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PP1_ORYSJ
ID   PP1_ORYSJ               Reviewed;         322 AA.
AC   P48489; Q10NJ4; Q84J82;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1;
DE            EC=3.1.3.16;
GN   OrderedLocusNames=Os03g0268000, LOC_Os03g16110;
GN   ORFNames=OJ1364E02.17, OJA1364E02.7;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=10080713; DOI=10.1023/a:1006152223183;
RA   Chang M., Wang B., Chen X., Wu R.;
RT   "Molecular characterization of catalytic-subunit cDNA sequences encoding
RT   protein phosphatases 1 and 2A and study of their roles in the gibberellin-
RT   dependent Osamy-c expression in rice.";
RL   Plant Mol. Biol. 39:105-115(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP06889.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAP06897.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U31773; AAA74625.1; -; mRNA.
DR   EMBL; AC135208; AAP06889.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC139168; AAP06897.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000009; ABF95164.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF95165.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF95166.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF11583.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS83435.1; -; Genomic_DNA.
DR   EMBL; AK073140; BAG93306.1; -; mRNA.
DR   PIR; T03304; T03304.
DR   AlphaFoldDB; P48489; -.
DR   SMR; P48489; -.
DR   STRING; 4530.OS03T0268000-01; -.
DR   PaxDb; P48489; -.
DR   PRIDE; P48489; -.
DR   EnsemblPlants; Os03t0268000-01; Os03t0268000-01; Os03g0268000.
DR   Gramene; Os03t0268000-01; Os03t0268000-01; Os03g0268000.
DR   eggNOG; KOG0374; Eukaryota.
DR   HOGENOM; CLU_004962_0_0_1; -.
DR   InParanoid; P48489; -.
DR   OMA; EEHEIRY; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; P48489; baseline and differential.
DR   Genevisible; P48489; OS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0016311; P:dephosphorylation; IEA:EnsemblPlants.
DR   GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:EnsemblPlants.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:EnsemblPlants.
DR   GO; GO:0010161; P:red light signaling pathway; IEA:EnsemblPlants.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..322
FT                   /note="Serine/threonine-protein phosphatase PP1"
FT                   /id="PRO_0000058809"
FT   ACT_SITE        136
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        3..11
FT                   /note="AAPGAGGQG -> PRRR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17
FT                   /note="A -> P (in Ref. 1; AAA74625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25..26
FT                   /note="RR -> PP (in Ref. 1; AAA74625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="Q -> H (in Ref. 1; AAA74625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="T -> S (in Ref. 1; AAA74625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="A -> G (in Ref. 1; AAA74625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="V -> M (in Ref. 1; AAA74625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199..201
FT                   /note="SLP -> RLA (in Ref. 1; AAA74625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215..216
FT                   /note="LL -> YF (in Ref. 1; AAA74625)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   322 AA;  36166 MW;  F4C8280134836BE7 CRC64;
     MAAAPGAGGQ GGGGMDAVLL DDIIRRLLEV RTARPGKQVQ LSESEIRQLC TVSREIFLSQ
     PNLLELEAPI KICGDIHGQY SDLLRLFEYG GFPPEANYLF LGDYVDRGKQ SLETICLLLA
     YKIKYPENFF LLRGNHECAS INRIYGFYDE CKRRFNVRLW KVFTDCFNCL PVAALIDDKI
     LCMHGGLSPD LTHLDEIKSL PRPTDVPDTG LLCDLLWSDP GKDVQGWGMN DRGVSYTFGA
     DKVSEFLEKH DLDLICRAHQ VVEDGYEFFA DRQLVTIFSA PNYCGEFDNA GAMMSVDETL
     MCSFQILKPA ERKGKFMASN KM
 
 
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