Primary Information |
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BoMiProt ID | Bomi5496 |
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Protein Name | Endoplasmic reticulum chaperone BiP /78 kDa glucose-regulated protein/Binding-immunoglobulin protein/Heat shock protein 70 family protein 5/Heat shock protein family A member 5/Immunoglobulin heavy chain-binding protein |
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Organism | Bos taurus |
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Uniprot ID | Q0VCX2 |
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Milk Fraction | Whey |
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Aminoacid Length | 655 |
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Molecular Weight | 72400 |
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FASTA Sequence |
Download |
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Gene Name | HSPA5/GRP78 |
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Gene ID | 415113 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | protein folding and quality control in the ER lumen.correct folding of proteins and degradation of misfolded proteins.key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR).BiP performs its functions with the assistance of ER-localized DnaJ cofactors (ERdjs), which stimulate BiP's ATP-dependent substrate interactions. |
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Biochemical Properties | Monomer and homooligomer.a highly conserved N-terminal nucleotide-binding domain (NBD), a substrate-binding domain (SBD) composed of eight β-strands with a helical lid, and a linker between them that controls the allosteric interaction between these two domains. |
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Significance in milk | assist in the refolding of proteins during periparturient phase in which the dairy cows face with ER stress. |
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PTMs | Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation |
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Predicted Disorder Regions | 2 predicted disordered segments;(583-586), 614th residue, (639-655) |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | AMPylation at Thr-519 by FICD inactivates the chaperone activity.interdomain linker regulates the chaperone activity. |
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Bibliography | 1.Gessner DK, Schlegel G, Ringseis R, Schwarz FJ, Eder K. Up-regulation of endoplasmic reticulum stress induced genes of the unfolded protein response in the liver of periparturient dairy cows. BMC Vet Res. 2014 Feb 20;10:46. doi: 10.1186/1746-6148-10-46. PMID: 24555446; PMCID: PMC3936700. 2.Pobre KFR, Poet GJ, Hendershot LM. The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends. J Biol Chem. 2019 Feb 8;294(6):2098-2108. doi: 10.1074/jbc.REV118.002804. Epub 2018 Dec 18. PMID: 30563838; PMCID: PMC6369273. |