Detail Information for IndEnz0002005420
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;