Fibrinogen beta chain

Details

Name
Fibrinogen beta chain
Kind
protein
Synonyms
Not Available
Gene Name
FGB
UniProtKB Entry
P02675Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
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
extracellular matrix structural constituent / protein-folding chaperone binding / signaling receptor binding
Processes
protein-containing complex assembly
Components
collagen-containing extracellular matrix / endoplasmic reticulum / synapse
General 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
Specific Function
extracellular matrix structural constituent
Pfam Domain Function
Signal Regions
1-30
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
4q31.3
External Identifiers
ResourceLink
UniProtKB IDP02675
UniProtKB Entry NameFIBB_HUMAN
GenBank Protein ID182430
GenBank Gene IDJ00129
GeneCard IDFGB
GenAtlas IDFGB
HGNC IDHGNC:3662
PDB ID(s)1FZA, 1FZB, 1FZC, 1FZE, 1FZF, 1FZG, 1LT9, 1LTJ, 1N86, 1N8E, 1RE3, 1RE4, 1RF0, 1RF1, 2A45, 2FFD, 2H43, 2HLO, 2HOD, 2HPC, 2OYH, 2OYI, 2Q9I, 2XNX, 2XNY, 2Z4E, 3BVH, 3E1I, 3GHG, 3H32, 3HUS, 6ATZ, 6BIJ, 6BIL, 6V0Y, 6V13, 6V15, 6V18, 6V19, 6V1A
KEGG IDhsa:2244
NCBI Gene ID2244
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]
  8. Blomback B, Hessel B, Hogg D: Disulfide bridges in nh2 -terminal part of human fibrinogen. Thromb Res. 1976 May;8(5):639-58. [Article]
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  11. Gardlund B, Hessel B, Marguerie G, Murano G, Blomback B: Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments. Eur J Biochem. 1977 Aug 1;77(3):595-610. [Article]
  12. Doolittle RF: Fibrinogen and fibrin. Annu Rev Biochem. 1984;53:195-229. [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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  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]
  31. Lounes KC, Lefkowitz JB, Henschen-Edman AH, Coates AI, Hantgan RR, Lord ST: The impaired polymerization of fibrinogen Longmont (Bbeta166Arg-->Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers. Blood. 2001 Aug 1;98(3):661-6. [Article]
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Associated Data

Drug Relations
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