ID PPE1_RAT Reviewed; 640 AA. AC Q3SWT6; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Serine/threonine-protein phosphatase with EF-hands 1; DE Short=PPEF-1; DE EC=3.1.3.16; GN Name=Ppef1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 have a role in the recovery or adaptation response of CC photoreceptors. May have a role in development (By similarity). CC {ECO:0000250}. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Activated by calcium. {ECO:0000250}. 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; BC104696; AAI04697.1; -; mRNA. DR RefSeq; NP_001030107.1; NM_001034935.1. DR AlphaFoldDB; Q3SWT6; -. DR SMR; Q3SWT6; -. DR STRING; 10116.ENSRNOP00000055729; -. DR PhosphoSitePlus; Q3SWT6; -. DR PaxDb; 10116-ENSRNOP00000055729; -. DR Ensembl; ENSRNOT00000058947.5; ENSRNOP00000055729.5; ENSRNOG00000027331.7. DR Ensembl; ENSRNOT00055049628; ENSRNOP00055040829; ENSRNOG00055028661. DR Ensembl; ENSRNOT00060034691; ENSRNOP00060028489; ENSRNOG00060019970. DR Ensembl; ENSRNOT00065021025; ENSRNOP00065016227; ENSRNOG00065012855. DR GeneID; 317498; -. DR KEGG; rno:317498; -. DR AGR; RGD:1562772; -. DR CTD; 5475; -. DR RGD; 1562772; Ppef1. DR eggNOG; KOG0377; Eukaryota. DR GeneTree; ENSGT00940000159830; -. DR InParanoid; Q3SWT6; -. DR PhylomeDB; Q3SWT6; -. DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade. DR PRO; PR:Q3SWT6; -. DR Proteomes; UP000002494; Chromosome X. 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:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:InterPro. DR CDD; cd00051; EFh; 1. DR CDD; cd07420; MPP_RdgC; 1. DR Gene3D; 3.60.21.10; -; 1. 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; 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:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE WITH EF-HANDS 1; 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; 2. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 3. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. PE 2: Evidence at transcript level; KW Calcium; Hydrolase; Magnesium; Manganese; Metal-binding; KW Protein phosphatase; Reference proteome; Repeat. FT CHAIN 1..640 FT /note="Serine/threonine-protein phosphatase with EF-hands FT 1" FT /id="PRO_0000294517" FT DOMAIN 16..45 FT /note="IQ" FT DOMAIN 473..508 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 556..591 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 596..631 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 122..445 FT /note="Catalytic" FT /evidence="ECO:0000250" FT ACT_SITE 235 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 173 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 175 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 202 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 202 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 234 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 286 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 393 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 569 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 571 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 573 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 580 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 609 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 611 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 613 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 615 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 620 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" SQ SEQUENCE 640 AA; 73966 MW; BC841AF1E11F031C CRC64; MGCGSSSKKG KKSEKVVRAA LIIQNWYRRY RARLSARQHY ALAIFQSIEY ADEQGQMQLS SFFSFMLENY TNTHKEDSAL VSRLFENTRL ESKDREEYVG LIDVPDSYDG PRLQFPLTFT DINLLLQAFK QQQTLHAHYV LEVLFEARKI LKQMPNFTRI QTFPAKEITI CGDLHGKLDD LMLIFYKNGL PSEKNPYVFN GDFVDRGNNS MEILMILLVS FLVYPTDLHL NRGNHEDFMM NLRYGFTKEI LQKYKLHGKK ILQVLEELYT WLPIGTIIDN EILVIHGGIS ESTDLNILQQ LQRNKMKSVL MPPMSTNQEC NIKKNKAGPS EQSASEQLTK LEWEQIIDLL WSDPRGKKGC YPNTSRGGGC YFGPDVTSKV LNKNQLKMVI RSHECKPDGY EICHDGKVIT VFSASNYYEE GSNRGAYIRL SYGTSPQFFQ YQVTSTSCLN PLYQRVNAME FSAFRILKER MIARKTDLIN AFELRDHSRT GKISLAQWAF SMESILGLNL PWRSLSSHLV STDSSGSVDY MSSFDDIHIE KPMKDMKSDL IETMYRYRSD LKIIFNIIDT DQSGLISMDE FRTMWKLFNA HYKVHIDDSQ IDELASTMDS NKDGNIDFNE FLRAFYVVHK YETPESPLNK //