ID PPE2_MOUSE Reviewed; 757 AA. AC O35385; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 188. DE RecName: Full=Serine/threonine-protein phosphatase with EF-hands 2; DE Short=PPEF-2; DE EC=3.1.3.16; GN Name=Ppef2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Eye; RX PubMed=9326663; DOI=10.1073/pnas.94.21.11639; RA Sherman P.M., Sun H., Macke J.P., Williams J., Smallwood P.M., Nathans J.; RT "Identification and characterization of a conserved family of protein RT serine/threonine phosphatases homologous to Drosophila retinal degeneration RT C."; RL Proc. Natl. Acad. Sci. U.S.A. 94:11639-11644(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May play a role in phototransduction. May dephosphorylate CC photoactivated rhodopsin. May function as a calcium sensing regulator CC of ionic currents, energy production or synaptic transmission. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Activated by calcium. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Detected in retina, more specifically in CC photoreceptors. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF023458; AAB82798.1; -; mRNA. DR EMBL; BC027049; AAH27049.1; -; mRNA. DR CCDS; CCDS39151.1; -. DR RefSeq; NP_035278.1; NM_011148.3. DR RefSeq; XP_006534880.1; XM_006534817.2. DR AlphaFoldDB; O35385; -. DR SMR; O35385; -. DR BioGRID; 202323; 1. DR STRING; 10090.ENSMUSP00000144157; -. DR GlyGen; O35385; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O35385; -. DR PhosphoSitePlus; O35385; -. DR PaxDb; 10090-ENSMUSP00000031359; -. DR ProteomicsDB; 289877; -. DR Antibodypedia; 13410; 70 antibodies from 18 providers. DR DNASU; 19023; -. DR Ensembl; ENSMUST00000031359.9; ENSMUSP00000031359.9; ENSMUSG00000029410.12. DR Ensembl; ENSMUST00000201130.4; ENSMUSP00000144157.2; ENSMUSG00000029410.12. DR GeneID; 19023; -. DR KEGG; mmu:19023; -. DR UCSC; uc008yco.2; mouse. DR AGR; MGI:1342304; -. DR CTD; 5470; -. DR MGI; MGI:1342304; Ppef2. DR VEuPathDB; HostDB:ENSMUSG00000029410; -. DR eggNOG; KOG0377; Eukaryota. DR GeneTree; ENSGT00940000157870; -. DR InParanoid; O35385; -. DR OMA; CRENKVR; -. DR OrthoDB; 3076469at2759; -. DR PhylomeDB; O35385; -. DR TreeFam; TF313342; -. DR BioGRID-ORCS; 19023; 0 hits in 77 CRISPR screens. DR PRO; PR:O35385; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; O35385; Protein. DR Bgee; ENSMUSG00000029410; Expressed in retinal neural layer and 43 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI. DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:MGI. DR GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:InterPro. DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:MGI. DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISO:MGI. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd00051; EFh; 1. DR CDD; cd07420; MPP_RdgC; 1. DR Gene3D; 3.60.21.10; -; 2. DR Gene3D; 1.10.238.10; EF-hand; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR013235; PPP_dom. DR InterPro; IPR012008; Ser/Thr-Pase_EF-hand_contain. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1. DR PANTHER; PTHR45668:SF2; SERINE_THREONINE-PROTEIN PHOSPHATASE WITH EF-HANDS 2; 1. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF08321; PPP5; 1. DR PIRSF; PIRSF000912; PPEF; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00054; EFh; 3. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00018; EF_HAND_1; 3. DR PROSITE; PS50222; EF_HAND_2; 3. DR PROSITE; PS50096; IQ; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. DR Genevisible; O35385; MM. PE 2: Evidence at transcript level; KW Calcium; Hydrolase; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome; Repeat; Sensory transduction; Vision. FT CHAIN 1..757 FT /note="Serine/threonine-protein phosphatase with EF-hands FT 2" FT /id="PRO_0000058902" FT DOMAIN 21..46 FT /note="IQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 572..607 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 656..691 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 696..731 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 128..544 FT /note="Catalytic" FT REGION 318..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 318..336 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 241 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 179 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 181 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 208 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 208 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 240 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 292 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 492 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 585 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 587 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 589 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 596 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 669 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 671 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 673 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 680 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 709 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 711 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 713 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 715 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 720 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" SQ SEQUENCE 757 AA; 86645 MW; 821B3D1061AC00C8 CRC64; MGSSSSTQHH FAFQNAEKAF KAAALIQRWY RRYMARLEMR RRCTWNIFQS IEYAGQQDQV KLHEFFSYLV DHFTPSSHHE RDFLNRMFTE ERFAQDVETE EGGDFESIEV PDSYTGPRLS FPLLPDHATA LVEAFRLRQQ LHARYVLNLL YETRKHLAQL PNINRVSTCY SEEVTVCGDL HGQLDDLIFI FYKNGLPSPE RAYVFNGDFV DRGKDSVEVL MVLFAFMLVY PKEFHLNRGN HEDHLVNLRY GFTKEVMHKY KIHGKKILRT LQDVFCWLPL ATLVDEKVLV LHGGVSDKTD LELLAKLDRH KIVSTMRCKT RKESENREEQ KRKDNQTSSG QKPTPWFLPQ SRSLPSSPFH LGSGFKAYKA GRSCSIPCGS PNSKELSRRG QVRRSVDLEL EQCRQQAGFL GIREKGESLP LAPDADCVAD GGGVLEPTPE EWKQVVDILW SDPAAQEGCK ANAVRGGGCY FGPDVTERLM EKYKLQLLIR SHECKPEGYE FCHNRKVLTI FSASNYYEVG SNRGAYVKLG PALTPHIVQY QANKATHRLT MRQRISRVEE SALRALRQKL FAHSSDLLVE FRKRDPDESG VITLSDWATA VESVLHLGLP WRMLRPQLVN SSADNVLEYR SWLDSLAKEQ LSRENIQSSL LEKLYRNRSN LETIFRIIDS DHSGFISLDE FRQTWKLFSS HMSIDITDDG ICDLARSIDF NKDGHIDINE FLEAFRLVEQ SCLEGHASAC LQSTDTAESG HSSPGPC //