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Protein

Fibrinogen beta chain

Gene

FGB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

  • glycoprotein binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Blood coagulation, Hemostasis, Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen beta chain
Cleaved into the following 2 chains:
Gene namesi
Name:FGB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 2121Fibrinopeptide B1 PublicationPRO_0000009055Add
BLAST
Chaini22 – 468447Fibrinogen beta chainPRO_0000009056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid1 Publication
Glycosylationi4 – 41O-linked (GalNAc...)1 Publication
Modified residuei6 – 61Sulfotyrosine1 Publication
Disulfide bondi72 – 72Interchain (with C-58 in alpha chain)1 Publication
Disulfide bondi83 – 83Interchain (with C-71 in alpha chain)1 Publication
Disulfide bondi87 – 87Interchain (with C-43 in gamma chain)
Disulfide bondi200 – 200Interchain (with C-187 in alpha chain)By similarity
Disulfide bondi204 – 204Interchain (with C-159 in gamma chain)By similarity
Disulfide bondi208 ↔ 293PROSITE-ProRule annotation
Disulfide bondi218 ↔ 247PROSITE-ProRule annotation
Glycosylationi371 – 3711N-linked (GlcNAc...)Curated
Disulfide bondi401 ↔ 414PROSITE-ProRule annotation

Post-translational modificationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei21 – 222Cleavage; by thrombin; to release fibrinopeptide B

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PaxDbiP02676.
PRIDEiP02676.

PTM databases

UniCarbKBiP02676.

Expressioni

Tissue specificityi

Detected in blood plasma (at protein level).1 Publication

Interactioni

Subunit structurei

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.2 Publications

GO - Molecular functioni

  • glycoprotein binding Source: UniProtKB

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000029826.

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni77 – 793Combined sources
Beta strandi81 – 844Combined sources
Helixi86 – 11227Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEQX-ray3.50B/E/O/R61-468[»]
1JY2X-ray1.40O/R61-116[»]
1JY3X-ray1.60O/R61-116[»]
2Z4EX-ray2.70I/J22-26[»]
3H32X-ray3.60M/N22-26[»]
ProteinModelPortaliP02676.
SMRiP02676. Positions 64-466.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini209 – 465257Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili88 – 2041171 PublicationAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000059561.
HOVERGENiHBG005707.
InParanoidiP02676.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR012290. Fibrinogen_a/b/g_coil_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
SM01212. Fib_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02676-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QFPTDYDEGQ DDRPKVGLGA RGHRPYDKKK EEAPSLRPVP PPISGGGYRA
60 70 80 90 100
RPATATVGQK KVERKPPDAD GCLHADPDLG VLCPTGCKLQ DTLVRQERPI
110 120 130 140 150
RKSIEDLRNT VDSVSRTSSS TFQYITLLKN MWKGRQNQVQ DNENVVNEYS
160 170 180 190 200
SHLEKHQLYI DETVKNNIPT KLRVLRSILE NLRSKIQKLE SDVSTQMEYC
210 220 230 240 250
RTPCTVTCNI PVVSGKECEK IIRNEGETSE MYLIQPEDSS KPYRVYCDMK
260 270 280 290 300
TEKGGWTVIQ NRQDGSVDFG RKWDPYKQGF GNIATNAEGK KYCGVPGEYW
310 320 330 340 350
LGNDRISQLT NMGPTKLLIE MEDWKGDKVT ALYEGFTVQN EANKYQLSVS
360 370 380 390 400
KYKGTAGNAL IEGASQLVGE NRTMTIHNSM FFSTYDRDND GWKTTDPRKQ
410 420 430 440 450
CSKEDGGGWW YNRCHAANPN GRYYWGGAYT WDMAKHGTDD GVVWMNWQGS
460
WYSMKKMSMK IRPYFPEQ
Length:468
Mass (Da):53,340
Last modified:February 1, 1996 - v2
Checksum:i2DED42F443AA4B37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00110 mRNA. Translation: CAA23444.1.
PIRiA03122. FGBOB.
S69115.
UniGeneiBt.23917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00110 mRNA. Translation: CAA23444.1.
PIRiA03122. FGBOB.
S69115.
UniGeneiBt.23917.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEQX-ray3.50B/E/O/R61-468[»]
1JY2X-ray1.40O/R61-116[»]
1JY3X-ray1.60O/R61-116[»]
2Z4EX-ray2.70I/J22-26[»]
3H32X-ray3.60M/N22-26[»]
ProteinModelPortaliP02676.
SMRiP02676. Positions 64-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000029826.

PTM databases

UniCarbKBiP02676.

Proteomic databases

PaxDbiP02676.
PRIDEiP02676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000059561.
HOVERGENiHBG005707.
InParanoidiP02676.

Miscellaneous databases

EvolutionaryTraceiP02676.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR012290. Fibrinogen_a/b/g_coil_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
SM01212. Fib_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The sequence of amino acids at the N-terminal end of bovine fibrinopeptide B."
    Blombaeck B., Doolittle R.F.
    Acta Chem. Scand. 17:1816-1819(1963)
    Cited for: PROTEIN SEQUENCE OF 1-4, PYROGLUTAMATE FORMATION AT GLN-1.
  2. "Amino acid sequence of bovine fibrinopeptides."
    Sjoquist J., Blombaeck B., Wallen P.
    Ark. Kemi 16:425-436(1960)
    Cited for: PROTEIN SEQUENCE OF 5-21, SULFATION AT TYR-6.
  3. "Amino acid sequences of portions of the alpha and beta chains of bovine fibrinogen."
    Martinelli R.A., Inglis A.S., Rubira M.R., Hageman T.C., Hurrell J.G.R., Leach S.J., Scheraga H.A.
    Arch. Biochem. Biophys. 192:27-32(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-53.
  4. "Characterization of a cDNA clone coding for the beta chain of bovine fibrinogen."
    Chung D.W., Rixon M.W., McGillivray R.T.A., Davie E.W.
    Proc. Natl. Acad. Sci. U.S.A. 78:1466-1470(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 44-468.
  5. "Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum."
    Darula Z., Medzihradszky K.F.
    Mol. Cell. Proteomics 8:2515-2526(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-4, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Fibrinogen structure in projection at 18 A resolution. Electron density by co-ordinated cryo-electron microscopy and X-ray crystallography."
    Rao S.P., Poojary M.D., Elliott B.W. Jr., Melanson L.A., Oriel B., Cohen C.
    J. Mol. Biol. 222:89-98(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 61-468, COILED COIL DOMAIN, SUBUNIT.
  7. "Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution."
    Madrazo J., Brown J.H., Litvinovich S., Dominguez R., Yakovlev S., Medved L., Cohen C.
    Proc. Natl. Acad. Sci. U.S.A. 98:11967-11972(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 61-116, SUBUNIT, DISULFIDE BONDS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiFIBB_BOVIN
AccessioniPrimary (citable) accession number: P02676
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.