PP14_ARATH
ID PP14_ARATH Reviewed; 321 AA.
AC P48484; Q147H5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein phosphatase PP1 isozyme 4 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:21222654};
DE AltName: Full=Type one protein phosphatase 4 {ECO:0000303|PubMed:17368080};
GN Name=TOPP4 {ECO:0000303|PubMed:17368080};
GN OrderedLocusNames=At2g39840 {ECO:0000312|Araport:AT2G39840};
GN ORFNames=T5I7.14 {ECO:0000312|EMBL:AAB87136.1};
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].
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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP FUNCTION, INTERACTION WITH RGA AND GAI, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25010794; DOI=10.1371/journal.pgen.1004464;
RA Qin Q., Wang W., Guo X., Yue J., Huang Y., Xu X., Li J., Hou S.;
RT "Arabidopsis DELLA protein degradation is controlled by a type-one protein
RT phosphatase, TOPP4.";
RL PLoS Genet. 10:E1004464-E1004464(2014).
RN [11]
RP FUNCTION, INTERACTION WITH THE AUXIN EFFLUX CARRIER PIN1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25560878; DOI=10.1104/pp.114.249904;
RA Guo X., Qin Q., Yan J., Niu Y., Huang B., Guan L., Li Y., Ren D., Li J.,
RA Hou S.;
RT "TYPE-ONE PROTEIN PHOSPHATASE4 regulates pavement cell interdigitation by
RT modulating PIN-FORMED1 polarity and trafficking in Arabidopsis.";
RL Plant Physiol. 167:1058-1075(2015).
RN [12]
RP FUNCTION, INTERACTION WITH PIF3 AND PIF5, AND SUBCELLULAR LOCATION.
RX PubMed=26704640; DOI=10.1104/pp.15.01729;
RA Yue J., Qin Q., Meng S., Jing H., Gou X., Li J., Hou S.;
RT "TOPP4 regulates the stability of PHYTOCHROME INTERACTING FACTOR5 during
RT photomorphogenesis in Arabidopsis.";
RL Plant Physiol. 170:1381-1397(2016).
CC -!- FUNCTION: Serine/threonine-protein phosphatase that possesses
CC phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro
CC (PubMed:21222654). Acts as positive regulator in the gibberellin (GA)
CC signaling pathway to regulate plant growth and development. Promotes
CC the GA-induced and proteasomal-dependent degradation of the DELLA
CC proteins RGA and GAI by directly binding and dephosphorylating these
CC proteins (PubMed:25010794). Involved in the regulation of phytochrome B
CC (phyB) signaling pathway that controls photomorphogenesis. Promotes the
CC proteasomal-dependent degradation of PIF5 factor by directly binding
CC and dephosphorylating this protein (PubMed:26704640). Involved in the
CC regulation of pavement cell (PC) interdigitation by modulating the
CC auxin efflux carrier PIN1 polarity and endocytic trafficking. Regulates
CC PIN1 polar targeting through direct binding and dephosphorylation. Acts
CC antagonistically with PID in regulating PC development
CC (PubMed:25560878). {ECO:0000269|PubMed:21222654,
CC ECO:0000269|PubMed:25010794, ECO:0000269|PubMed:25560878,
CC ECO:0000269|PubMed:26704640}.
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). {ECO:0000269|PubMed:21222654}.
CC -!- SUBUNIT: Interacts with the DELLA proteins RGA and GAI
CC (PubMed:25010794). Interacts with PIF3 and PIF5 (PubMed:26704640).
CC Interacts with the auxin efflux carrier PIN1 (PubMed:25560878).
CC {ECO:0000269|PubMed:25010794, ECO:0000269|PubMed:25560878,
CC ECO:0000269|PubMed:26704640}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19329567,
CC ECO:0000269|PubMed:25010794, ECO:0000269|PubMed:25560878,
CC ECO:0000269|PubMed:26704640}. Cytoplasm {ECO:0000269|PubMed:19329567,
CC ECO:0000269|PubMed:25560878}. Note=Localizes predominantly to the
CC nucleus. {ECO:0000269|PubMed:19329567, ECO:0000269|PubMed:25560878}.
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature of roots and
CC cotyledons, tips of leaves, guard cells, bases of trichomes, pistils
CC and stamen filaments. {ECO:0000269|PubMed:25010794}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype and decreased fertility.
CC {ECO:0000269|PubMed:25010794}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; M93411; AAA32839.1; -; mRNA.
DR EMBL; AC003000; AAB87136.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09737.1; -; Genomic_DNA.
DR EMBL; BT026118; ABG48474.1; -; mRNA.
DR EMBL; AK229028; BAF00914.1; -; mRNA.
DR PIR; S31088; S31088.
DR RefSeq; NP_181514.1; NM_129543.3.
DR AlphaFoldDB; P48484; -.
DR SMR; P48484; -.
DR BioGRID; 3909; 7.
DR STRING; 3702.AT2G39840.1; -.
DR iPTMnet; P48484; -.
DR PaxDb; P48484; -.
DR PRIDE; P48484; -.
DR ProteomicsDB; 249134; -.
DR EnsemblPlants; AT2G39840.1; AT2G39840.1; AT2G39840.
DR GeneID; 818571; -.
DR Gramene; AT2G39840.1; AT2G39840.1; AT2G39840.
DR KEGG; ath:AT2G39840; -.
DR Araport; AT2G39840; -.
DR TAIR; locus:2063942; AT2G39840.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P48484; -.
DR OMA; YLVMESR; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P48484; -.
DR PRO; PR:P48484; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P48484; baseline and differential.
DR Genevisible; P48484; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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 GO; GO:0016311; P:dephosphorylation; IDA:TAIR.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IGI:TAIR.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IPI:TAIR.
DR GO; GO:0010161; P:red light signaling pathway; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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 Acetylation; Cytoplasm; Growth regulation; Hydrolase; Manganese;
KW Metal-binding; Nucleus; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..321
FT /note="Serine/threonine-protein phosphatase PP1 isozyme 4"
FT /id="PRO_0000058800"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 321 AA; 36372 MW; 9E96830AB996FFB3 CRC64;
MATTTTTQGQ QTAIDSAVLD DIIRRLTEVR LARPGKQVQL SEAEIKQLCT TARDIFLQQP
NLLELEAPIK ICGDIHGQYS DLLRLFEYGG FPPSANYLFL GDYVDRGKQS LETICLLLAY
KIKYPGNFFL LRGNHECASI NRIYGFYDEC KRRFNVRVWK VFTDCFNCLP VAALIDDKIL
CMHGGLSPDL DHLDEIRNLP RPTMIPDTGL LCDLLWSDPG KDVKGWGMND RGVSYTFGPD
KVSEFLTKHD LDLVCRAHQV VEDGYEFFAD RQLVTVFSAP NYCGEFDNAG AMMSVDENLM
CSFQILKPAE KKTKFMMSTK I
