Primary information |
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ID | 12442 |
Uniprot ID | Q8VCM7 |
Description | Fibrinogen gamma chain |
Organism | Mus musculus |
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; Mus; Mus; Mus musculus (Mouse) |
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 | Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB); polymerizes 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 |
Length | 436 |
Molecular Weight | 49 |
Name | Fibrinogen gamma chain |
Sequence | VATRDNCCILDERFGSFCPTTCGIADFLSSYQTDVDNDLRTLEDILFRAENRTTEAKELIKAIQVYYNPDQPPKPGMIDSATQKSKKMVEEIVKYEALLLTHETSIRYLQEIYNSNNQKITNLKQKVAQLEAQCQEPCKDSVQIHDTTGKDCQEIANKGAKESGLYFIRPLKAKQQFLVYCEIDGSGNGWTVLQKRIDGSLDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWNGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYHQGGTYSKSSTTNGFDDGIIWATWKSRWYSMKETTMKIIPFNRLSIGEGQQHHMGGSKQAGDV |
Sequence map | 33-16 |
PDB ID | NA |
Drugpedia | NA |
Receptor | NA |
Domain | A long coiled coil structure formed by 3 polypepti |
Pharmaceutical Use | NA
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