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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)DescriptionActionsGraphical viewLength
Metal bindingi384CalciumCombined sources1 Publication1
Metal bindingi386CalciumCombined sources1 Publication1
Metal bindingi388Calcium; via carbonyl oxygenCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Metal-binding

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)DescriptionActionsGraphical viewLength
PeptideiPRO_0000009093‹1 – 17Fibrinopeptide B1 PublicationAdd BLAST›17
ChainiPRO_000000909418 – 463Fibrinogen beta chainAdd BLAST446

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5SulfotyrosineBy similarity1
Disulfide bondi69Interchain (with alpha chain)PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi80Interchain (with alpha chain)PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi84Interchain (with gamma chain)PROSITE-ProRule annotation
Disulfide bondi197Interchain (with alpha chain)PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi201Interchain (with gamma chain)PROSITE-ProRule annotation
Disulfide bondi205 ↔ 289PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi215 ↔ 244PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi367N-linked (GlcNAc...)Sequence analysis1 Publication1
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)DescriptionActionsGraphical viewLength
Sitei17 – 18Cleavage; by thrombin; to release fibrinopeptide B2

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiQ02020.
PRIDEiQ02020.

Expressioni

Gene expression databases

BgeeiENSGALG00000009262.

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

1463
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni74 – 76Combined sources3
Beta strandi78 – 81Combined sources4
Helixi85 – 162Combined sources78
Helixi164 – 196Combined sources33
Beta strandi207 – 209Combined sources3
Beta strandi212 – 214Combined sources3
Helixi215 – 220Combined sources6
Beta strandi227 – 231Combined sources5
Beta strandi240 – 245Combined sources6
Helixi248 – 250Combined sources3
Beta strandi253 – 261Combined sources9
Helixi270 – 275Combined sources6
Beta strandi284 – 288Combined sources5
Beta strandi294 – 296Combined sources3
Helixi299 – 306Combined sources8
Beta strandi311 – 318Combined sources8
Beta strandi320 – 322Combined sources3
Beta strandi324 – 334Combined sources11
Helixi337 – 339Combined sources3
Beta strandi343 – 352Combined sources10
Helixi355 – 358Combined sources4
Helixi366 – 369Combined sources4
Helixi397 – 400Combined sources4
Beta strandi408 – 410Combined sources3
Beta strandi412 – 414Combined sources3
Helixi427 – 429Combined sources3
Beta strandi437 – 440Combined sources4
Helixi441 – 444Combined sources4
Beta strandi446 – 448Combined sources3
Beta strandi451 – 459Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ02020.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini206 – 461Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST256

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

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: 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)DescriptionActionsGraphical viewLength
Non-terminal residuei11

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EI3X-ray5.50B/E1-463[»]
1M1JX-ray2.70B/E1-463[»]
DisProtiDP00234.
ProteinModelPortaliQ02020.
SMRiQ02020.
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.

Miscellaneous databases

EvolutionaryTraceiQ02020.

Gene expression databases

BgeeiENSGALG00000009262.

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_CHICK
AccessioniPrimary (citable) accession number: Q02020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 119 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.