PPEF1

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; OMA:PPEF1 - orthologs
Gene location (Human)
Chr.	X chromosome (human)
End	18,827,921 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	159,518,761 bp
RNA expression pattern
	Top expressed in
	sperm; ; secondary oocyte; ; endothelial cell; ; spinal ganglia; ; testicle; ; left testis; ; right testis; ; C1 segment; ; prefrontal cortex; ; orbitofrontal cortex;
	Top expressed in
	spermatid; ; secondary oocyte; ; zygote; ; testicle; ; primary oocyte; ; spermatocyte; ; spinal ganglia; ; embryo; ; embryo; ; ganglion of neuraxis;
	More reference expression data
	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; protein binding;
Cellular component	cytosol; nucleus;
Biological process	protein dephosphorylation; detection of stimulus involved in sensory perception; regulation of rhodopsin mediated signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	5475
	237178
	ENSG00000086717
	ENSMUSG00000062168
	O14829
	O35655
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_001389620; NM_001389621; NM_001389623; NM_001389624
	NM_011147
NP_006231; NP_689410; NP_689412; NP_001364915; NP_001364922;
	NP_001364923; NP_001364924; NP_001364925; NP_001365310; NP_001365311
	NP_035277
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000086717 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000062168 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: PPEF1 protein phosphatase, EF-hand calcium binding domain 1".
^ 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.

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. S2CID 17770945.
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. S2CID 23783563.
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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

This article on a gene on the human X chromosome and/or its associated protein is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000086717 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid9215685-5] 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.

[pmid9326663-6] 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.

[entrez-7] "Entrez Gene: PPEF1 protein phosphatase, EF-hand calcium binding domain 1".

[pmid12051765-8] 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.

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Function

Interactions

References

Further reading