PPE1_MOUSE
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 03-AUG-2022, entry version 166.
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 EPD; O35655; -.
DR MaxQB; O35655; -.
DR PaxDb; O35655; -.
DR PRIDE; O35655; -.
DR ProteomicsDB; 291781; -.
DR Antibodypedia; 24151; 168 antibodies from 23 providers.
DR DNASU; 237178; -.
DR Ensembl; ENSMUST00000071204; ENSMUSP00000071191; ENSMUSG00000062168.
DR GeneID; 237178; -.
DR KEGG; mmu:237178; -.
DR UCSC; uc009uto.2; mouse.
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; 316811at2759; -.
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 74 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 41 other 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 Gene3D; 3.60.21.10; -; 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 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; SSF47473; 1.
DR SUPFAM; SSF56300; SSF56300; 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
