ID   PPM1J_RAT               Reviewed;         504 AA.
AC   Q641Y6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Protein phosphatase 1J;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase 2C isoform zeta;
DE            Short=PP2C-zeta;
GN   Name=Ppm1j; Synonyms=Ppp2cz;
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 MRNA].
RC   TISSUE=Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, 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   -!- 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   -!- SUBUNIT: Interacts with UBE2I/UBC9. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; BC082053; AAH82053.1; -; mRNA.
DR   RefSeq; NP_001005540.1; NM_001005540.1.
DR   AlphaFoldDB; Q641Y6; -.
DR   SMR; Q641Y6; -.
DR   STRING; 10116.ENSRNOP00000016833; -.
DR   CarbonylDB; Q641Y6; -.
DR   iPTMnet; Q641Y6; -.
DR   PhosphoSitePlus; Q641Y6; -.
DR   PaxDb; Q641Y6; -.
DR   PRIDE; Q641Y6; -.
DR   GeneID; 295341; -.
DR   KEGG; rno:295341; -.
DR   UCSC; RGD:1359104; rat.
DR   CTD; 333926; -.
DR   RGD; 1359104; Ppm1j.
DR   eggNOG; KOG1323; Eukaryota.
DR   HOGENOM; CLU_029072_2_0_1; -.
DR   InParanoid; Q641Y6; -.
DR   PhylomeDB; Q641Y6; -.
DR   TreeFam; TF314700; -.
DR   PRO; PR:Q641Y6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; Q641Y6; RN.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; 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; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   PANTHER; PTHR13832; PTHR13832; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Phosphoprotein; Protein phosphatase; Reference proteome.
FT   CHAIN           1..504
FT                   /note="Protein phosphatase 1J"
FT                   /id="PRO_0000289060"
FT   DOMAIN          103..496
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         41
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q149T7"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JR12"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   504 AA;  55211 MW;  66A1BD3CAA69D8D8 CRC64;
     MLNRVRSAVA HLVSSSGTSS QRSKSPDLPK AISPPPGALE TPKSPGTKSG NEIPAPQKTA
     ETPVSFSRPT FLQLSPGGLR RADDHVGRAV QSPPDTGRRL PWSTGYAEVI NAGKSRHNED
     QACCEVVYVE SRRSITGVSR EPSHNQGFSF YYWGLFDGHA GGGAAEMASR LLHRHIREQL
     KDLVEILQDP LPPPLCLPST PGTPGVSSPS QLVSPQSWSP QKEVTHDSLV VGAIENAFQL
     MDEQMARERR GHLVEGGCCA LVVVYLLGKM YVANAGDSRA IIVRNGEIIP MSREFTPETE
     RQRLQLLGFL KPELLGSEFT HLEFPRRVQP KELGQRMLYR DQNMTGWAYK KIELEDLRFP
     LVCGEGKKAR VMATIGVTRG LGDHNLKVCS STLPIKPFLS CFPEVRVYDL TQYEHCPDDV
     LVLGTDGLWD VTNDSEVAAT VDRVLSTYEP NDPSRYTALA QALVLGARGI PRDRGWRLPN
     NKLGSGDDIS VFVIPLGGPG SSYS