| IED ID | IndEnz0002010340 |
| Enzyme Type ID | protease010340 |
| Protein Name |
Fibrinogen alpha chain Cleaved into: Fibrinopeptide A Fragment |
| Gene Name | FGA |
| Organism | Tiliqua rugosa (Shingleback lizard) (Trachydosaurus rugosus) |
| 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) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Scinciformata Scincidae (skinks) Egerniinae Tiliqua Tiliqua rugosa (Shingleback lizard) (Trachydosaurus rugosus) |
| Enzyme Sequence | EDTGTFEEGHGGVR |
| Enzyme Length | 14 |
| Uniprot Accession Number | Q7LZT3 |
| 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 | Non-terminal residue (1); Peptide (1) |
| Keywords | Blood coagulation;Coiled coil;Direct protein sequencing;Disulfide bond;Hemostasis;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02671}. |
| Modified Residue | |
| 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 | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,491 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |