PPEF1

Serine/threonine-protein phosphatase with EF-hands 1 is an enzyme that in humans is encoded by the PPEF1 gene.[5][6][7]

PPEF1
Identifiers
Aliases	PPEF1, PP7, PPEF, PPP7C, PPP7CA, protein phosphatase with EF-hand domain 1
External IDs	OMIM: 300109 MGI: 1097157 HomoloGene: 55960 GeneCards: PPEF1
Gene location (Human) Chr. X chromosome (human)[1] Band Xp22.13 Start 18,675,909 bp[1] End 18,827,921 bp[1]
Gene location (Mouse) Chr. X chromosome (mouse)[2] Band X F4|X 73.95 cM Start 160,623,094 bp[2] End 160,735,765 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • iron ion binding • calcium ion binding • protein serine/threonine phosphatase activity • phosphoprotein phosphatase activity • manganese ion binding • hydrolase activity • metal ion binding • GO:0001948 protein binding Cellular component • cytosol • cell nucleus Biological process • protein dephosphorylation • detection of stimulus involved in sensory perception • regulation of rhodopsin mediated signaling pathway Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5475	237178
Ensembl	ENSG00000086717	ENSMUSG00000062168
UniProt	O14829	O35655
RefSeq (mRNA)	NM_006240 NM_152223 NM_152224 NM_152225 NM_152226 NM_001377986 NM_001377993 NM_001377994 NM_001377995 NM_001377996 NM_001378381 NM_001378382	NM_011147
RefSeq (protein)	NP_006231 NP_689410 NP_689412 NP_001364915 NP_001364922 NP_001364923 NP_001364924 NP_001364925 NP_001365310 NP_001365311	NP_035277
Location (UCSC)	Chr X: 18.68 – 18.83 Mb	Chr X: 160.62 – 160.74 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[7]

Interactions

PPEF1 has been shown to interact with Calmodulin 1.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000086717 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000062168 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: PPEF1 protein phosphatase, EF-hand calcium binding domain 1".
8. 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. doi:10.1152/physrev.2000.80.1.173. 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.