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 27-MAR-2024, entry version 136. 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}; 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; 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; 39947.P48489; -. DR PaxDb; 39947-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 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 CDD; cd07414; MPP_PP1_PPKL; 1. 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 PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF459; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1 ISOZYME 2-RELATED; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF16891; STPPase_N; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. DR Genevisible; P48489; OS. 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 //