ID   PP11_ARATH              Reviewed;         318 AA.
AC   P30366;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1 isozyme 1 {ECO:0000305};
DE            EC=3.1.3.16 {ECO:0000269|PubMed:21222654};
DE   AltName: Full=Type one protein phosphatase 1 {ECO:0000303|PubMed:17368080};
GN   Name=TOPP1 {ECO:0000303|PubMed:17368080};
GN   Synonyms=PP1 {ECO:0000312|EMBL:CAA45611.1};
GN   OrderedLocusNames=At2g29400 {ECO:0000312|Araport:AT2G29400};
GN   ORFNames=F16P2.22 {ECO:0000312|EMBL:AAC95198.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=1314161; DOI=10.1002/j.1460-2075.1992.tb05177.x;
RA   Nitschke K., Fleig U., Schell J., Palme K.;
RT   "Complementation of the cs dis2-11 cell cycle mutant of Schizosaccharomyces
RT   pombe by a protein phosphatase from Arabidopsis thaliana.";
RL   EMBO J. 11:1327-1333(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7678768; DOI=10.1007/bf00019946;
RA   Smith R.D., Walker J.C.;
RT   "Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis
RT   thaliana.";
RL   Plant Mol. Biol. 21:307-316(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17368080; DOI=10.1016/j.tplants.2007.03.003;
RA   Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.;
RT   "Arabidopsis PPP family of serine/threonine phosphatases.";
RL   Trends Plant Sci. 12:169-176(2007).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19329567; DOI=10.1104/pp.109.135335;
RA   Takemiya A., Ariyoshi C., Shimazaki K.;
RT   "Identification and functional characterization of inhibitor-3, a
RT   regulatory subunit of protein phosphatase 1 in plants.";
RL   Plant Physiol. 150:144-156(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP   ACTIVITY REGULATION.
RX   PubMed=21222654; DOI=10.1042/bj20101035;
RA   Templeton G.W., Nimick M., Morrice N., Campbell D., Goudreault M.,
RA   Gingras A.C., Takemiya A., Shimazaki K., Moorhead G.B.;
RT   "Identification and characterization of AtI-2, an Arabidopsis homologue of
RT   an ancient protein phosphatase 1 (PP1) regulatory subunit.";
RL   Biochem. J. 435:73-83(2011).
RN   [9]
RP   FUNCTION, ACTIVITY REGULATION, INTERACTION WITH I-2; SRK2D/SNRK2.2;
RP   SRK2I/SNRK2.3; SRK2A/SNRK2.4; SRK2E/SNRK2.6; SRK2C/SNRK2.8; PYL4; PYL9 AND
RP   PYL11, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=26943172; DOI=10.1371/journal.pgen.1005835;
RA   Hou Y.J., Zhu Y., Wang P., Zhao Y., Xie S., Batelli G., Wang B., Duan C.G.,
RA   Wang X., Xing L., Lei M., Yan J., Zhu X., Zhu J.K.;
RT   "Type one protein phosphatase 1 and its regulatory protein inhibitor 2
RT   negatively regulate ABA signaling.";
RL   PLoS Genet. 12:E1005835-E1005835(2016).
CC   -!- FUNCTION: Serine/threonine-protein phosphatase that possesses
CC       phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro
CC       (PubMed:21222654, PubMed:26943172). Acts as a negative regulator of
CC       abscisic acid (ABA) signaling. In vitro, can dephosphorylate and
CC       inhibit the kinase activity of SRK2E/SNRK2.6, an activator of ABA
CC       signaling. {ECO:0000269|PubMed:21222654, ECO:0000269|PubMed:26943172}.
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         Evidence={ECO:0000269|PubMed:21222654};
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         Evidence={ECO:0000269|PubMed:21222654};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Phosphatase activity is strongly reduced by the
CC       protein phosphatase inhibitor 2 (I-2) (PubMed:21222654,
CC       PubMed:26943172). Phosphatase activity is strongly reduced by PYL11, an
CC       abscisic acid (ABA) receptor (PubMed:26943172).
CC       {ECO:0000269|PubMed:21222654, ECO:0000269|PubMed:26943172}.
CC   -!- SUBUNIT: Interacts with I-2, SRK2D/SNRK2.2, SRK2I/SNRK2.3,
CC       SRK2A/SNRK2.4, SRK2E/SNRK2.6, SRK2C/SNRK2.8, PYL4, PYL9 and PYL11.
CC       {ECO:0000269|PubMed:26943172}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm
CC       {ECO:0000269|PubMed:19329567}.
CC   -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves and flowers.
CC       {ECO:0000269|PubMed:26943172}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant seedlings exhibit hypersensitivity to abscisic
CC       acid (ABA) or salt treatments. {ECO:0000269|PubMed:26943172}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X64328; CAA45611.1; -; mRNA.
DR   EMBL; M93408; AAA32723.1; -; mRNA.
DR   EMBL; AC004561; AAC95198.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08250.1; -; Genomic_DNA.
DR   EMBL; AY080871; AAL87342.1; -; mRNA.
DR   EMBL; AY142593; AAN13162.1; -; mRNA.
DR   PIR; S20882; S20882.
DR   RefSeq; NP_180501.1; NM_128494.5.
DR   AlphaFoldDB; P30366; -.
DR   SMR; P30366; -.
DR   BioGRID; 2839; 1.
DR   IntAct; P30366; 1.
DR   STRING; 3702.P30366; -.
DR   PaxDb; 3702-AT2G29400-1; -.
DR   ProteomicsDB; 250579; -.
DR   EnsemblPlants; AT2G29400.1; AT2G29400.1; AT2G29400.
DR   GeneID; 817489; -.
DR   Gramene; AT2G29400.1; AT2G29400.1; AT2G29400.
DR   KEGG; ath:AT2G29400; -.
DR   Araport; AT2G29400; -.
DR   TAIR; AT2G29400; TOPP1.
DR   eggNOG; KOG0374; Eukaryota.
DR   HOGENOM; CLU_004962_0_0_1; -.
DR   InParanoid; P30366; -.
DR   OMA; RNIARPM; -.
DR   OrthoDB; 5484004at2759; -.
DR   PhylomeDB; P30366; -.
DR   PRO; PR:P30366; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P30366; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; ISS:TAIR.
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; IDA:TAIR.
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:SF499; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1 ISOZYME 1; 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; P30366; AT.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..318
FT                   /note="Serine/threonine-protein phosphatase PP1 isozyme 1"
FT                   /id="PRO_0000058797"
FT   ACT_SITE        138
FT                   /note="Proton donor"
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         79
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   318 AA;  36279 MW;  DAAA11674B148294 CRC64;
     MAEKPAQEQE QKRAMEPAVL DDIIRRLVEF RNTRPGSGKQ VHLSEGEIRQ LCAVSKEIFL
     QQPNLLELEA PIKICGDIHG QYSDLLRLFE YGGFPPEANY LFLGDYVDRG KQSLETICLL
     LAYKIKYPEN FFLLRGNHES ASINRIYGFY DECKRRFNVR LWKIFTDCFN CLPVAALIDD
     RILCMHGGIS PELKSLDQIR NIARPMDIPE SGLVCDLLWS DPSGDVGWGM NDRGVSYTFG
     ADKVAEFLEK HDMDLICRAH QVVEDGYEFF AERQLVTVFS APNYCGEFDN AGAMMSIDES
     LMCSFQILKP SEKKSPFL
//