Fibrinogen beta chain

Details

Name
Fibrinogen beta chain
Synonyms
  • Fibrinogen beta chain precursor
Gene Name
FGB
Organism
Humans
Amino acid sequence
>lcl|BSEQ0004100|Fibrinogen beta chain
MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLR
PAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQE
RPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQ
LYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKE
CEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYK
QGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFT
VQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDP
RKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKM
SMKIRPFFPQQ
Number of residues
491
Molecular Weight
55927.9
Theoretical pI
8.38
GO Classification
Functions
chaperone binding / structural molecule activity
Processes
adaptive immune response / blood coagulation / blood coagulation, fibrin clot formation / cell-matrix adhesion / cellular protein complex assembly / cellular response to interleukin-1 / cellular response to leptin stimulus / extracellular matrix organization / fibrinolysis / induction of bacterial agglutination / innate immune response / negative regulation of endothelial cell apoptotic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / plasminogen activation / platelet activation / platelet aggregation / platelet degranulation / positive regulation of ERK1 and ERK2 cascade / positive regulation of exocytosis / positive regulation of heterotypic cell-cell adhesion / positive regulation of peptide hormone secretion / positive regulation of protein secretion / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of vasoconstriction / protein polymerization / response to calcium ion / signal transduction
Components
blood microparticle / cell cortex / cell surface / external side of plasma membrane / extracellular exosome / extracellular region / extracellular space / extracellular vesicle / fibrinogen complex / plasma membrane / platelet alpha granule / platelet alpha granule lumen
General Function
Structural molecule activity
Specific 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0019235|Fibrinogen beta chain (FGB)
ATGAAAAGGATGGTTTCTTGGAGCTTCCACAAACTTAAAACCATGAAACATCTATTATTG
CTACTATTGTGTGTTTTTCTAGTTAAGTCCCAAGGTGTCAACGACAATGAGGAGGGTTTC
TTCAGTGCCCGTGGTCATCGACCCCTTGACAAGAAGAGAGAAGAGGCTTTGCTACAACAG
GAAAGGCCAATCAGAAATAGTGTTGATGAGTTAAATAACAATGTGGAAGCTGTTTCCCAG
ACCTCCTCTTCTTCCTTTCAGTACATGTATTTGCTGAAAGACCTGTGGCAAAAGAGGCAG
AAGCAAGTAAAAGATAATGAAAATGTAGTCAATGAGTACTCCTCAGAACTGGAAAAGCAC
CAATTATATATAGATGAGACTGTGAATAGCAATATCCCAACTAACCTTCGTGTGCTTCGT
TCAATCCTGGAAAACCTGAGAAGCAAAATACAAAAGTTAGAATCTGATGTCTCAGCTCAA
ATGGAATATTGTCGCACCCCATGCACTGTCAGTTGCAATATTCCTGTGGTGTCTGGCAAA
GAATGTGAGGAAATTATCAGGAAAGGAGGTGAAACATCTGAAATGTATCTCATTCAACCT
GACAGTTCTGTCAAACCGTATAGAGTATACTGTGACATGAATACAGAAAATGGAGGATGG
ACAGTGATTCAGAACCGTCAAGACGGTAGTGTTGACTTTGGCAGGAAATGGGATCCATAT
AAACAGGGATTTGGAAATGTTGCAACCAACACAGATGGGAAGAATTACTGTGGCCTACCA
GGTGAATATTGGCTTGGAAATGATAAAATTAGCCAGCTTACCAGGATGGGACCCACAGAA
CTTTTGATAGAAATGGAGGACTGGAAAGGAGACAAAGTAAAGGCTCACTATGGAGGATTC
ACTGTACAGAATGAAGCCAACAAATACCAGATCTCAGTGAACAAATACAGAGGAACAGCC
GGTAATGCCCTCATGGATGGAGCATCTCAGCTGATGGGAGAAAACAGGACCATGACCATT
CACAACGGCATGTTCTTCAGCACGTATGACAGAGACAATGACGGCTGGTTAACATCAGAT
CCCAGAAAACAGTGTTCTAAAGAAGACGGTGGTGGATGGTGGTATAATAGATGTCATGCA
GCCAATCCAAACGGCAGATACTACTGGGGTGGACAGTACACCTGGGACATGGCAAAGCAT
GGCACAGATGATGGTGTAGTATGGATGAATTGGAAGGGGTCATGGTACTCAATGAGGAAG
ATGAGTATGAAGATCAGGCCCTTCTTCCCACAGCAATAG
Chromosome Location
4
Locus
4q28
External Identifiers
ResourceLink
UniProtKB IDP02675
UniProtKB Entry NameFIBB_HUMAN
GenBank Protein ID182430
GenBank Gene IDJ00129
GenAtlas IDFGB
HGNC IDHGNC:3662
General References
  1. Chung DW, Que BG, Rixon MW, Mace M Jr, Davie EW: Characterization of complementary deoxyribonucleic acid and genomic deoxyribonucleic acid for the beta chain of human fibrinogen. Biochemistry. 1983 Jun 21;22(13):3244-50. [Article]
  2. Chung DW, Harris JE, Davie EW: Nucleotide sequences of the three genes coding for human fibrinogen. Adv Exp Med Biol. 1990;281:39-48. [Article]
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  5. Chung DW, Rixon MW, Que BG, Davie EW: Cloning of fibrinogen genes and their cDNA. Ann N Y Acad Sci. 1983 Jun 27;408:449-56. [Article]
  6. Huber P, Dalmon J, Courtois G, Laurent M, Assouline Z, Marguerie G: Characterization of the 5'-flanking region for the human fibrinogen beta gene. Nucleic Acids Res. 1987 Feb 25;15(4):1615-25. [Article]
  7. Watt KW, Takagi T, Doolittle RF: Amino acid sequence of the beta chain of human fibrinogen. Biochemistry. 1979 Jan 9;18(1):68-76. [Article]
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  22. Everse SJ, Spraggon G, Veerapandian L, Doolittle RF: Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. Biochemistry. 1999 Mar 9;38(10):2941-6. [Article]
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  29. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [Article]
  30. Duga S, Asselta R, Santagostino E, Zeinali S, Simonic T, Malcovati M, Mannucci PM, Tenchini ML: Missense mutations in the human beta fibrinogen gene cause congenital afibrinogenemia by impairing fibrinogen secretion. Blood. 2000 Feb 15;95(4):1336-41. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04919AlfimepraseinvestigationalunknownDetails
DB11311ProthrombinapprovedyescleavageDetails
DB13151Anti-inhibitor coagulant complexapproved, investigationalyescleavageDetails
DB11572Thrombin alfaapprovedyesactivatorDetails
DB11571Human thrombinapprovedyesactivatorDetails
DB11300Thrombinapproved, investigationalyesactivatorDetails
DB00364SucralfateapprovedunknownbinderDetails