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Protein

Fibrinogen beta chain

Gene

FGB

Organism
Gallus gallus (Chicken)
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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi384 – 3841CalciumCombined sources1 Publication
Metal bindingi386 – 3861CalciumCombined sources1 Publication
Metal bindingi388 – 3881Calcium; via carbonyl oxygenCombined sources1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-GGA-114608. Platelet degranulation.
R-GGA-140875. Common Pathway of Fibrin Clot Formation.
R-GGA-216083. Integrin cell surface interactions.
R-GGA-354192. Integrin alphaIIb beta3 signaling.
R-GGA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-GGA-372708. p130Cas linkage to MAPK signaling for integrins.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen beta chain
Cleaved into the following 2 chains:
Gene namesi
Name:FGB
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei‹1 – 17›17Fibrinopeptide B1 PublicationPRO_0000009093Add
BLAST
Chaini18 – 463446Fibrinogen beta chainPRO_0000009094Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51SulfotyrosineBy similarity
Disulfide bondi69 – 69Interchain (with alpha chain)PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi80 – 80Interchain (with alpha chain)PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi84 – 84Interchain (with gamma chain)PROSITE-ProRule annotation
Disulfide bondi197 – 197Interchain (with alpha chain)PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi201 – 201Interchain (with gamma chain)PROSITE-ProRule annotation
Disulfide bondi205 ↔ 289PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi215 ↔ 244PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence analysis1 Publication
Disulfide bondi397 ↔ 410PROSITE-ProRule annotationCombined sources1 Publication

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
Sitei17 – 182Cleavage; by thrombin; to release fibrinopeptide B

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiQ02020.
PRIDEiQ02020.

Expressioni

Gene expression databases

BgeeiENSGALG00000009262.
ExpressionAtlasiQ02020. baseline and differential.

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

STRINGi9031.ENSGALP00000038105.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni74 – 763Combined sources
Beta strandi78 – 814Combined sources
Helixi85 – 16278Combined sources
Helixi164 – 19633Combined sources
Beta strandi207 – 2093Combined sources
Beta strandi212 – 2143Combined sources
Helixi215 – 2206Combined sources
Beta strandi227 – 2315Combined sources
Beta strandi240 – 2456Combined sources
Helixi248 – 2503Combined sources
Beta strandi253 – 2619Combined sources
Helixi270 – 2756Combined sources
Beta strandi284 – 2885Combined sources
Beta strandi294 – 2963Combined sources
Helixi299 – 3068Combined sources
Beta strandi311 – 3188Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi324 – 33411Combined sources
Helixi337 – 3393Combined sources
Beta strandi343 – 35210Combined sources
Helixi355 – 3584Combined sources
Helixi366 – 3694Combined sources
Helixi397 – 4004Combined sources
Beta strandi408 – 4103Combined sources
Beta strandi412 – 4143Combined sources
Helixi427 – 4293Combined sources
Beta strandi437 – 4404Combined sources
Helixi441 – 4444Combined sources
Beta strandi446 – 4483Combined sources
Beta strandi451 – 4599Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EI3X-ray5.50B/E1-463[»]
1M1JX-ray2.70B/E1-463[»]
DisProtiDP00234.
ProteinModelPortaliQ02020.
SMRiQ02020. Positions 62-463.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02020.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini206 – 461256Fibrinogen C-terminalPROSITE-ProRule annotationAdd
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.2 Publications

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000059561.
HOVERGENiHBG005707.
InParanoidiQ02020.
KOiK03904.
PhylomeDBiQ02020.

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: Fragment.

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

Q02020-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ASVEYDNEED SPQIDARAHR PLDKRQEAAP TLRPVAPPIS GTGYQPRPPK
60 70 80 90 100
QDKQAMKKGP IIYPDAGGCK HPLDELGVLC PTGCELQTTL LKQEKTVKPV
110 120 130 140 150
LRDLKDRVAK FSDTSTTMYQ YVNMIDNKLV KTQKQRKDND IILSEYNTEM
160 170 180 190 200
ELHYNYIKDN LDNNIPSSLR VLRAVIDSLH KKIQKLENAI ATQTDYCRSP
210 220 230 240 250
CVASCNIPVV SGRECEDIYR KGGETSEMYI IQPDPFTTPY RVYCDMETDN
260 270 280 290 300
GGWTLIQNRQ DGSVNFGRAW DEYKRGFGNI AKSGGKKYCD TPGEYWLGND
310 320 330 340 350
KISQLTKIGP TKVLIEMEDW NGDKVSALYG GFTIHNEGNK YQLSVSNYKG
360 370 380 390 400
NAGNALMEGA SQLYGENRTM TIHNGMYFST YDRDNDGWLT TDPRKQCSKE
410 420 430 440 450
DGGGWWYNRC HAANPNGRYY WGGTYSWDMA KHGTDDGIVW MNWKGSWYSM
460
KKMSMKIKPY FPD
Length:463
Mass (Da):52,678
Last modified:July 1, 1993 - v1
Checksum:i2044CD49BA79EC7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58514 mRNA. Translation: AAA48770.1.
PIRiA38463.
RefSeqiNP_001161155.1. NM_001167683.1.
UniGeneiGga.41812.

Genome annotation databases

GeneIDi373926.
KEGGigga:373926.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58514 mRNA. Translation: AAA48770.1.
PIRiA38463.
RefSeqiNP_001161155.1. NM_001167683.1.
UniGeneiGga.41812.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EI3X-ray5.50B/E1-463[»]
1M1JX-ray2.70B/E1-463[»]
DisProtiDP00234.
ProteinModelPortaliQ02020.
SMRiQ02020. Positions 62-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000038105.

Proteomic databases

PaxDbiQ02020.
PRIDEiQ02020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi373926.
KEGGigga:373926.

Organism-specific databases

CTDi2244.

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000059561.
HOVERGENiHBG005707.
InParanoidiQ02020.
KOiK03904.
PhylomeDBiQ02020.

Enzyme and pathway databases

ReactomeiR-GGA-114608. Platelet degranulation.
R-GGA-140875. Common Pathway of Fibrin Clot Formation.
R-GGA-216083. Integrin cell surface interactions.
R-GGA-354192. Integrin alphaIIb beta3 signaling.
R-GGA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-GGA-372708. p130Cas linkage to MAPK signaling for integrins.

Miscellaneous databases

EvolutionaryTraceiQ02020.

Gene expression databases

BgeeiENSGALG00000009262.
ExpressionAtlasiQ02020. baseline and differential.

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...

Entry informationi

Entry nameiFIBB_CHICK
AccessioniPrimary (citable) accession number: Q02020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 7, 2016
This is version 116 of the entry and version 1 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.