| IED ID | IndEnz0002003785 |
| Enzyme Type ID | protease003785 |
| Protein Name |
Fibrinogen alpha chain Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain |
| Gene Name | Fga |
| 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 | MLSLRVTCLILSVASTVWTTDTEDKGEFLSEGGGVRGPRVVERHQSQCKDSDWPFCSDDDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQRNNKDSNSLTRNIMEYLRGDFANANNFDNTYGQVSEDLRRRIEILRRKVIEKAQQIQALQSNVRAQLIDMKRLEVDIDIKIRSCKGSCSRAVNREINLQDYEGHQKQLQQVIAKELLPTKDRQYLPALKMSPVPDLVPGSFKSQLQEAPPEWKALTEMRQMRMELERPGKDGGSRGDSPGDSRGDSRGDFATRGPGSKAENPTNPGPGGSGYWRPGNSGSGSDGNRNPGTTGSDGTGDWGTGSPRPGSDSGNFRPANPNWGVFSEFGDSSSPATRKEYHTGKAVTSKGDKELLIGKEKVTSSGTSTTHRSCSKTITKTVTGPDGRREVVKEVITSDDGSDCGDATELDISHSFSGSLDELSERHPDLSGFFDNHFGLISPNFKEFGSKTHSDSDILTNIEDPSSHVPEFSSSSKTSTVKKQVTKTYKMADEAGSEAHREGETRNTKRGRARARPTRDCDDVLQTQTSGAQNGIFSIKPPGSSKVFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDKGEGEFWLGNDYLHLLTLRGSVLRVELEDWAGKEAYAEYHFRVGSEAEGYALQVSSYRGTAGDALVQGSVEEGTEYTSHSNMQFSTFDRDADQWEENCAEVYGGGWWYNSCQAANLNGIYYPGGTYDPRNNSPYEIENGVVWVPFRGADYSLRAVRMKIRPLVGQ |
| Enzyme Length | 789 |
| Uniprot Accession Number | E9PV24 |
| 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 beta (FGB) 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 (PubMed:7649481). In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization (PubMed:11389004). Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood (PubMed:7649481). However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo (PubMed:10930441). Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway (PubMed:19332769). Maternal fibrinogen is essential for successful pregnancy (PubMed:7649481). Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage (PubMed:12629066). May also facilitate the immune response via both innate and T-cell mediated pathways (PubMed:23487423). {ECO:0000250|UniProtKB:P02671, ECO:0000269|PubMed:10930441, ECO:0000269|PubMed:11389004, ECO:0000269|PubMed:12629066, ECO:0000269|PubMed:15972474, ECO:0000269|PubMed:19332769, ECO:0000269|PubMed:23487423, ECO:0000269|PubMed:7649481}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (4); Disulfide bond (8); Domain (1); Glycosylation (1); Metal binding (4); Modified residue (3); Peptide (1); Region (2); Signal peptide (1); Site (4) |
| Keywords | Adaptive immunity;Alternative splicing;Blood coagulation;Calcium;Coiled coil;Disulfide bond;Glycoprotein;Hemostasis;Hydroxylation;Immunity;Innate immunity;Metal-binding;Phosphoprotein;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7649481}. |
| Modified Residue | MOD_RES 46; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 447; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 504; /note=4-hydroxyproline; by P4HA1; /evidence=ECO:0000250|UniProtKB:P02671 |
| 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. {ECO:0000250|UniProtKB:P02671}.; PTM: Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. {ECO:0000250|UniProtKB:P02671}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02671}. |
| Signal Peptide | SIGNAL 1..19; /evidence="ECO:0000250|UniProtKB:P06399, ECO:0000255" |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10749569; 10829076; 10903997; 11018075; 11104787; 11154109; 11159184; 11704568; 11733368; 11891199; 11906694; 12218060; 12460914; 12579195; 12750384; 14504091; 14615369; 14644995; 14709993; 15031212; 15096619; 15304043; 15364412; 15367435; 15914557; 16006527; 16141072; 16434493; 16452087; 16615898; 16707424; 16824188; 16877357; 17307940; 17371949; 17664291; 17722076; 17932565; 18593877; 19036705; 19056689; 20028811; 20152176; 20547128; 20876456; 21267068; 21305474; 21356363; 21677750; 21724997; 21734641; 22006565; 22159717; 22272319; 22381526; 22507835; 22539596; 22819533; 23029147; 23187627; 23804451; 24664548; 24821909; 24990151; 25007874; 25336631; 26214526; 26228483; 26238780; 26647393; 27140400; 28071719; 28275164; 29400711; 29723163; 30737131; 31101623; 34572594; 34941394; 8288233; 8497848; 8929539; 9275201; 9473227; 9486990; 9788960; 9819035; |
| Motif | |
| Gene Encoded By | |
| Mass | 87,429 |
| Kinetics | |
| Metal Binding | METAL 714; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P02671; METAL 716; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P02671; METAL 718; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P02671; METAL 720; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P02671 |
| Rhea ID | |
| Cross Reference Brenda |