| Identification |
|---|
| HMDB Protein ID
| HMDBP13517 |
| Secondary Accession Numbers
| None |
| Name
| Fibrinogen gamma-B chain |
| Synonyms
|
- Gamma'
|
| Gene Name
| FGG |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| 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. |
| Pathways
|
- Complement and coagulation cascades
- Coronavirus disease - COVID-19
- Neutrophil extracellular trap formation
- Platelet activation
- Staphylococcus aureus infection
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| cell-matrix adhesion |
| protein polymerization |
| platelet aggregation |
| blood coagulation, fibrin clot formation |
| Cellular Component |
| extracellular space |
| collagen-containing extracellular matrix |
| fibrinogen complex |
| Molecular Function |
| metal ion binding |
| receptor binding |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 444 |
| Molecular Weight
| 50243.745 |
| Theoretical pI
| 5.83 |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P12799 |
| UniProtKB/Swiss-Prot Entry Name
| FIBG_BOVIN |
| PDB IDs
|
|
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Brown WM, Dziegielewska KM, Foreman RC, Saunders NR: Nucleotide and deduced amino acid sequence of a gamma subunit of bovine fibrinogen. Nucleic Acids Res. 1989 Aug 11;17(15):6397. doi: 10.1093/nar/17.15.6397. [PubMed:2771651 ]
- Timpl R, Fietzek PP, Wachter E, Van Delden V: Disulfide-linked cyanogen bromide peptides of bovine fibrinogen. II. Isolation and sequence analysis of the chain constituents from the amino terminal region. Biochim Biophys Acta. 1977 Feb 22;490(2):420-9. doi: 10.1016/0005-2795(77)90017-4. [PubMed:836881 ]
- Sharp JJ, Cassman KG, Doolittle RF: Amino acid sequence of the carboxy-terminal cyanogen bromide fragment from bovine and human fibrinogen gamma-chains. FEBS Lett. 1972 Sep 15;25(2):334-336. doi: 10.1016/0014-5793(72)80517-9. [PubMed:11946783 ]
- Brown JH, Volkmann N, Jun G, Henschen-Edman AH, Cohen C: The crystal structure of modified bovine fibrinogen. Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):85-90. doi: 10.1073/pnas.97.1.85. [PubMed:10618375 ]
- Madrazo J, Brown JH, Litvinovich S, Dominguez R, Yakovlev S, Medved L, Cohen C: Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution. Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):11967-72. doi: 10.1073/pnas.211439798. [PubMed:11593005 ]
|
