Search by BoMiProt ID - Bomi106


Primary Information

BoMiProt ID Bomi106
Protein Name Fibrinogen beta chain
Organism Bos taurus
Uniprot IdP02676
Milk FractionWhey
Amino Acid Lenth 468
Molecular Weight 53340
Fasta Sequence https://www.uniprot.org/uniprot/P02676.fasta
Gene Name FGB
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry 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
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