ID   PPE1_MOUSE              Reviewed;         650 AA.
AC   O35655; A2AIC6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Serine/threonine-protein phosphatase with EF-hands 1;
DE            Short=PPEF-1;
DE            EC=3.1.3.16;
DE   AltName: Full=DRES10;
DE   AltName: Full=Protein phosphatase with EF calcium-binding domain;
DE            Short=PPEF;
GN   Name=Ppef1; Synonyms=Dres10, Ppef;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-253.
RX   PubMed=9215685; DOI=10.1093/hmg/6.7.1137;
RA   Montini E., Rugarli E.I., van de Vosse E., Andolfi G., Mariani M.,
RA   Puca A.A., Consales G.G., den Dunnen J.T., Ballabio A., Franco B.;
RT   "A novel human serine-threonine phosphatase related to the Drosophila
RT   retinal degeneration C (rdgC) gene is selectively expressed in sensory
RT   neurons of neural crest origin.";
RL   Hum. Mol. Genet. 6:1137-1145(1997).
CC   -!- FUNCTION: May have a role in the recovery or adaptation response of
CC       photoreceptors. May have a role in diverse sensory neurons and in
CC       development.
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   -!- TISSUE SPECIFICITY: In the embryo it is almost exclusively expressed in
CC       the peripheral nervous system, within sensory neurons of cranial and
CC       dorsal root ganglia. Otherwise found in fetal inner ear and a small
CC       group of neurons in the midbrain/pons junction.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated at 12.3 dpc in dorsal root ganglia
CC       (DRG) and in some sensory cranial ganglia. A slightly decreased
CC       expression could still be detected in sensory ganglia at 16.5 dpc. It
CC       is not known if expression in sensory neurons persists in adult life.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. {ECO:0000305}.
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DR   EMBL; AL732450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL974311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Y08234; CAA69403.1; -; Genomic_DNA.
DR   CCDS; CCDS41200.1; -.
DR   RefSeq; NP_035277.1; NM_011147.1.
DR   AlphaFoldDB; O35655; -.
DR   SMR; O35655; -.
DR   STRING; 10090.ENSMUSP00000071191; -.
DR   iPTMnet; O35655; -.
DR   PhosphoSitePlus; O35655; -.
DR   SwissPalm; O35655; -.
DR   EPD; O35655; -.
DR   MaxQB; O35655; -.
DR   PaxDb; 10090-ENSMUSP00000071191; -.
DR   ProteomicsDB; 291781; -.
DR   Antibodypedia; 24151; 192 antibodies from 23 providers.
DR   DNASU; 237178; -.
DR   Ensembl; ENSMUST00000071204.12; ENSMUSP00000071191.6; ENSMUSG00000062168.13.
DR   GeneID; 237178; -.
DR   KEGG; mmu:237178; -.
DR   UCSC; uc009uto.2; mouse.
DR   AGR; MGI:1097157; -.
DR   CTD; 5475; -.
DR   MGI; MGI:1097157; Ppef1.
DR   VEuPathDB; HostDB:ENSMUSG00000062168; -.
DR   eggNOG; KOG0377; Eukaryota.
DR   GeneTree; ENSGT00940000159830; -.
DR   HOGENOM; CLU_012603_1_0_1; -.
DR   InParanoid; O35655; -.
DR   OMA; SHDNEIN; -.
DR   OrthoDB; 3076469at2759; -.
DR   PhylomeDB; O35655; -.
DR   TreeFam; TF313342; -.
DR   Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   BioGRID-ORCS; 237178; 0 hits in 79 CRISPR screens.
DR   ChiTaRS; Ppef1; mouse.
DR   PRO; PR:O35655; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; O35655; Protein.
DR   Bgee; ENSMUSG00000062168; Expressed in spermatid and 43 other cell types or tissues.
DR   ExpressionAtlas; O35655; baseline and differential.
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; ISS:MGI.
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; 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: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; 3.
DR   SMART; SM00015; IQ; 1.
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; 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..650
FT                   /note="Serine/threonine-protein phosphatase with EF-hands
FT                   1"
FT                   /id="PRO_0000058900"
FT   DOMAIN          16..45
FT                   /note="IQ"
FT   DOMAIN          484..519
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          567..602
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          607..642
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          124..456
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   REGION          315..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        237
FT                   /note="Proton donor"
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         177
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         497
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         499
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         501
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         503
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         508
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="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         582
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         584
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         591
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="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         622
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         624
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         626
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         631
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   650 AA;  75058 MW;  F5B349BE006B60F5 CRC64;
     MGCGTSSKKG NKSKKVIKAA LVIQNWYRRY RARLRVRQHY ALAIFQSIEY SDEQGQMQLS
     SFFSFMLENY TKTNNEDSAL VTRIFDNTRR ESQIKDRDDF LGLIEVPDSY DGPRLQFPLT
     FTDIHILLQA FKQQQILHAH YVLEVLFEAR KVLKQMPNFS HVKTFPAKEI TICGDLHGKL
     DDLMLIFYKN GLPSENNPYV FNGDFVDRGN NSMEILMILL VCFLVYPSDL HLNRGNHEDF
     MMNLRYGFTK EILQKYKLHG RKILQVLEEV YTWLPIGTII DNEILVIHGG ISESTDLNTL
     HQLQRNKMKS VLMPPVLGNQ ETGEKRNKSA SNYVEPRKVE PDKTPSEDLT KQEWEQIVDI
     LWSDPRGKKG CYPNTSRGGG CYFGPDVTSK VLSKNQLKML IRSHECKPDG YEVSHDGKVI
     TVFSASNYYE EGSNRGAYIR LSYGTMPQFF QYQVTSTSCL NPLHQRMNAM ESSAFKILKE
     KMISRKTDLI NAFELRDHSR SGRISLAEWA FSMENILGLN LPWRSLSSHL VTIDSSGSVD
     YMSSFDDIRI EKPTKDMKSN LTETMYRYRS DLKIIFNIID SDQSGLISMD EFRTMWKLFN
     AHYKAHIDDS QIDELASIVD FNKDGNIDFN EFLKAFYVVH KYDKPGTSLA
//