Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q02020 (FIBB_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibrinogen beta chain

Cleaved into the following 2 chains:

  1. Fibrinopeptide B
  2. Fibrinogen beta chain
Gene names
Name:FGB
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length463 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.

Subunit structure

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 By similarity.

Subcellular location

Secreted.

Domain

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.

Post-translational modification

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.

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide‹1 – 17›17Fibrinopeptide B
PRO_0000009093
Chain18 – 463446Fibrinogen beta chain
PRO_0000009094

Regions

Domain206 – 461256Fibrinogen C-terminal

Sites

Site17 – 182Cleavage; by thrombin; to release fibrinopeptide B

Amino acid modifications

Modified residue51Sulfotyrosine By similarity
Glycosylation3671N-linked (GlcNAc...) Potential
Disulfide bond69Interchain (with alpha chain) By similarity
Disulfide bond80Interchain (with alpha chain) By similarity
Disulfide bond84Interchain (with gamma chain) By similarity
Disulfide bond197Interchain (with alpha chain) By similarity
Disulfide bond201Interchain (with gamma chain) By similarity
Disulfide bond205 ↔ 289 By similarity
Disulfide bond215 ↔ 244 By similarity
Disulfide bond397 ↔ 410 By similarity

Experimental info

Non-terminal residue11

Secondary structure

1 ........................................................... 463
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02020 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 2044CD49BA79EC7B

FASTA46352,678
        10         20         30         40         50         60 
ASVEYDNEED SPQIDARAHR PLDKRQEAAP TLRPVAPPIS GTGYQPRPPK QDKQAMKKGP 

        70         80         90        100        110        120 
IIYPDAGGCK HPLDELGVLC PTGCELQTTL LKQEKTVKPV LRDLKDRVAK FSDTSTTMYQ 

       130        140        150        160        170        180 
YVNMIDNKLV KTQKQRKDND IILSEYNTEM ELHYNYIKDN LDNNIPSSLR VLRAVIDSLH 

       190        200        210        220        230        240 
KKIQKLENAI ATQTDYCRSP CVASCNIPVV SGRECEDIYR KGGETSEMYI IQPDPFTTPY 

       250        260        270        280        290        300 
RVYCDMETDN GGWTLIQNRQ DGSVNFGRAW DEYKRGFGNI AKSGGKKYCD TPGEYWLGND 

       310        320        330        340        350        360 
KISQLTKIGP TKVLIEMEDW NGDKVSALYG GFTIHNEGNK YQLSVSNYKG NAGNALMEGA 

       370        380        390        400        410        420 
SQLYGENRTM TIHNGMYFST YDRDNDGWLT TDPRKQCSKE DGGGWWYNRC HAANPNGRYY 

       430        440        450        460 
WGGTYSWDMA KHGTDDGIVW MNWKGSWYSM KKMSMKIKPY FPD

« Hide

References

[1]"The beta chain of chicken fibrinogen contains an atypical thrombin cleavage site."
Weissbach L., Oddoux C., Procyk R., Grieninger G.
Biochemistry 30:3290-3294(1991) [PubMed: 2009266] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-13 AND 18-39.
[2]"Crystal structure of native chicken fibrinogen at 5.5-A resolution."
Yang Z., Mochalkin I., Veerapandian L., Riley M., Doolittle R.F.
Proc. Natl. Acad. Sci. U.S.A. 97:3907-3912(2000) [PubMed: 10737772] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M58514 mRNA. Translation: AAA48770.1.
IPIIPI00588322.
PIRA38463.
RefSeqNP_001161155.1. NM_001167683.1.
UniGeneGga.41812.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EI3X-ray5.50B/E1-463[»]
1M1JX-ray2.70B/E1-463[»]
ProteinModelPortalQ02020.
SMRQ02020. Positions 62-463.
DisProtDP00234.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ02020.

Proteomic databases

PRIDEQ02020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID373926.
KEGGgga:373926.

Organism-specific databases

CTD2244.

Phylogenomic databases

eggNOGveNOG05157.
GeneTreeENSGT00600000084261.
HOGENOMHBG717207.
HOVERGENHBG005707.
InParanoidQ02020.
OrthoDBEOG4WQ12K.

Family and domain databases

InterProIPR002181. Fibrinogen_a/b/g_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR012290. Fibrinogen_a/b/g_coil_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
Gene3DG3DSA:3.90.215.10. Fibrinogen_a/b/g_C_1. 1 hit.
G3DSA:4.10.530.10. Fibrinogen_a/b/g_C_2. 1 hit.
G3DSA:1.20.5.50. Fibrinogen_a/b/g_coil. 1 hit.
KOK03904.
PfamPF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. Fibrinogen_a/b/g_C. 1 hit.
PROSITEPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFIBB_CHICK
AccessionPrimary (citable) accession number: Q02020
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 16, 2011
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents