Primary Information | |
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BoMiProt ID | Bomi106 |
Protein Name | Fibrinogen beta chain |
Organism | Bos taurus |
Uniprot ID | P02676 |
Milk Fraction | Whey |
Aminoacid Length | 468 |
Molecular Weight | 53340 |
FASTA Sequence | Download |
Gene Name | FGB |
Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
Presence in other biological fluids/tissue/cells | Plasma; seminal plasma |
Protein Function | Participates in blood clotting; sperm protection from proteolysis; acts as agglutination factor to regulate capacitation |
Biochemical Properties | Intact protein is a trinodular, dimeric structure and functionally bivalent; has affinity for plateler surface receptors; it also binds to several plasma proteins; presence of 3 disulfide bonds between α,ß and γ polypeptides that confer structural stability to the molecule; the COOH terminus of the Aα chain is very susceptible to degradation by most proteolytic enzymes; Ca2+ ions affect the conformation of the fibrinngen molecule and may be responsible for the formation of noncovalently bound fibrinogen dimers; 3 calcium binding sites were demonstrated in rat fibrinogen ; irreversibly denatured at 56°C; |
Significance in milk | Regulated clotting of milk; high in cinical and subclinical mastitis |
PTMs | Glycosylated; biantennary oligosaccharides; sialic acids vary in the normal subpopulation of fibrinogen polypeptide as found in humans; sialic acids linkage in monosialylated sugars is either on 90% Manα(l -3) side and 10% on the Manα(1-6) side ; |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P02676|FIBB_BOVIN Fibrinogen beta chain OS=Bos taurus OX=9913 GN=FGB PE=1 SV=2 QFPT*4DYDEGQDDRPKVGLGARGHRPYDKKKEEAPSLRPVPPPISGGGYRARPATATVGQK KVERKPPDADGCLHADPDLGVLCPTGCKLQDTLVRQERPIRKSIEDLRNTVDSVSRTSSS TFQYITLLKNMWKGRQNQVQDNENVVNEYSSHLEKHQLYIDETVKNNIPTKLRVLRSILE NLRSKIQKLESDVSTQMEYCRTPCTVTCNIPVVSGKECEKIIRNEGETSEMYLIQPEDSS KPYRVYCDMKTEKGGWTVIQNRQDGSVDFGRKWDPYKQGFGNIATNAEGKKYCGVPGEYW LGNDRISQLTNMGPTKLLIEMEDWKGDKVTALYEGFTVQNEANKYQLSVSKYKGTAGNAL IEGASQLVGENRTMTIHNSMFFSTYDRDNDGWKTTDPRKQCSKEDGGGWWYNRCHAANPN GRYYWGGAYTWDMAKHGTDDGVVWMNWQGSWYSMKKMSMKIRPYFPEQ |
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 O:64-114 |
CATH | Matched CATH superfamily 1.20.5.50 |
Predicted Disorder Regions | 1-71,396-397 |
DisProt Annotation | |
TM Helix Prediction | No TM helices |
PDB ID | 1deq, 1jy2, 1jy3, 2z4e, 3h32, |
Bibliography | 1. Rego, J. P. A., Crisp, J. M., Moura, A. A., Nouwens, A. S., Li, Y., Venus, B., Corbet, N. J., Corbet, D. H., Burns, B. M., Boe-Hansen, G. B., and McGowan, M. R. (2014) Seminal plasma proteome of electroejaculated Bos indicus bulls. Anim. Reprod. Sci. 148, 1–17. 2. Prunkard, D., Cottingham, I., Garner, I., Bruce, S., Dalrymple, M., Lasser, G., Bishop, P., and Foster, D. (1996) High-level expression of recombinant human fibrinogen in the milk of transgenic mice. Nat. Biotechnol. 14, 867–871. 3. Hermans, J. and McDonagh, J. (1982) Fibrin: Structure and Interactions. Semin. Thromb. Hemost. 8, 11–24. 4. Hessel, B., Makino, M., Iwanaga, S., and Blombäck, B. (1979) Primary structure of human fibrinogen and fibrin. Structural studies on NH2-terminal part of B beta chain. Eur. J. Biochem. 98, 521–534. . 5. Martinez, J., Palascak, J. E., and Kwasniak, D. (1978) Abnormal sialic acid content of the dysfibrinogenemia associated with liver disease. J. Clin. Invest. 61, 535–538. 6. Palascak, J. E. and Martinez, J. (1977) Dysfibrinogenemia Associated with Liver Disease. J. Clin. Invest. 60, 89–95. 7. Gralnick, H. R., Givelber, H., and Abrams, E. (1978) Dysfibrinogenemia Associated with Hepatoma. N. Engl. J. Med. 299, 221–226. 8. Martinez, J., MacDonald, K. A., and Palascak, J. E. (1983) The role of sialic acid in the dysfibrinogenemia associated with liver disease: distribution of sialic acid on the constituent chains. Blood 61, 1196–1202. 9. Marguerie, G., Chagniel, G., and Suscillon, M. (1977) The binding of calcium to bovine fibrinogen. Biochim. Biophys. Acta 490, 94–103. 10. Van Ruijven-Vermeer, I. A. M., Nieuwenhuizen, W., and Nooijen, W. J. (1978) Ca binding of rat fibrinogen and fibrin(ogen) degradation products. FEBS Lett. 93, 177–180 |