Primary Information |
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BoMiProt ID | Bomi249 |
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Protein Name | Calcium-binding protein p22 |
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Organism | Bos taurus |
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Uniprot ID | Q3SYS6 |
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Milk Fraction | MFGM, Exosome |
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Ref Sequence ID | NP_001069044.1 |
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Aminoacid Length | 195 |
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Molecular Weight | 22442 |
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FASTA Sequence |
Download |
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Gene Name | CHP1 |
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Gene ID | 512662 |
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Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | expressed in most tissues such as the brain, lung, testis, kidney, spleen, and heart |
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Protein Function | required for regulation of the plasma membrane Na /H exchanger protein function, to carrier vesicle trafficking and
gene transcription; associates with the microtubule cytoskeleton indirectly via a cytosolic microtubulebinding
factor - regulated mitosis |
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Biochemical Properties | consists of two globular domains, the N-lobe and C-lobe, which are composed of α-
helical structures containing four EF-hand motifs in pairs; contains four potential EF-hand Cα -binding motifs; two
of these bind Cα (EF3 and EF4); binding affinity of CHP1 for Cα increased by ∼40-fold when CHP1 formed a complex
with Na+ /H+ exchanger; Cα -binding affinity is is ∼70nM; two conserved nuclear export signals; binding of Cα may play an important role in maintaining
CHP1 structure |
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PTMs | myristoylated |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | required for Ca -induced conformational changes in CHP1 as for other Ca -binding
proteins |
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Bibliography | 1. Pang, T. et al. (2004) ‘Role of calcineurin B homologous protein in pH regulation by the Na+/H+ exchanger 1: tightly bound Ca2+ ions as important structural elements.’, Biochemistry, 43(12), pp. 3628–36. doi: 10.1021/bi0360004. 2. Timm, S. et al. (1999) ‘The EF-hand Ca 2+ -binding Protein p22 Associates with Microtubules in an N-Myristoylation–dependent Manner’, Molecular Biology of the Cell. Edited by T. Stearns, 10(10), pp. 3473–3488. doi: 10.1091/mbc.10.10.3473. 3. Lin, X. and Barber, D. L. (1996) ‘A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange.’, Proceedings of the National Academy of Sciences, 93(22), pp. 12631–12636. doi: 10.1073/pnas.93.22.12631. 4. Naoe, Y. et al. (2005) ‘Structural Characterization of Calcineurin B Homologous Protein 1’, Journal of Biological Chemistry, 280(37), pp. 32372–32378. doi: 10.1074/jbc.M503390200. 5. Stemmer, P. M. and Klee, C. B. (1994) ‘Dual Calcium Ion Regulation of Calcineurin by Calmodulin and Calcineurin B’, Biochemistry, 33(22), pp. 6859–6866. doi: 10.1021/bi00188a015. |