Search by BoMiProt ID - Bomi292

Primary Information

BoMiProt ID Bomi292
Protein Name Heat shock cognate 71 kDa protein
Organism Bos taurus
Uniprot IDP19120
Milk FractionWhey, 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,
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
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.
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.
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.
4. Samali, A., & Cotter, T. G. (1996). Heat shock proteins increase resistance to apoptosis. Experimental Cell Research, 223(1), 163–170.
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.
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.
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.
8. Chappells, T. G., Konforti, B. B., Schmids, S. L., & Rothmann, J. E. (1987). The ATPase Core of. 262(2), 746–751.