Primary Information |
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| BoMiProt ID | Bomi110 |
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| Protein Name | Alpha-2-HS-glycoprotein |
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| Organism | Bos taurus |
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| Uniprot Id | P12763 |
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| Milk Fraction | Whey |
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| Ref Sequence Id | NP_776409.1 |
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| Amino Acid Lenth | 359 |
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| Molecular Weight | 38419 |
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| Fasta Sequence | https://www.uniprot.org/uniprot/P12763.fasta |
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| Gene Name | AHSG |
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| Gene Id | 280988 |
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| Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondry Information |
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| Presence in other biological fluids/tissue/cells | Serum; |
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| 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 |
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| 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 |
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| Significance in milk | Abundant in mastitic milk; enhances lipid uptake and lipogenesis in milk |
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| 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 |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P12763|FETUA_BOVIN Alpha-2-HS-glycoprotein OS=Bos taurus OX=9913 GN=AHSG PE=1 SV=2
MKSFVLLFCLAQLWGCHSIPLDPVAGYKEPACDDPDTEQAALAAVDYINKHLPRGYKHTLNQIDSVKVWPRRPTGEVYDIEIDTLETTCHVLDPTPLAN*99CSVRQQTQHAVEGDCDIHVLKQDGQFSVLFTKCDSSPDSAEDVRKLCPDCPLLAPLN*156DSRVVHAVEVALATFNAESN*176GSYLQLVEISRAQFVPLPVSVSVEFAVAATDCIAKEVVDPTKCNLLAEKQYGFCKGSVIQKALGGEDVRVTCTLFQTQPVIPQPQPDGAEAEAPS*271AVPDAAGPT*280PS*282AAGPPVASVVVGPS*296VVAVPLPLHRAHYDLRHTFSGVAS*320VES*323SS*325GEAFHVGKT*334PIVGQPS*341IPGGPVRLC
PGRIRYFKI
|
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| 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. |
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