PP11_ARATH
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 03-AUG-2022, entry version 162.
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 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.AT2G29400.1; -.
DR PaxDb; P30366; -.
DR PRIDE; P30366; -.
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; locus:2043122; AT2G29400.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P30366; -.
DR OMA; RNIARPM; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P30366; -.
DR PRO; PR:P30366; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P30366; baseline and differential.
DR Genevisible; P30366; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 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 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
