Primary information |
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ID | 13553 |
Uniprot ID | P06399 |
Description | Fibrinogen alpha chain [Cleaved into- Fibrinopeptide A; Fibrinogen alpha chain] |
Organism | Rattus norvegicus |
Txonomy | 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; Rattus; Rattus norvegicus (Rat) |
Subcellular Location | Secreted |
Developmental Stage | NA |
Similarity | NA |
Tissue Specificity | NA |
Post Translational Modification | 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 |
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. In addition; functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation; based on in vitro studies using anticoagulated blood. However; subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection; where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. |
Length | 782 |
Molecular Weight | 86 |
Name | Fibrinogen alpha chain |
Sequence | PRIVERQPSQCKETDWPFCSDEDWNHKCPSGCRMKGLIDEANQDFTNRINKLKNSLFDFQKNNKDSNSLTRNIMEYLRGDFANANNFDNTFGQVSEDLRRRIQILKRKVIEKAQQIQVLQKDVRDQLIDMKRLEVDIDIKIRSCKGSCSRSVSREINLKDYEGQQKQLEQVIAKDLLPAKDRQYLPAIKMSPVPDLVPGSFKSQLQEGPPEWKALTEMRQMRMELERPGKDGASRGDLPGDSRGDSATRGPGSKIENPMTPGHGGSGYWRPGSSGSGSDGNWGSGTTGSDDTGTWGAGSSRPSSGSGNLKPSNPDWGEFSEFGGSSSPATRKEYHTGKLVTSKGDKELLIGNEKVTSTGTSTTRRSCSKTITKTVLGNDGHREVVKEVVTSDDGSDCGDGMDLGLTHSFSGRLDELSRMHPELGSFYDSRFGSLTSNFKEFGSKTSDSDIFTDIENPSSHVPEFSSSSKTSTVRKQVTKSYKMADEAASEAHQEGDTRTTKRGRARTMRDCDDVLQTHPSGAQNGIFSIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDKGEGEFWLGNDYLHLLTLRGSVLRVELEDWAGKEAYAEYHFRVGSEAEGYALQVSSYQGTAGDALMEGSVEEGTEYTSHSNMQFSTFDRDADQWEENCAEVYGGGWWYNSCQAANLNGIYYPGGTYDPRNNSPYEIENGVLWVPFRGADYSLWAVRMKIRPLVGQ |
Sequence map | 50-02 |
PDB ID | NA |
Drugpedia | NA |
Receptor | NA |
Domain | A long coiled coil structure formed by 3 polypepti |
Pharmaceutical Use | NA
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