IED ID | IndEnz0002005420 |
Enzyme Type ID | protease005420 |
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 | Homo sapiens (Human) |
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV |
Enzyme Length | 625 |
Uniprot Accession Number | P03951 |
Absorption | |
Active Site | ACT_SITE 431; /note=Charge relay system; ACT_SITE 480; /note=Charge relay system; ACT_SITE 575; /note=Charge relay system |
Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000269|PubMed:2844223}. |
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. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Alternative sequence (1); Beta strand (44); Chain (2); Disulfide bond (19); Domain (5); Glycosylation (5); Helix (21); Natural variant (63); Region (1); Sequence conflict (1); Signal peptide (1); Turn (4) |
Keywords | 3D-structure;Alternative splicing;Blood coagulation;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Hemostasis;Heparin-binding;Hydrolase;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal |
Interact With | P23827; Itself |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | 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. Glycosylation at Asn-163 uses a rare non-canonical Asn-X-Cys glycosite. {ECO:0000269|PubMed:25092234}.; 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. |
Signal Peptide | SIGNAL 1..18 |
Structure 3D | NMR spectroscopy (2); X-ray crystallography (93) |
Cross Reference PDB | 1XX9; 1XXD; 1XXF; 1ZHM; 1ZHP; 1ZHR; 1ZJD; 1ZLR; 1ZMJ; 1ZML; 1ZMN; 1ZOM; 1ZPB; 1ZPC; 1ZPZ; 1ZRK; 1ZSJ; 1ZSK; 1ZSL; 1ZTJ; 1ZTK; 1ZTL; 2F83; 2FDA; 2J8J; 2J8L; 3BG8; 3SOR; 3SOS; 4CR5; 4CR9; 4CRA; 4CRB; 4CRC; 4CRD; 4CRE; 4CRF; 4CRG; 4D76; 4D7F; 4D7G; 4NA7; 4NA8; 4TY6; 4TY7; 4WXI; 4X6M; 4X6N; 4X6O; 4X6P; 4Y8X; 4Y8Y; 4Y8Z; 5E2O; 5E2P; 5EOD; 5EOK; 5EXL; 5EXM; 5EXN; 5I25; 5Q0D; 5Q0E; 5Q0F; 5Q0G; 5Q0H; 5QCK; 5QCL; 5QCM; 5QCN; 5QQO; 5QQP; 5QTT; 5QTV; 5QTW; 5QTY; 5TKS; 5TKT; 5TKU; 5WB6; 6AOD; 6C0S; 6HHC; 6I58; 6R8X; 6TS4; 6TS5; 6TS6; 6TS7; 6TWB; 6USY; 6VLU; 6VLV; 6W50; 7MBO; |
Mapped Pubmed ID | 10781579; 11342438; 11696542; 12391017; 15545266; 16085935; 16204896; 16524727; 16613788; 16699514; 16876411; 17181160; 1730602; 17884987; 2019570; 2162822; 22505407; 22961984; 24405333; 25405503; 25592713; 25629509; 25728130; 2592373; 26005539; 26704266; 27006387; 27073051; 2713493; 2738071; 2752109; 2775660; 2788012; 28085275; 28687203; 28780160; 29077405; 29223926; 29336885; 29501396; 3009023; 3017409; 30692123; 30801944; 31445854; 31655039; 31833761; 31932224; 32309939; 32393891; 32456431; 32551603; 34494428; 588558; 8338946; 8463288; 893417; 9169594; 9888880; |
Motif | |
Gene Encoded By | |
Mass | 70,109 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.21.27; |