PPM1E_RAT
ID PPM1E_RAT Reviewed; 750 AA.
AC Q80Z30;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein phosphatase 1E;
DE EC=3.1.3.16;
DE AltName: Full=Ca(2+)/calmodulin-dependent protein kinase phosphatase N;
DE Short=CaMKP-N;
DE AltName: Full=CaMKP-nucleus;
DE Short=CaMKN;
DE AltName: Full=Partner of PIX 1;
DE AltName: Full=Partner of PIX-alpha;
DE Short=Partner of PIXA;
GN Name=Ppm1e; Synonyms=Camkn;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RC TISSUE=Brain;
RX PubMed=12807427; DOI=10.1046/j.1471-4159.2003.01817.x;
RA Kitani T., Okuno S., Takeuchi M., Fujisawa H.;
RT "Subcellular distributions of rat CaM kinase phosphatase N and other
RT members of the CaM kinase regulatory system.";
RL J. Neurochem. 86:77-85(2003).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11726284; DOI=10.1093/oxfordjournals.jbchem.a003055;
RA Takeuchi M., Ishida A., Kameshita I., Kitani T., Okuno S., Fujisawa H.;
RT "Identification and characterization of CaMKP-N, nuclear calmodulin-
RT dependent protein kinase phosphatase.";
RL J. Biochem. 130:833-840(2001).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=16269004; DOI=10.1111/j.1471-4159.2005.03540.x;
RA Kitani T., Okuno S., Nakamura Y., Tokuno H., Takeuchi M., Fujisawa H.;
RT "Post-translational excision of the carboxyl-terminal segment of CaM kinase
RT phosphatase N and its cytosolic occurrence in the brain.";
RL J. Neurochem. 96:374-384(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Protein phosphatase that inactivates multifunctional CaM
CC kinases such as CAMK4 and CAMK2. Dephosphorylates and inactivates PAK.
CC May play a role in the inhibition of actin fiber stress breakdown and
CC in morphological changes driven by TNK2/CDC42. Inactivates
CC multifunctional CaM kinases. Dephosphorylates PRKAA2 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:12807427}.
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=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterotrimer. Interacts with PAX1 and ARHGEF6 (or ARHGEF7) (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q80Z30; P05065: Aldoa; NbExp=2; IntAct=EBI-7473061, EBI-522118;
CC Q80Z30; P04797: Gapdh; NbExp=5; IntAct=EBI-7473061, EBI-349219;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11726284,
CC ECO:0000269|PubMed:16269004}. Cytoplasm {ECO:0000269|PubMed:12807427,
CC ECO:0000269|PubMed:16269004}. Note=A truncated form, major form, with
CC the C-terminal part missing, is mostly found in the cytoplasm and a
CC little in the nucleus throughout the central nervous system. Although
CC in some large neurons, the full-length, minor form, is found in the
CC nucleus. {ECO:0000269|PubMed:16269004}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain especially in
CC hippocampus, thalamus and midbrain and to a lower extent in heart and
CC spinal cord. Weakly expressed in testis. A very slow signal is also
CC observed in heart, kidney and liver. {ECO:0000269|PubMed:11726284,
CC ECO:0000269|PubMed:12807427}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AB081729; BAC66021.1; -; mRNA.
DR RefSeq; NP_942068.1; NM_198773.1.
DR AlphaFoldDB; Q80Z30; -.
DR SMR; Q80Z30; -.
DR BioGRID; 262052; 2.
DR IntAct; Q80Z30; 4.
DR MINT; Q80Z30; -.
DR STRING; 10116.ENSRNOP00000003859; -.
DR iPTMnet; Q80Z30; -.
DR PhosphoSitePlus; Q80Z30; -.
DR jPOST; Q80Z30; -.
DR PaxDb; Q80Z30; -.
DR PRIDE; Q80Z30; -.
DR Ensembl; ENSRNOT00000003859; ENSRNOP00000003859; ENSRNOG00000024730.
DR GeneID; 360593; -.
DR KEGG; rno:360593; -.
DR CTD; 22843; -.
DR RGD; 735028; Ppm1e.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000157884; -.
DR HOGENOM; CLU_013173_15_1_1; -.
DR InParanoid; Q80Z30; -.
DR OMA; SHLRYHY; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q80Z30; -.
DR TreeFam; TF317617; -.
DR PRO; PR:Q80Z30; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000024730; Expressed in frontal cortex and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:RGD.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Repeat.
FT CHAIN 1..750
FT /note="Protein phosphatase 1E"
FT /id="PRO_0000286822"
FT REPEAT 31..32
FT /note="1"
FT REPEAT 33..34
FT /note="2"
FT REPEAT 35..36
FT /note="3"
FT REPEAT 37..38
FT /note="4; approximate"
FT REPEAT 39..40
FT /note="5"
FT REPEAT 41..42
FT /note="6"
FT REPEAT 43..44
FT /note="7"
FT DOMAIN 224..485
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 21..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..44
FT /note="7 X 2 AA tandem repeats of P-E"
FT REGION 495..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..103
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TL0"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 750 AA; 83439 MW; AD18B60517D57347 CRC64;
MAGCIPEEKT YRRFLELFLG EFRGPCGGGE PEPEPESEPE PEPEAELVAA EAAEASGEDP
GEDAATVEAA EEGVQDQDPE PEEEAVEEEA AAEGEEEEEE EEAAAPGHSA VPPPQPQLPP
LPPLPRPLSE RITREEVEGE SLDLCLQQLY KYNCPSFLAA ALARATSDEV LQSDLSAHCI
PKETDGTEGT VEIETVKLAR SVFSKLHEIC CNWVKDFPLR RRPQIYYETS IHAIKNMRRK
MEDKHVCIPD FNMLFNLEDQ EEQAYFAVFD GHGGVDAAIY ASVHLHVNLV RQEMFPHDPA
EALCRAFRVT DERFVQKAAR ESLRCGTTGV VTFIRGNMLH VAWVGDSQVM LVRKGQAVEL
MKPHKPDRED EKQRIEALGG CVVWFGAWRV NGSLSVSRAI GDAEHKPYIC GDADSASTVL
DGTEDYLILA CDGFYDTVNP DEAVKVVSDH LKENNGDSSM VAHKLVASAR DAGSSDNITV
IVVFLRDMNK AVNVSEESDW TENSFQGGQE DGGDDKENHG ECKRPWPQHQ CSAPADLGYE
GRVDSFTDRT SLSPGPQINV LEDPDYLDLT QIETSKPHST QFLPPVEMIG PGAPKKAYVN
ELIMEESSVT PSQPERSGAG ELLVSFNLGS TGQQICRMEN LSPVYSGLEN EQFKSPGKRA
SRLYHLRHHY SKRQRGFRFN PKFYSFFSAQ ESSRKIGISL SSLTRSGKRN KMLRSSLPWR
ENSWEGYSGN MAIRKRNNIS CPDLPWDYKI
