ID   PPM1H_RAT               Reviewed;         513 AA.
AC   Q5M821;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Protein phosphatase 1H;
DE            EC=3.1.3.16;
GN   Name=Ppm1h;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, 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: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal
CC       for proteasomal degradation. {ECO:0000250|UniProtKB:Q9ULR3}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULR3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9ULR3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Named isoforms=2.;
CC       Name=1;
CC         IsoId=Q5M821-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5M821-2; Sequence=VSP_025123, VSP_025124;
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH88307.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABR03055580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03055960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03056001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03056562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03058099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03058942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC088307; AAH88307.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001258008.1; NM_001271079.2. [Q5M821-1]
DR   AlphaFoldDB; Q5M821; -.
DR   SMR; Q5M821; -.
DR   STRING; 10116.ENSRNOP00000005798; -.
DR   iPTMnet; Q5M821; -.
DR   PhosphoSitePlus; Q5M821; -.
DR   PaxDb; 10116-ENSRNOP00000005798; -.
DR   Ensembl; ENSRNOT00000005798.8; ENSRNOP00000005798.4; ENSRNOG00000004314.8. [Q5M821-1]
DR   Ensembl; ENSRNOT00000066381.2; ENSRNOP00000061506.3; ENSRNOG00000004314.8. [Q5M821-2]
DR   GeneID; 314897; -.
DR   KEGG; rno:314897; -.
DR   AGR; RGD:1309528; -.
DR   CTD; 57460; -.
DR   RGD; 1309528; Ppm1h.
DR   eggNOG; KOG1323; Eukaryota.
DR   GeneTree; ENSGT00940000160095; -.
DR   HOGENOM; CLU_029072_2_0_1; -.
DR   InParanoid; Q5M821; -.
DR   OMA; YKEHIEW; -.
DR   OrthoDB; 1450097at2759; -.
DR   PhylomeDB; Q5M821; -.
DR   TreeFam; TF314700; -.
DR   PRO; PR:Q5M821; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000004314; Expressed in kidney and 20 other cell types or tissues.
DR   ExpressionAtlas; Q5M821; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0004741; F:[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF287; PROTEIN PHOSPHATASE 1H; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; Q5M821; RN.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Methylation; Nucleus;
KW   Phosphoprotein; Protein phosphatase; Reference proteome.
FT   CHAIN           1..513
FT                   /note="Protein phosphatase 1H"
FT                   /id="PRO_0000286605"
FT   DOMAIN          77..506
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          110..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UYC0"
FT   MOD_RES         113
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT   MOD_RES         212
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UYC0"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT   MOD_RES         223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT   VAR_SEQ         1..319
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025123"
FT   VAR_SEQ         320..357
FT                   /note="MQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGW -> MEEFRYKYVP
FT                   WSSEIQQEGGGMRATVSTRKKTASEMIR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025124"
SQ   SEQUENCE   513 AA;  56380 MW;  4CA4B69E70C106FD CRC64;
     MLTRVKSAVA NFMGGIMAGS SGSEHGGSGC GGSDLPLRFP YGRPEFLGLS QDEVECSADH
     IARPILILKE TRRLPWATGY AEVINAGKST HNEDQASCEV LTVKKKVGTI TSTPNRNSKR
     RSSLPNGEGL QLKENSESEG ISCHYWSLFD GHAGSGAAVV ASRLLQHHIT QQLQDIVEIL
     KNSAILPPTC LGEEPESTPA HGRTLTRAAS LRGGVGAPGS PSTPPTRFFT EKKIPHECLV
     IGALESAFKE MDLQIERERS AYNISGGCTA LIVVCLLGKL YVANAGDSRA IIIRNGEIIP
     MSSEFTPETE RQRLQYLAFM QPHLLGNEFT HLEFPRRVQR KELGKKMLYR DFNMTGWAYK
     TIEDDDLKFP LIYGEGKKAR VMATIGVTRG LGDHDLKVHD SNIYIKPFLS SAPEVRVYDL
     SKYEHGADDV LILATDGLWD VLSNEEVAEA ITQFLPNCDP DDPHRYTLAA QDLVMRARGV
     LKDRGWRISN DRLGSGDDIS VYVIPLIHGN KLS
//