|Ref Sequence ID||NP_001029390.1|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||Identified primarily in blood and brain|
|Protein Function||member of the cystatin superfamily; identified as major proteins during fetal life; mRNAlevel is down-regulated during the acute phase of experimentally induced inflammation in rat; opsonize cationic macrophage-deactivating molecules;|
|Biochemical Properties||homologous to fetuin-A structurally; Nonspecific hydrophobic interactions were supposed to play a central role in maintaining a hydrophobic core, around which are held together the secondary structural elements and the fluctuating side chains of the protein; potential stabilizing factor for the stability of the molten globule state of BSF is the presence of disulfide bonds|
|Significance in milk||Involved in host defence related responses in bovine milk during an experimentally induced Streptococcus uberis infection|
|PTMs||complex triantennary oligosaccharides; possesses considerable N-glycosylation site heterogeneity; asialo-fetuin contains two variant triantennary oligosaccharides with either Galß(l - 3)^3 or Galß(1 - 4) at one of the terminal branch positions; presence of sialylation heterogeneity among each of these oligosaccharides; contains 12 cysteines and makes 6 disulfide bonds|
| Site(s) of PTM(s) |
|>sp|Q58D62|FETUB_BOVIN Fetuin-B OS=Bos taurus OX=9913 GN=FETUB PE=1 SV=1|
MNVLLLLVLCTLAMGCGATSPPQPAARPSSLLSLDCNSSYVLDIANDILQDINRDRKDGY VLSLNRVSDAREHRQEAGLGSLFYFTLDVLETGCHVLSRTSWKNCEVRIFHESVYGQCKA IFYINKEKRIFYLPAYNCTLRPVSQSAIIMTCPDCPSTSPYDLSNPRFMETATESLAKYN SESPSKQYSLVKITKTSSQWVFGPAYFVEYLIKESPCVKSEGSSCALESPGSVPVGICHG SLGEPQGNQGKIISVTCSFFNSQAPTPRGENATVNQRPANPSKTEELQQQNT*292APT*295NSPTK AVPKGSVQYLPDWDKKREGSQEKDPVETFPVQLDLTTNPQGESLDVSFLFQEPMEEKVVV LPFPSKEQRSAECPGPAQKGYPFILPS
|Predicted Disorder Regions||264-306,366-387|
|TM Helix Prediction||No TM helices|
|Additional Comments||the fetuin family encompasses a series of tightly related proteins that are synthesized mostly in the liver and have been variably designated fetuin in sheep, pig and cow, a2-HS-glycoprotein (AHSG) in human, phosphoprotein of 63 kDa (pp63) in rat, or countertrypin in mouse and gerbil|
|Bibliography||1. Rice, K. G., Rao, N. B. N., & Lee, Y. C. (1990). Large-scale preparation and characterization of N-linked glycopeptides from bovine fetuin. Analytical Biochemistry, 184(2), 249–258. https://doi.org/10.1016/0003-2697(90)90676-Z. |
2. Smolenski, G. A., Broadhurst, M. K., Stelwagen, K., Haigh, B. J., & Wheeler, T. T. (2014). Host defence related responses in bovine milk during an experimentally induced Streptococcus uberis infection. Proteome Science, 12(1). https://doi.org/10.1186/1477-5956-12-19.
3. Olivier, E., Soury, E., Ruminy, P., Husson, A., Parmentier, F., Daveau, M., & Salier, J. P. (2000). Fetuin-B, a second member of the fetuin family in mammals. The Biochemical Journal, 350 Pt 2, 589–597. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/10947975.
4 Wang, C., Lascu, I., & Giartosio, A. (1998). Bovine serum fetuin is unfolded through a molten globule state. Biochemistry, 37(23), 8457–8464. https://doi.org/10.1021/bi9723010.