYSGILNQSEIKEDTSFFGVQEIIIHDQYEKAESGYDIALLKLETAMNYTDSQWPICLPSKGDRNVMYTECWVTGWGYRKLRDKIQNTLQKAKVPLMTNEECQAGYREHRITSKMVCAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCGQRERPGVYSNVVEYVDWILEKTQGP |
| Enzyme Length | 625 |
| Uniprot Accession Number | Q5NTB3 |
| Absorption | |
| Active Site | ACT_SITE 431; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 480; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 575; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.; EC=3.4.21.27; |
| DNA Binding | |
| EC Number | 3.4.21.27 |
| Enzyme Function | FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (19); Domain (5); Glycosylation (4); Natural variant (1); Region (1); Signal peptide (1) |
| Keywords | Blood coagulation;Disease variant;Disulfide bond;Glycoprotein;Hemostasis;Heparin-binding;Hydrolase;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by factor XIIa (or XII), which cleaves each polypeptide after Arg-387 into the light chain, which contains the active site, and the heavy chain, which associates with high molecular weight (HMW) kininogen. {ECO:0000250}.; PTM: N-glycosylated on both chains. N-glycosylated sites mainly consist of nonfucosylated sialylated biantennary (in high abundance) and/or triantennary (in low abundance) complex structures. {ECO:0000250|UniProtKB:P03951}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 69,872 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |