FGA
entrez
2243
canonical
uniprot
P02671
canonical
ensembl
ENSG00000171560
resolver
ensp
ENSP00000385981
resolver
ensp
ENSP00000498441
resolver
genesymbol
FGA
resolver
hgnc
HGNC:3661
resolver
uniprot
A8K3E4
resolver
uniprot
D3DP14
resolver
uniprot
D3DP15
resolver
uniprot
Q4QQH7
resolver
uniprot
Q9BX62
resolver
uniprot
Q9UCH2
resolver
uniprot_entry
FIBA_HUMAN
resolver
uniprot_sec
A8K3E4
resolver
uniprot_sec
D3DP14
resolver
uniprot_sec
D3DP15
resolver
uniprot_sec
Q4QQH7
resolver
uniprot_sec
Q9BX62
resolver
uniprot_sec
Q9UCH2
resolver
amino_acid_sequence
MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ
uniprot
proteins
disease_involvement
DISEASE: Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. {ECO:0000269|PubMed:25427968}. Note=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: Amyloidosis, hereditary systemic 2 (AMYLD2) [MIM:105200]: A form of hereditary systemic amyloidosis, a disorder characterized by amyloid deposition in multiple tissues resulting in a wide clinical spectrum. AMYLD2 is an autosomal dominant form characterized by deposition of amyloid preferentially in the glomeruli of the kidney. It clinically presents with hypertension, proteinuria, and finally azotemia. Involvement of liver and spleen may be seen in advanced cases, but heavy glomerular deposition without significant medium sized vessel involvement is characteristic of the disease. {ECO:0000269|PubMed:8097946, ECO:0000269|PubMed:8113408}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Dysfibrinogenemia, congenital (DYSFIBRIN) [MIM:616004]: A disorder characterized by qualitative abnormalities (dysfibrinogenemia) of the circulating fibrinogen. Affected individuals are frequently asymptomatic, but some patients have bleeding diathesis, thromboembolic complications, or both. In some cases, dysfibrinogenemia is associated with low circulating fibrinogen levels (hypodysfibrinogenemia). {ECO:0000269|PubMed:16846481, ECO:0000269|PubMed:8473507}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
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. 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. {ECO:0000250|UniProtKB:E9PV24}.
uniprot
proteins
mass_dalton
94973
uniprot
proteins
post_translational_modification
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. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23151259, ECO:0000269|PubMed:9689040, ECO:0000305}.; PTM: O-glycosylated. {ECO:0000269|PubMed:23050552}.; 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. {ECO:0000269|PubMed:2143188}.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.
uniprot
proteins
pubmed
10074346
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
11418620
uniprot
proteins
pubmed
1457396
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1560020
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
1634621
uniprot
proteins
pubmed
1675636
uniprot
proteins
pubmed
16807684
uniprot
proteins
pubmed
16846481
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19296670
uniprot
proteins
pubmed
19696023
uniprot
proteins
pubmed
2070049
uniprot
proteins
pubmed
2102623
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2143188
uniprot
proteins
pubmed
23050552
uniprot
proteins
pubmed
23151259
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24348255
uniprot
proteins
pubmed
25427968
uniprot
proteins
pubmed
26091039
uniprot
proteins
pubmed
2877981
uniprot
proteins
pubmed
518845
uniprot
proteins
pubmed
518846
uniprot
proteins
pubmed
6318767
uniprot
proteins
pubmed
632262
uniprot
proteins
pubmed
6383194
uniprot
proteins
pubmed
6575389
uniprot
proteins
pubmed
6575700
uniprot
proteins
pubmed
6688355
uniprot
proteins
pubmed
6689067
uniprot
proteins
pubmed
741445
uniprot
proteins
pubmed
8097946
uniprot
proteins
pubmed
8113408
uniprot
proteins
pubmed
8461606
uniprot
proteins
pubmed
8473507
uniprot
proteins
pubmed
8675656
uniprot
proteins
pubmed
9333233
uniprot
proteins
pubmed
936108
uniprot
proteins
pubmed
9628725
uniprot
proteins
pubmed
9689040
uniprot
proteins
sequence_length
866
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9628725}.
uniprot
proteins