Primary Information
BoMiProt ID	Bomi70
Protein Name	Peptidyl-prolyl cis-trans isomerase A
Organism	Bos taurus
Uniprot ID	P62935
Milk Fraction	Whey, MFGM, Exosome
Ref Sequence ID	XP_005205627.1
Aminoacid Length	164
Molecular Weight	17869
FASTA Sequence	Download
Gene Name	PPIA
Gene ID	281418
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Protein Function	possess chaperone activity and fold proteins into active configuration by catalyzing slow cis/trans isomerization on proline- peptide bonds; play an important role in pathogenesis; play an important role in protein folding , reactivation of denaturated proteins , protein synthesis de novo and restoration of polypeptide active structures; take part in such cell processes as signal transduction, protein secretion , RNA processing , apoptosis , cell cycle control , development regulation , photosynthesis and host-pathogen interaction
Biochemical Properties	conservative and abundant among Pro- and Eukaryotes; part of large chaperone complexes [, transmembrane channels responsible for Ca 2+ and other ions transport
Linking IDs	Bomi70
Bibliography	1. Patterson, C. E., Schaub, T., Coleman, E. J., & Davis, E. C. (2000). Developmental regulation of FKBP65. An ER-localized extracellular matrix binding-protein. Molecular Biology of the Cell, 11(11), 3925–3935. https://doi.org/10.1091/mbc.11.11.3925. 2. Shen, M., Stukenberg, P. T., Kirschner, M. W., & Lu, K. P. (1998). The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes & Development, 12(5), 706–720. https://doi.org/10.1101/gad.12.5.706. 3. Lu, K. P., Hanes, S. D., & Hunter, T. (1996). A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature, 380(6574), 544–547. https://doi.org/10.1038/380544a0. 4. Yurchenko, V., Zybarth, G., O’Connor, M., Dai, W. W., Franchin, G., Hao, T., … Bukrinsky, M. (2002). Active site residues of cyclophilin A are crucial for its signaling activity via CD147. The Journal of Biological Chemistry, 277(25), 22959–22965. https://doi.org/10.1074/jbc.M201593200. 5. Marx, S. O., Reiken, S., Hisamatsu, Y., Jayaraman, T., Burkhoff, D., Rosemblit, N., & Marks, A. R. (2000). PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell, 101(4), 365–376. https://doi.org/10.1016/s0092-8674(00)80847-8. 6. Nicolli, A., Basso, E., Petronilli, V., Wenger, R. M., & Bernardi, P. (1996). Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, and cyclosporin A-sensitive channel. The Journal of Biological Chemistry, 271(4), 2185–2192. https://doi.org/10.1074/jbc.271.4.2185. 7. Ng, K. K. S., & Weis, W. I. (1998). Coupling of prolyl peptide bond isomerization and Ca2+ binding in a C- type mannose-binding protein. Biochemistry, 37(51), 17977–17989. https://doi.org/10.1021/bi9819733. 8. Zhou, X. Z., Kops, O., Werner, A., Lu, P. J., Shen, M., Stoller, G., … Lu, K. P. (2000). Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins. Molecular Cell, 6(4), 873–883. https://doi.org/10.1016/s1097-2765(05)00083-3.
Protein Function	possess chaperone activity and fold proteins into active configuration by catalyzing slow cis/trans isomerization on proline- peptide bonds; play an important role in pathogenesis; play an important role in protein folding , reactivation of denaturated proteins , protein synthesis de novo and restoration of polypeptide active structures; take part in such cell processes as signal transduction, protein secretion , RNA processing , apoptosis , cell cycle control , development regulation , photosynthesis and host-pathogen interaction
Biochemical Properties	conservative and abundant among Pro- and Eukaryotes; part of large chaperone complexes [, transmembrane channels responsible for Ca 2+ and other ions transport
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	NA
DisProt Annotation
TM Helix Prediction	No TM helices
Linking IDs
Bibliography	1. Patterson, C. E., Schaub, T., Coleman, E. J., & Davis, E. C. (2000). Developmental regulation of FKBP65. An ER-localized extracellular matrix binding-protein. Molecular Biology of the Cell, 11(11), 3925–3935. https://doi.org/10.1091/mbc.11.11.3925. 2. Shen, M., Stukenberg, P. T., Kirschner, M. W., & Lu, K. P. (1998). The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Genes & Development, 12(5), 706–720. https://doi.org/10.1101/gad.12.5.706. 3. Lu, K. P., Hanes, S. D., & Hunter, T. (1996). A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature, 380(6574), 544–547. https://doi.org/10.1038/380544a0. 4. Yurchenko, V., Zybarth, G., O’Connor, M., Dai, W. W., Franchin, G., Hao, T., … Bukrinsky, M. (2002). Active site residues of cyclophilin A are crucial for its signaling activity via CD147. The Journal of Biological Chemistry, 277(25), 22959–22965. https://doi.org/10.1074/jbc.M201593200. 5. Marx, S. O., Reiken, S., Hisamatsu, Y., Jayaraman, T., Burkhoff, D., Rosemblit, N., & Marks, A. R. (2000). PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell, 101(4), 365–376. https://doi.org/10.1016/s0092-8674(00)80847-8. 6. Nicolli, A., Basso, E., Petronilli, V., Wenger, R. M., & Bernardi, P. (1996). Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, and cyclosporin A-sensitive channel. The Journal of Biological Chemistry, 271(4), 2185–2192. https://doi.org/10.1074/jbc.271.4.2185. 7. Ng, K. K. S., & Weis, W. I. (1998). Coupling of prolyl peptide bond isomerization and Ca2+ binding in a C- type mannose-binding protein. Biochemistry, 37(51), 17977–17989. https://doi.org/10.1021/bi9819733. 8. Zhou, X. Z., Kops, O., Werner, A., Lu, P. J., Shen, M., Stoller, G., … Lu, K. P. (2000). Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins. Molecular Cell, 6(4), 873–883. https://doi.org/10.1016/s1097-2765(05)00083-3.