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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)DescriptionActionsGraphical viewLength
PeptideiPRO_00000090551 – 21Fibrinopeptide B1 PublicationAdd BLAST21
ChainiPRO_000000905622 – 468Fibrinogen beta chainAdd BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid1 Publication1
Glycosylationi4O-linked (GalNAc...)1 Publication1
Modified residuei6Sulfotyrosine1 Publication1
Disulfide bondi72Interchain (with C-58 in alpha chain)1 Publication
Disulfide bondi83Interchain (with C-71 in alpha chain)1 Publication
Disulfide bondi87Interchain (with C-43 in gamma chain)
Disulfide bondi200Interchain (with C-187 in alpha chain)By similarity
Disulfide bondi204Interchain (with C-159 in gamma chain)By similarity
Disulfide bondi208 ↔ 293PROSITE-ProRule annotation
Disulfide bondi218 ↔ 247PROSITE-ProRule annotation
Glycosylationi371N-linked (GlcNAc...)Curated1
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)DescriptionActionsGraphical viewLength
Sitei21 – 22Cleavage; by thrombin; to release fibrinopeptide B2

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PaxDbiP02676.
PeptideAtlasiP02676.
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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000029826.

Structurei

Secondary structure

1468
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni77 – 79Combined sources3
Beta strandi81 – 84Combined sources4
Helixi86 – 112Combined sources27

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02676.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini209 – 465Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST257

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili88 – 2041 PublicationAdd BLAST117

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

CDDicd00087. FReD. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000029826.

PTM databases

UniCarbKBiP02676.

Proteomic databases

PaxDbiP02676.
PeptideAtlasiP02676.
PRIDEiP02676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

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

Miscellaneous databases

EvolutionaryTraceiP02676.

Family and domain databases

CDDicd00087. FReD. 1 hit.
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...

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: November 30, 2016
This is version 126 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.