| Primary information |
|---|
| ID | 13570 |
| Uniprot ID | P02675 |
| Description | Fibrinogen beta chain [Cleaved into- Fibrinopeptide B; Fibrinogen beta chain] |
| Organism | Homo sapiens |
| Txonomy | Eukaryota; Opisthokonta; Metazoa; Eumetazoa; Bilateria; Deuterostomia; Chordata; Craniata; Vertebrata; Gnathostomata (jawed vertebrates); Teleostomi; Euteleostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Mammalia; Theria; Eutheria; Boreoeutheria; Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini; Hominoidea (apes); Hominidae (great apes); Homininae; Homo; Homo sapiens (Human) |
| Subcellular Location | Secreted |
| Developmental Stage | NA |
| Similarity | NA |
| Tissue Specificity | Detected in blood plasma (at protein level). |
| 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 alpha (FGA) 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. 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 antibacterial immune response via both innate and T-cell mediated pathways. |
| Length | 491 |
| Molecular Weight | 55 |
| Name | Fibrinogen beta chain |
| Sequence | HRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ |
| Sequence map | 53-11 |
| PDB ID | 1FZA; 1FZB; 1FZC; 1FZE; 1FZF; 1FZG; 1LT9; 1LTJ; 1N86; 1N8E; 1RE3; 1RE4; 1RF0; 1RF1; 2A45; 2FFD; 2H43 |
| Drugpedia | DB04919;DB13151;DB11571;DB11311;DB00364;DB11300;DB |
| Receptor | NA |
| Domain | A long coiled coil structure formed by 3 polypepti |
| Pharmaceutical Use | NA
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