PPE2_MOUSE
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 03-AUG-2022, entry version 180.
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}.
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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.ENSMUSP00000031359; -.
DR iPTMnet; O35385; -.
DR PhosphoSitePlus; O35385; -.
DR PaxDb; O35385; -.
DR PRIDE; O35385; -.
DR ProteomicsDB; 289877; -.
DR Antibodypedia; 13410; 65 antibodies from 18 providers.
DR DNASU; 19023; -.
DR Ensembl; ENSMUST00000031359; ENSMUSP00000031359; ENSMUSG00000029410.
DR Ensembl; ENSMUST00000201130; ENSMUSP00000144157; ENSMUSG00000029410.
DR GeneID; 19023; -.
DR KEGG; mmu:19023; -.
DR UCSC; uc008yco.2; mouse.
DR CTD; 5470; -.
DR MGI; MGI:1342304; Ppef2.
DR VEuPathDB; HostDB:ENSMUSG00000029410; -.
DR eggNOG; KOG0377; Eukaryota.
DR GeneTree; ENSGT00940000157870; -.
DR InParanoid; O35385; -.
DR OMA; ATHMLTM; -.
DR OrthoDB; 316811at2759; -.
DR PhylomeDB; O35385; -.
DR TreeFam; TF313342; -.
DR BioGRID-ORCS; 19023; 0 hits in 72 CRISPR screens.
DR PRO; PR:O35385; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O35385; protein.
DR Bgee; ENSMUSG00000029410; Expressed in retinal neural layer and 41 other tissues.
DR Genevisible; O35385; MM.
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 Gene3D; 3.60.21.10; -; 2.
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; 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; PS50096; IQ; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
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
