| IED ID | IndEnz0002006999 |
| Enzyme Type ID | protease006999 |
| Protein Name |
Fibrinogen alpha chain Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain |
| Gene Name | FGA |
| 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 | MIPVTILCVLLCLNLAWAQDGKTTFEKEGGGGRGPRILENMHESSCKYEKNWPICVDDDWGTKCPSCCRMQGIIDDTDQNYSQRIDNIRQQLADSQNKYKTSNRVIVETINILKPGLEGAQQLDENYGHVSTELRRRIVTLKQRVATQVNRIKALQNSIQEQVVEMKRLEVDIDIKIRACKGSCARSFDYQVDKEGYDNIQKHLTQASSIDMHPDFQTTTLSTLKMRPLKDSNVPEHFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKDCDDIRQKHTSGAKSGIFKIKPEGSNKVLSVYCDQETTLGGWLLIQQRMDGSVNFNRTWQDYRRGFGSVDGKGQGELWLGNENIHLLTQNDTLLRVELEDWDGNAAYAEYIVQVGTEAEGYALTVSSYEGTAGDALVAGWLEEGSEYTSHAQMQFSTFDRDQDHWEESCAEVYGGGWWYNSCQAANLNGIYYPGGHYDPRYNVPYEIENGVVWIPFRASDYSLKVVRMKIRPLETL |
| Enzyme Length | 741 |
| Uniprot Accession Number | P14448 |
| 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. {ECO:0000250|UniProtKB:E9PV24}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (1); Chain (1); Coiled coil (1); Compositional bias (3); Disulfide bond (8); Domain (1); Helix (3); Metal binding (4); Modified residue (1); Peptide (1); Region (2); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Alternative splicing;Blood coagulation;Calcium;Coiled coil;Direct protein sequencing;Disulfide bond;Hemostasis;Metal-binding;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10737772, ECO:0000269|PubMed:11601975}. |
| Modified Residue | MOD_RES 19; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:656462 |
| 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.; PTM: Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:656462 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1EI3; 1M1J; |
| Mapped Pubmed ID | 21932842; |
| Motif | |
| Gene Encoded By | |
| Mass | 82,438 |
| Kinetics | |
| Metal Binding | METAL 666; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P02671; METAL 668; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P02671; METAL 670; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P02671; METAL 672; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P02671 |
| Rhea ID | |
| Cross Reference Brenda |