PPM1E_MOUSE
ID PPM1E_MOUSE Reviewed; 749 AA.
AC Q80TL0; Q5SX30; Q8BGM6; Q8CB81;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
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, Kiaa1072;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, Cerebellum, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-749.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP PROTEIN SEQUENCE OF 198-205, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION.
RX PubMed=23088624; DOI=10.1042/bj20121201;
RA Chida T., Ando M., Matsuki T., Masu Y., Nagaura Y., Takano-Yamamoto T.,
RA Tamura S., Kobayashi T.;
RT "N-Myristoylation is essential for protein phosphatases PPM1A and PPM1B to
RT dephosphorylate their physiological substrates in cells.";
RL Biochem. J. 449:741-749(2013).
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 (By similarity).
CC Dephosphorylates PRKAA2. {ECO:0000250, ECO:0000269|PubMed:23088624}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WY54}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8WY54}. 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. The full-length, minor form, is found in the
CC nucleus. {ECO:0000250|UniProtKB:Q8WY54}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AK036583; BAC29490.1; -; mRNA.
DR EMBL; AK046962; BAC32927.1; -; mRNA.
DR EMBL; AK053696; BAC35479.1; -; mRNA.
DR EMBL; AL596130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122434; BAC65716.1; -; mRNA.
DR CCDS; CCDS25211.1; -.
DR RefSeq; NP_796141.2; NM_177167.4.
DR AlphaFoldDB; Q80TL0; -.
DR SMR; Q80TL0; -.
DR BioGRID; 236046; 3.
DR IntAct; Q80TL0; 1.
DR STRING; 10090.ENSMUSP00000061278; -.
DR iPTMnet; Q80TL0; -.
DR PhosphoSitePlus; Q80TL0; -.
DR MaxQB; Q80TL0; -.
DR PaxDb; Q80TL0; -.
DR PRIDE; Q80TL0; -.
DR ProteomicsDB; 291786; -.
DR Antibodypedia; 18444; 67 antibodies from 16 providers.
DR DNASU; 320472; -.
DR Ensembl; ENSMUST00000055438; ENSMUSP00000061278; ENSMUSG00000046442.
DR GeneID; 320472; -.
DR KEGG; mmu:320472; -.
DR UCSC; uc007kto.1; mouse.
DR CTD; 22843; -.
DR MGI; MGI:2444096; Ppm1e.
DR VEuPathDB; HostDB:ENSMUSG00000046442; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000157884; -.
DR HOGENOM; CLU_013173_15_1_1; -.
DR InParanoid; Q80TL0; -.
DR OMA; SHLRYHY; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q80TL0; -.
DR TreeFam; TF317617; -.
DR BioGRID-ORCS; 320472; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Ppm1e; mouse.
DR PRO; PR:Q80TL0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q80TL0; protein.
DR Bgee; ENSMUSG00000046442; Expressed in lateral septal nucleus and 145 other tissues.
DR ExpressionAtlas; Q80TL0; baseline and differential.
DR Genevisible; Q80TL0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
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; Direct protein sequencing; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Repeat.
FT CHAIN 1..749
FT /note="Protein phosphatase 1E"
FT /id="PRO_0000286821"
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..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..627
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 64..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..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:0007744|PubMed:21183079"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z30"
FT CONFLICT 107
FT /note="H -> D (in Ref. 1; BAC29490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 749 AA; 83419 MW; C59BC6CAC3E268B0 CRC64;
MAGCIPEEKT YRRFLELFLG EFRGPCGGGE PEPEPESEPE PEPEAELVAA EAAEASGEEP
GEDAATVEAT EEGEQDQDPE PEDEAVEEET ATEGEEEEEE EAAAPGHSAV PPPPQPQLPP
LPPLPRPLSE RITREEVEGE SLDLCLQQLY KYNCPSFLAA ALARATSDEV LQSDLSAHCI
PKETDGTEGT VEIETVKLAR SVFSKLHEIC CSWVKDFPLR 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 AVNVSEESEW TENSFQGGQE DGGDDKETHG ECKRPWPQHQ CSAPADLGYE
GRVDSFTDRT SLSPGPQINV LEDPDYLDLT QIEASKPHST QFLPPVEMIG PGAPKKDLNE
LIMEERSVKS SLPERSGAGE PRVSFNLGST GQQICRMENL SPVSSGLENE QFKSRGKTAS
RLYHLRHHYS KRQRGFRFNP KFYSFLSARE PSHKIGISLS SLTRSGKRNK MLRSSLPWRE
NSWEGYSGNV KIRKRNDIPC PDFPWSYKI
