ID   PPM1F_MOUSE             Reviewed;         452 AA.
AC   Q8CGA0;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Protein phosphatase 1F;
DE            EC=3.1.3.16;
DE   AltName: Full=Ca(2+)/calmodulin-dependent protein kinase phosphatase;
DE            Short=CaM-kinase phosphatase;
DE            Short=CaMKPase;
GN   Name=Ppm1f;
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].
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 MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=30250217; DOI=10.1038/s41436-018-0288-x;
RA   Maddirevula S., Alhebbi H., Alqahtani A., Algoufi T., Alsaif H.S.,
RA   Ibrahim N., Abdulwahab F., Barr M., Alzaidan H., Almehaideb A., AlSasi O.,
RA   Alhashem A., Hussaini H.A., Wali S., Alkuraya F.S.;
RT   "Identification of novel loci for pediatric cholestatic liver disease
RT   defined by KIF12, PPM1F, USP53, LSR, and WDR83OS pathogenic variants.";
RL   Genet. Med. 21:1164-1172(2019).
CC   -!- FUNCTION: Dephosphorylates and concomitantly deactivates CaM-kinase II
CC       activated upon autophosphorylation, and CaM-kinases IV and I activated
CC       upon phosphorylation by CaM-kinase kinase. Promotes apoptosis (By
CC       similarity). {ECO:0000250}.
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: Associates with FEM1B. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the liver.
CC       {ECO:0000269|PubMed:30250217}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AK154192; BAE32429.1; -; mRNA.
DR   EMBL; AK164964; BAE37981.1; -; mRNA.
DR   EMBL; BC042570; AAH42570.1; -; mRNA.
DR   CCDS; CCDS27991.1; -.
DR   RefSeq; NP_789803.1; NM_176833.4.
DR   RefSeq; XP_017172613.1; XM_017317124.1.
DR   AlphaFoldDB; Q8CGA0; -.
DR   SMR; Q8CGA0; -.
DR   BioGRID; 212948; 3.
DR   IntAct; Q8CGA0; 2.
DR   MINT; Q8CGA0; -.
DR   STRING; 10090.ENSMUSP00000027373; -.
DR   GlyGen; Q8CGA0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8CGA0; -.
DR   PhosphoSitePlus; Q8CGA0; -.
DR   SwissPalm; Q8CGA0; -.
DR   EPD; Q8CGA0; -.
DR   MaxQB; Q8CGA0; -.
DR   PaxDb; 10090-ENSMUSP00000027373; -.
DR   PeptideAtlas; Q8CGA0; -.
DR   ProteomicsDB; 289738; -.
DR   Pumba; Q8CGA0; -.
DR   Antibodypedia; 23605; 365 antibodies from 28 providers.
DR   DNASU; 68606; -.
DR   Ensembl; ENSMUST00000027373.12; ENSMUSP00000027373.10; ENSMUSG00000026181.14.
DR   GeneID; 68606; -.
DR   KEGG; mmu:68606; -.
DR   UCSC; uc007yjo.2; mouse.
DR   AGR; MGI:1918464; -.
DR   CTD; 9647; -.
DR   MGI; MGI:1918464; Ppm1f.
DR   VEuPathDB; HostDB:ENSMUSG00000026181; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   GeneTree; ENSGT00940000158884; -.
DR   HOGENOM; CLU_013173_15_0_1; -.
DR   InParanoid; Q8CGA0; -.
DR   OMA; GDICQKP; -.
DR   OrthoDB; 202023at2759; -.
DR   PhylomeDB; Q8CGA0; -.
DR   TreeFam; TF317617; -.
DR   BioGRID-ORCS; 68606; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Ppm1f; mouse.
DR   PRO; PR:Q8CGA0; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q8CGA0; Protein.
DR   Bgee; ENSMUSG00000026181; Expressed in ear vesicle and 225 other cell types or tissues.
DR   ExpressionAtlas; Q8CGA0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; ISS:UniProtKB.
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:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:MGI.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0051224; P:negative regulation of protein transport; ISO:MGI.
DR   GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0045927; P:positive regulation of growth; ISS:UniProtKB.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR   GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF233; PROTEIN PHOSPHATASE 1F; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; Q8CGA0; MM.
PE   1: Evidence at protein level;
KW   Apoptosis; Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..452
FT                   /note="Protein phosphatase 1F"
FT                   /id="PRO_0000057759"
FT   DOMAIN          153..410
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         401
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         452
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49593"
SQ   SEQUENCE   452 AA;  49611 MW;  7C8ED2E597F9D1B8 CRC64;
     MASGAAQNSS QMACDSEIPG FLDAFLQDFP APLSLESPLP WKVPGTVLSQ EEVEAELIEL
     ALGFLGSRNA PPSFAVAVTH EAISQLLQTD LSEFKRLPEQ EEEEEEEEEE KALVTLLDAK
     GLARSFFNCL WKVCSQWQKQ VPLTAQAPQW QWLVSIHAIR NTRRKMEDRH VSLPAFNHLF
     GLSDSVHRAY FAVFDGHGGV DAARYASVHV HTNASHQPEL RTNPAAALKE AFRLTDEMFL
     QKAKRERLQS GTTGVCALIA GAALHVAWLG DSQVILVQQG RVVKLMEPHK PERQDEKARI
     EALGGFVSLM DCWRVNGTLA VSRAIGDVFQ KPYVSGEADA ASRELTGSED YLLLACDGFF
     DVVPHHEVTG LVHGHLLRHK GNGMRIAEEL VAVARDRGSH DNITVMVVFL REPLELLEGG
     VQGTGDAQAD VGSQDLSTGL SELEISNTSQ RS
//