|Ref Sequence ID||NP_776409.1|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||Serum;|
|Protein Function||Role in bone formation, opsonization, cellular immunity; modulate the inflammatory potential of basic calcium phosphate crystals associated with various clinical manifestations of inflammation; chondrocyte differentiation ; negative acute phase proteins; free fatty acid transporter; enhances cellular lipid uptake and lipogenesis|
|Biochemical Properties||composed of two polypeptides, the A and B chains, and shares a high degree of amino acid identity with fetuin; mouse AHSG shares 60% and 65% amino acid identity with human AHSG and bovine fetuin; A and B chains of human AHSG, held together by a disulfide bond, are generated by limited proteolysis at Arg-Thr, equivalent position at bovine fetuin sequence is Pro-lie|
|Significance in milk||Abundant in mastitic milk; enhances lipid uptake and lipogenesis in milk|
|PTMs||three potential N-glycosylation sites identified in mouse AHSG are conserved in bovine fetuin, while only two of them are conserved in human AHSG; in humans A-chain of a2HS contains 2 biantennary N- and 2 O-linked glycans; N-glycan has a2-6 NeuAc residues, 4 Gal, αMan, N glycans are partially (~90%) sialylated; O-glycans have partially sialylated 2.5 α2-3-linked NeuAc; 3 0-trisaccharides have the structure NeuAcα2-3Gal01-3GalNAcαl- 0|
| Site(s) of PTM(s) |
|>sp|P12763|FETUA_BOVIN Alpha-2-HS-glycoprotein OS=Bos taurus OX=9913 GN=AHSG PE=1 SV=2|
|Predicted Disorder Regions||(254-285)|
|TM Helix Prediction||No TM helices|
|Bibliography||1. Yang, F., Chen, Z. L., Bergeron, J. M., Cupples, R. L., & Friedrichs, W. E. (1992). Human alpha 2-HS-glycoprotein/bovine fetuin homologue in mice: identification and developmental regulation of the gene. Biochimica et Biophysica Acta, 1130(2), 149–156. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1373325. |
Watzlawick, H., Walsh, M. T., Yoshioka, Y., Schmid, K., & Brossmer, R. (1992). Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases. Biochemistry, 31(48), 12198–12203. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1457416.
3. Strieder-Barboza, C., de Souza, J., Raphael, W., Lock, A. L., & Contreras, G. A. (2018). Fetuin-A: A negative acute-phase protein linked to adipose tissue function in periparturient dairy cows. Journal of Dairy Science, 101(3), 2602–2616. https://doi.org/10.3168/jds.2017-13644.