Primary Information
BoMiProt ID	Bomi292
Protein Name	Heat shock cognate 71 kDa protein
Organism	Bos taurus
Uniprot ID	P19120
Milk Fraction	Whey, MFGM, Exosome
Ref Sequence ID	NP_776770.2
Aminoacid Length	650
Molecular Weight	71241
FASTA Sequence	Download
Gene Name	HSPA8
Gene ID	281831
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Protein Function	Constitutively expressed Hsp70 family members are known as heat-shock cognate (Hsc) proteins; bind ATP; molecular chaperone normal unstressed cells; role in modifying antigen presentation; glial-axon transfer proteins; interact directly with fatty acids - interaction may be part of their mode of binding to cell membranes; resist noxious stimuli both in vitro and in vivo; ubiquitous expression of hsp70, hsp90, calreticulin and gp96 in cells essentially ensures that the MHC I presentation pathway remains functional in all nucleated cells; Hsp70 and hsp90 form heteromultimeric complexes in the cytosol with other co-chaperones; Hsp90 and hsp70 are intimately involved in the extrusion of antigens from the endosomes to the cytosol through a putative pore structure;protection of human monocytes from hydrogen peroxideinduced toxicity; guinea pig gastric mucosal cells from ethanol damage
Biochemical Properties	b-sheet structures are the most hydrophobic parts of HSC-70 and thus are likely to be involved in the binding of hydrophobic peptides; changes in resting pHi neither affect the baseline levels of HSP-70 nor alter the ability of heat shock to induce HSP-70 as found in human A-431 cells;
Significance in milk	heat stress proteins in mamary gland
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
SCOP	Class : All beta proteins Fold : Heat shock protein 70kd (HSP70), peptide-binding domain Superfamily : heat shock protein 70kd (hsp70), peptide-binding domain Family : heat shock protein 70kd (hsp70), peptide-binding domain Domain Name : 1YUW A:385-543 Class : Alpha and beta proteins (a/b) Fold : Ribonuclease H-like motif Superfamily : Actin-like ATPases Family : Actin/HSP70 Domain Name : 1YUW A:1-188
CATH	Matched CATH superfamily 3.30.30.30 3.30.420.40 3.90.640.10 2.60.34.10
Predicted Disorder Regions	584-589,615-647
DisProt Annotation
TM Helix Prediction	No TM helices
Significance of PTMs	sensitive to heat stress and mainly responsible for mammary cell protection from heat stress
PDB ID	1ATR, 1ATS, 1BA0, 1BA1, 1BUP, 1HPM, 1HX1, 1KAX, 1KAY, 1KAZ, 1NGA, 1NGB, 1NGC, 1NGD, 1NGE, 1NGF, 1NGG, 1NGH, 1NGI, 1NGJ, 1Q2G, 1QQM, 1QQN, 1QQO, 1YUW, 2BUP, 2QW9, 2QWL, 2QWM, 2QWN, 2QWO, 2QWP, 2QWQ, 2QWR, 3C7N, 3HSC, 4FL9,
Bibliography	1. Ichiyanagi, T., Imai, T., Kajiwara, C., Mizukami, S., Nakai, A., Nakayama, T., & Udono, H. (2010). Essential role of endogenous heat shock protein 90 of dendritic cells in antigen cross-presentation. Journal of Immunology (Baltimore, Md. : 1950), 185(5), 2693–2700. https://doi.org/10.4049/jimmunol.1000821. 2. French, J. B., Zhao, H., An, S., Niessen, S., Deng, Y., Cravatt, B. F., & Benkovic, S. J. (2013). Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome. Proceedings of the National Academy of Sciences of the United States of America, 110(7), 2528–2533. https://doi.org/10.1073/pnas.1300173110 3. Srivastava, P. K., Udono, H., Blachere, N. E., & Li, Z. (1994). Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics, 39(2), 93–98. https://doi.org/10.1007/bf00188611 4. Samali, A., & Cotter, T. G. (1996). Heat shock proteins increase resistance to apoptosis. Experimental Cell Research, 223(1), 163–170. https://doi.org/10.1006/excr.1996.0070. 5. Polla, B. S., Healy, A. M., Wojno, W. C., & Krane, S. M. (1987). Hormone 1 alpha,25-dihydroxyvitamin D3 modulates heat shock response in monocytes. The American Journal of Physiology, 252(6 Pt 1), C640-9. https://doi.org/10.1152/ajpcell.1987.252.6.C640. 6. Shi, Y., & Thomas, J. O. (1992). The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Molecular and Cellular Biology, 12(5), 2186–2192. https://doi.org/10.1128/mcb.12.5.2186. 7. Guidon, P. T., & Hightower, L. E. (1986). Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins. Biochemistry, 25(11), 3231–3239. https://doi.org/10.1021/bi00359a023. 8. Chappells, T. G., Konforti, B. B., Schmids, S. L., & Rothmann, J. E. (1987). The ATPase Core of. 262(2), 746–751.