Detail Information for IndEnz0002006997
IED ID IndEnz0002006997
Enzyme Type ID protease006997
Protein Name Fibrinogen alpha chain
Cleaved into: Fibrinopeptide A
Fragment
Gene Name FGA
Organism Anas platyrhynchos (Mallard) (Anas boschas)
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 Anseriformes (ducks geese and swans) Anatidae (waterfowl) Anatinae Anas (ducks) Anas platyrhynchos (Mallard) (Anas boschas)
Enzyme Sequence QDGKSSFQKEGGGVR
Enzyme Length 15
Uniprot Accession Number P12801
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 Modified residue (1); Non-terminal residue (1); Peptide (1)
Keywords Blood coagulation;Coiled coil;Direct protein sequencing;Disulfide bond;Hemostasis;Pyrrolidone carboxylic acid;Secreted
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:3983613
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 1,580
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda