PPEF1

Protein phosphatase, EF-hand calcium binding domain 1
Identifiers
Symbols	PPEF1 ; PP7; PPEF; PPP7C; PPP7CA
External IDs	OMIM: 300109 MGI: 1097157 HomoloGene: 55960 GeneCards: PPEF1 Gene
EC number	3.1.3.16
Gene ontology Molecular function • protein serine/threonine phosphatase activity • iron ion binding • calcium ion binding • protein binding • manganese ion binding Cellular component • cytosol Biological process • protein dephosphorylation • phototransduction, visible light • rhodopsin mediated signaling pathway • regulation of rhodopsin mediated signaling pathway • detection of stimulus involved in sensory perception Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5475	237178
Ensembl	ENSG00000086717	ENSMUSG00000062168
UniProt	O14829	O35655
RefSeq (mRNA)	NM_006240	NM_011147
RefSeq (protein)	NP_006231	NP_035277
Location (UCSC)	Chr X: 18.68 – 18.83 Mb	Chr X: 160.62 – 160.74 Mb
PubMed search

Serine/threonine-protein phosphatase with EF-hands 1 is an enzyme that in humans is encoded by the PPEF1 gene.^[1][2][3]

Function

This gene encodes a member of the serine/threonine protein phosphatase with EF-hand motif family. The protein contains a protein phosphatase catalytic domain, and at least two EF-hand calcium-binding motifs in its C terminus. Although its substrate(s) is unknown, the encoded protein has been suggested to play a role in specific sensory neuron function and/or development. This gene shares high sequence similarity with the Drosophila retinal degeneration C (rdgC) gene. Several alternatively spliced transcript variants, each encoding a distinct isoform, have been described.^[3]

Interactions

PPEF1 has been shown to interact with Calmodulin 1.^[4]

References

1. Montini E, Rugarli EI, Van de Vosse E, Andolfi G, Mariani M, Puca AA, Consalez GG, den Dunnen JT, Ballabio A, Franco B (Jul 1997). "A novel human serine-threonine phosphatase related to the Drosophila retinal degeneration C (rdgC) gene is selectively expressed in sensory neurons of neural crest origin". Human Molecular Genetics 6 (7): 1137–45. doi:10.1093/hmg/6.7.1137. PMID 9215685.
2. Sherman PM, Sun H, Macke JP, Williams J, Smallwood PM, Nathans J (Oct 1997). "Identification and characterization of a conserved family of protein serine/threonine phosphatases homologous to Drosophila retinal degeneration C". Proceedings of the National Academy of Sciences of the United States of America 94 (21): 11639–44. doi:10.1073/pnas.94.21.11639. PMC 23563. PMID 9326663.
3. "Entrez Gene: PPEF1 protein phosphatase, EF-hand calcium binding domain 1".
4. Kutuzov MA, Solov'eva OV, Andreeva AV, Bennett N (May 2002). "Protein Ser/Thr phosphatases PPEF interact with calmodulin". Biochemical and Biophysical Research Communications 293 (3): 1047–52. doi:10.1016/S0006-291X(02)00338-8. PMID 12051765.

Further reading

• Herzig S, Neumann J (Jan 2000). "Effects of serine/threonine protein phosphatases on ion channels in excitable membranes". Physiological Reviews 80 (1): 173–210. PMID 10617768.
• Huang X, Honkanen RE (Jan 1998). "Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)". The Journal of Biological Chemistry 273 (3): 1462–8. doi:10.1074/jbc.273.3.1462. PMID 9430683.
• Ramulu P, Kennedy M, Xiong WH, Williams J, Cowan M, Blesh D, Yau KW, Hurley JB, Nathans J (Dec 2001). "Normal light response, photoreceptor integrity, and rhodopsin dephosphorylation in mice lacking both protein phosphatases with EF hands (PPEF-1 and PPEF-2)". Molecular and Cellular Biology 21 (24): 8605–14. doi:10.1128/MCB.21.24.8605-8614.2001. PMC 100021. PMID 11713293.
• Kutuzov MA, Solov'eva OV, Andreeva AV, Bennett N (May 2002). "Protein Ser/Thr phosphatases PPEF interact with calmodulin". Biochemical and Biophysical Research Communications 293 (3): 1047–52. doi:10.1016/S0006-291X(02)00338-8. PMID 12051765.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biology 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMC 395752. PMID 14759258.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.