PPM1K_MOUSE
ID PPM1K_MOUSE Reviewed; 372 AA.
AC Q8BXN7;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein phosphatase 1K, mitochondrial;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2C isoform kappa;
DE Short=PP2C-kappa;
DE Flags: Precursor;
GN Name=Ppm1k; Synonyms=Pp2cm;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17374715; DOI=10.1101/gad.1499107;
RA Lu G., Ren S., Korge P., Choi J., Dong Y., Weiss J., Koehler C.,
RA Chen J.-N., Wang Y.;
RT "A novel mitochondrial matrix serine/threonine protein phosphatase
RT regulates the mitochondria permeability transition pore and is essential
RT for cellular survival and development.";
RL Genes Dev. 21:784-796(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17336929; DOI=10.1016/j.bbrc.2007.02.108;
RA Joshi M.A., Jeoung N.H., Popov K.M., Harris R.A.;
RT "Identification of a novel PP2C-type mitochondrial phosphatase.";
RL Biochem. Biophys. Res. Commun. 356:38-44(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Regulates the mitochondrial permeability transition pore and
CC is essential for cellular survival and development.
CC {ECO:0000269|PubMed:17374715}.
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 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:17374715}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the heart, kidney, brain and
CC liver and to a lesser extent in testis, lung, spleen and adipose
CC tissue. Very low amount in muscle (at protein level). Also expressed in
CC the thymus (at protein level) and the diaphragm. Significantly reduced
CC in hypertrophied hearts. {ECO:0000269|PubMed:17336929,
CC ECO:0000269|PubMed:17374715}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AK044610; BAC32001.1; -; mRNA.
DR EMBL; BC092238; AAH92238.1; -; mRNA.
DR CCDS; CCDS20183.1; -.
DR RefSeq; NP_780732.1; NM_175523.4.
DR AlphaFoldDB; Q8BXN7; -.
DR SMR; Q8BXN7; -.
DR STRING; 10090.ENSMUSP00000041395; -.
DR iPTMnet; Q8BXN7; -.
DR PhosphoSitePlus; Q8BXN7; -.
DR MaxQB; Q8BXN7; -.
DR PaxDb; Q8BXN7; -.
DR PRIDE; Q8BXN7; -.
DR ProteomicsDB; 291715; -.
DR Antibodypedia; 14616; 162 antibodies from 28 providers.
DR DNASU; 243382; -.
DR Ensembl; ENSMUST00000042766; ENSMUSP00000041395; ENSMUSG00000037826.
DR GeneID; 243382; -.
DR KEGG; mmu:243382; -.
DR UCSC; uc009cch.1; mouse.
DR CTD; 152926; -.
DR MGI; MGI:2442111; Ppm1k.
DR VEuPathDB; HostDB:ENSMUSG00000037826; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000156633; -.
DR HOGENOM; CLU_013173_1_3_1; -.
DR InParanoid; Q8BXN7; -.
DR OMA; MKGADNC; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q8BXN7; -.
DR TreeFam; TF354344; -.
DR Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR BioGRID-ORCS; 243382; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ppm1k; mouse.
DR PRO; PR:Q8BXN7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BXN7; protein.
DR Bgee; ENSMUSG00000037826; Expressed in retrosplenial region and 216 other tissues.
DR ExpressionAtlas; Q8BXN7; baseline and differential.
DR Genevisible; Q8BXN7; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA: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; IBA:GO_Central.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 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 Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT CHAIN 30..372
FT /note="Protein phosphatase 1K, mitochondrial"
FT /id="PRO_0000278209"
FT DOMAIN 94..346
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 372 AA; 40918 MW; 3749BEB94F211E7A CRC64;
MLSAAFITLL RSGGNQVKKR VLLSSILLQD HRQATPACYF STSEARCSRF DPDGSGQPAT
WDNFGIWDNR IDEPILLPPS IKYGKPIPKI SLENVGCASL IGKRKENEDR FGFAQLTEEV
LYFAVYDGHG GPAAADFCHT HMEKCVMDLL PREKDLETVL TLAFLEIDKA FASYAHLSAD
ASLLTSGTTA TVALLRDGVE LVVASVGDSR ALLCRKGKPM KLTTDHTPER KDEKERIKKF
GGFVAWNSLG QPHVNGRLAM TRSIGDLDLK ASGVIAEPET TRIKLYHADD SFLVLTTDGI
NFMVNSQEIC DFVNQCHDPK EAAHSVTEQA IQYGTEDNST AVVVPFGAWG KYKNSEITFS
FSRSFASSGR WA
