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Details on Person UniProt:P02671-1 FGA
| Class:Id | ReferenceIsoform:402297 |
|---|---|
| _chainChangeLog | signal peptide:1-19 added on Sat February 7 2015;peptide:20-35 added on Sat February 7 2015;chain:36-866 added on Sat February 7 2015 |
| _displayName | UniProt:P02671-1 FGA |
| _timestamp | 2024-11-03 19:51:11 |
| chain | signal peptide:1-19 peptide:20-35 chain:36-866 |
| checksum | EA73A81204D8AEC4 |
| comment | 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.SUBUNIT Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain.SUBUNIT (Microbial infection) Interacts with Staphylococcus aureus protein Fib; this interaction inhibits fibrinogen-dependent platelet aggregation and protects the bacteria form phagocytosis.INTERACTION Detected in blood plasma (at protein level).DOMAIN A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.PTM The alpha chain is normally not N-glycosylated (PubMed:23151259), even though glycosylation at Asn-686 was observed when a fragment of the protein was expressed in insect cells (PubMed:9689040). It is well known that heterologous expression of isolated domains can lead to adventitious protein modifications. Besides, glycosylation at Asn-686 is supported by large-scale glycoproteomics studies (PubMed:16335952, PubMed:19159218), but the evidence is still quite tenuous. Most likely, Asn-686 is not glycosylated in the healthy human body, or only with low efficiency.PTM O-glycosylated.PTM Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.PTM About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.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 Phosphorylated by FAM20C in the extracellular medium.DISEASE The disease is caused by variants affecting the gene represented in this entry. The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.ONLINE INFORMATION Fibrinogen entry |
| created | [InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35 |
| description | recommendedName: Fibrinogen alpha chain component recommendedName: Fibrinopeptide A /component component recommendedName: Fibrinogen alpha chain /component |
| geneName | FGA |
| identifier | P02671 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Adaptive immunity Alternative splicing Amyloid Amyloidosis Blood coagulation Calcium Coiled coil Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemostasis Hydroxylation Immunity Innate immunity Isopeptide bond Metal-binding Phosphoprotein Proteomics identification Reference proteome Secreted Signal |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | FGA |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9001767] ENSEMBL:ENSG00000171560 FGA [Homo sapiens] |
| secondaryIdentifier | FIBA_HUMAN A8K3E4 D3DP14 D3DP15 Q4QQH7 Q9BX62 Q9UCH2 |
| sequenceLength | 866 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | P02671-1 |
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No pathways have been reviewed or authored by UniProt:P02671-1 FGA (402297)
