Primary Information | |
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BoMiProt ID | Bomi111 |
Protein Name | Fibrinogen gamma B |
Organism | Bos taurus |
Uniprot ID | P12799 |
Milk Fraction | Whey |
Ref Sequence ID | NP_776336.1 |
Aminoacid Length | 444 |
Molecular Weight | 50244 |
FASTA Sequence | Download |
Gene Name | FGG |
Gene ID | 280792 |
Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
Protein Function | fibrin polymerization and cross-linking, role in the initiation of fibrinolysis, binding and regulation of factor XIII activity, interactions with platelets and other cells, and role in mediating thrombin binding to fibrin, a thrombin inhibitory function termed ‘antithrombin I |
Biochemical Properties | Aα, Bß, and γ are joined by five symmetrical disulfide bridges; C-terminal region of each fibrinogen or fibrin γ chain contains a single cross-linking site at which factor XIII or XIIIa catalyzes the formation of γ dimers |
Significance in milk | Acute phase proteins; potential marker of mastitis |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
SCOP | Class : All alpha proteins Fold : Left-handed parallel coiled-coil Superfamily : Fibrinogen coiled-coil and central regions Family : Fibrinogen coiled-coil and central regions Domain Name : 1JY2 P:5-48 |
CATH | Matched CATH superfamily 1.20.5.50 |
Predicted Disorder Regions | NA |
DisProt Annotation | |
TM Helix Prediction | 1TMH; (9-27) |
PDB ID | 1DEQ, 1JY2, 1JY3, |
Bibliography | 1. Kanaide, H., & Shainoff, J. R. (1975). Cross-linking of fibrinogen and fibrin by fibrin-stablizing factor (factor XIIIa). The Journal of Laboratory and Clinical Medicine, 85(4), 574–597. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1168234. 2. McKee, P. A., Mattock, P., & Hill, R. L. (1970). Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proceedings of the National Academy of Sciences of the United States of America, 66(3), 738–744. https://doi.org/10.1073/pnas.66.3.738. 3. Siebenlist, K. R., Meh, D. A., & Mosesson, M. W. (2001). Protransglutaminase (factor XIII) mediated crosslinking of fibrinogen and fibrin. Thrombosis and Haemostasis, 86(5), 1221–1228. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/11816711. 4. Mosesson, M. W., Siebenlist, K. R., Hainfeld, J. F., & Wall, J. S. (1995). The covalent structure of factor XIIIa crosslinked fibrinogen fibrils. Journal of Structural Biology, 115(1), 88–101. https://doi.org/10.1006/jsbi.1995.1033. 5. Hoeprich, P. D., & Doolittle, R. F. (1983). Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation. Biochemistry, 22(9), 2049–2055. https://doi.org/10.1021/bi00278a003. 6. Zhang, J. Z., & Redman, C. M. (1992). Identification of B beta chain domains involved in human fibrinogen assembly. The Journal of Biological Chemistry, 267(30), 21727–21732. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1400483. 7. Huang, S., Cao, Z., & Davie, E. W. (1993). The role of amino-terminal disulfide bonds in the structure and assembly of human fibrinogen. Biochemical and Biophysical Research Communications, 190(2), 488–495. https://doi.org/10.1006/bbrc.1993.1074. 8. Blombäck, B., Hessel, B., & Hogg, D. (1976). Disulfide bridges in nh2 -terminal part of human fibrinogen. Thrombosis Research, 8(5), 639–658. https://doi.org/10.1016/0049-3848(76)90245-0. |