Search by BoMiProt ID - Bomi249


Primary Information

BoMiProt ID Bomi249
Protein Name Calcium-binding protein p22
Organism Bos taurus
Uniprot IDQ3SYS6
Milk FractionMFGM, Exosome
Ref Sequence ID NP_001069044.1
Aminoacid Length 195
Molecular Weight 22442
FASTA Sequence Download
Gene Name CHP1
Gene ID 512662
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Presence in other biological fluids/tissue/cells expressed in most tissues such as the brain, lung, testis, kidney, spleen, and heart
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
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
PTMs myristoylated
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs required for Ca -induced conformational changes in CHP1 as for other Ca -binding proteins
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.