| IED ID | IndEnz0002005721 |
| Enzyme Type ID | protease005721 |
| Protein Name |
Fibrinogen beta chain Cleaved into: Fibrinopeptide B; Fibrinogen beta chain Fragment |
| Gene Name | FGB |
| Organism | Gallus gallus (Chicken) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | ASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPIIYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKFSDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNLDNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVSGRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQDGSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPTKVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGASQLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYFPD |
| Enzyme Length | 463 |
| Uniprot Accession Number | Q02020 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. {ECO:0000250|UniProtKB:E9PV24}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (17); Chain (1); Compositional bias (1); Disulfide bond (8); Domain (1); Glycosylation (1); Helix (12); Metal binding (3); Modified residue (1); Non-terminal residue (1); Peptide (1); Region (1); Site (1); Turn (1) |
| Keywords | 3D-structure;Blood coagulation;Calcium;Coiled coil;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis;Metal-binding;Reference proteome;Secreted;Sulfation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10737772, ECO:0000269|PubMed:11601975}. |
| Modified Residue | MOD_RES 5; /note=Sulfotyrosine; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1EI3; 1M1J; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,678 |
| Kinetics | |
| Metal Binding | METAL 384; /note="Calcium"; /evidence="ECO:0000269|PubMed:11601975, ECO:0007744|PDB:1M1J"; METAL 386; /note="Calcium"; /evidence="ECO:0000269|PubMed:11601975, ECO:0007744|PDB:1M1J"; METAL 388; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11601975, ECO:0007744|PDB:1M1J" |
| Rhea ID | |
| Cross Reference Brenda |