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Protein

Fibrinogen gamma-B chain

Gene

FGG

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. 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 via an ITGB3-dependent pathway. 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi343 – 3431CalciumBy similarity
Metal bindingi345 – 3451CalciumBy similarity
Metal bindingi347 – 3471Calcium; via carbonyl oxygenBy similarity
Metal bindingi349 – 3491Calcium; via carbonyl oxygenBy similarity

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 gamma-B chain
Short name:
Gamma'
Gene namesi
Name:FGG
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
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 444420Fibrinogen gamma-B chainPRO_0000009098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 – 32Interchain (with C-33)Combined sources1 Publication
Disulfide bondi33 – 33Interchain (with C-32)Combined sources1 Publication
Disulfide bondi43 – 43Interchain (with C-87 in beta chain)By similarity
Disulfide bondi47 – 47Interchain (with C-67 in alpha chain)By similarity
Glycosylationi76 – 761N-linked (GlcNAc...)Curated
Disulfide bondi159 – 159Interchain (with C-204 in beta chain)By similarity
Disulfide bondi163 – 163Interchain (with C-183 in alpha chain)By similarity
Disulfide bondi177 ↔ 205PROSITE-ProRule annotation
Disulfide bondi351 ↔ 364PROSITE-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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP12799.
PeptideAtlasiP12799.
PRIDEiP12799.

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.3 Publications

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008877.

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 363Combined sources
Turni37 – 393Combined sources
Beta strandi42 – 443Combined sources
Helixi46 – 7126Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEQX-ray3.50C/F/P/S25-432[»]
1JY2X-ray1.40P/S25-72[»]
1JY3X-ray1.60P/S25-72[»]
ProteinModelPortaliP12799.
SMRiP12799. Positions 26-423.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12799.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 415248Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili25 – 1651411 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.2 Publications

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000037127.
HOVERGENiHBG099783.
InParanoidiP12799.
KOiK03905.

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.

P12799-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWSSHPPSV IFYILSLLSS ACLAYVATRD NCCILDERFG SYCPTTCGIA
60 70 80 90 100
DFLNNYQTSV DKDLRTLEGI LYQVENKTSE ARELVKAIQI SYNPDQPSKP
110 120 130 140 150
NNIESATKNS KSMMEEIMKY ETLISTHEST IRFLQEVYNS NSQKIVNLRD
160 170 180 190 200
KVVQLEANCQ EPCQDTVKIH DVTGRDCQDV ANKGAKESGL YFIRPLKAKQ
210 220 230 240 250
FLVYCEIDGS GNGWTVFQKR LDGSLDFKKN WIQYKEGFGH LSPTGTGNTE
260 270 280 290 300
FWLGNEKIHL ISTQSSIPYV LRIQLEDWNG RTSTADYASF KVTGENDKYR
310 320 330 340 350
LTYAYFIGGD AGDAFDGYDF GDDSSDKFFT SHNGMQFSTW DSDNDKYDGN
360 370 380 390 400
CAEQVGIGWW MNKCHAGHLN GVYYQGGTYS KTSTPNGYDN GIIWATWKSR
410 420 430 440
WYSMKKTTMK IIPLNRLAIG EGQQHQLGGA KQVGVEHHVE IEYD
Length:444
Mass (Da):50,244
Last modified:October 1, 1989 - v1
Checksum:i4573C994DE715C49
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti433 – 4364VGVE → AGDV AA sequence (PubMed:11946783).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15556 mRNA. Translation: CAA33562.1.
PIRiA05295.
S05313.
S69116.
RefSeqiNP_776336.1. NM_173911.2.
UniGeneiBt.107063.

Genome annotation databases

GeneIDi280792.
KEGGibta:280792.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15556 mRNA. Translation: CAA33562.1.
PIRiA05295.
S05313.
S69116.
RefSeqiNP_776336.1. NM_173911.2.
UniGeneiBt.107063.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEQX-ray3.50C/F/P/S25-432[»]
1JY2X-ray1.40P/S25-72[»]
1JY3X-ray1.60P/S25-72[»]
ProteinModelPortaliP12799.
SMRiP12799. Positions 26-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008877.

Proteomic databases

PaxDbiP12799.
PeptideAtlasiP12799.
PRIDEiP12799.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280792.
KEGGibta:280792.

Organism-specific databases

CTDi2266.

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000037127.
HOVERGENiHBG099783.
InParanoidiP12799.
KOiK03905.

Miscellaneous databases

EvolutionaryTraceiP12799.

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. "Nucleotide and deduced amino acid sequence of a gamma subunit of bovine fibrinogen."
    Brown W.M., Dziegielewska K.M., Foreman R.C., Saunders N.R.
    Nucleic Acids Res. 17:6397-6397(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Disulfide-linked cyanogen bromide peptides of bovine fibrinogen. II. Isolation and sequence analysis of the chain constituents from the amino terminal region."
    Timpl R., Fietzek P.P., Wachter E., van Delden V.
    Biochim. Biophys. Acta 490:420-429(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-63.
  3. "Amino acid sequence of the carboxy-terminal cyanogen bromide fragment from bovine and human fibrinogen gamma-chains."
    Sharp J.J., Cassman K.G., Doolittle R.F.
    FEBS Lett. 25:334-336(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 409-436.
  4. "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 25-436, SUBUNIT, COILED COIL DOMAIN.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), SUBUNIT, COILED COIL DOMAIN.
  6. "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 25-72, SUBUNIT, DISULFIDE BONDS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiFIBG_BOVIN
AccessioniPrimary (citable) accession number: P12799
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 6, 2016
This is version 114 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.