PPP7_ARATH
ID PPP7_ARATH Reviewed; 413 AA.
AC Q9FN02; O49346; Q3E865;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Serine/threonine-protein phosphatase 7;
DE EC=3.1.3.16;
GN Name=PP7; OrderedLocusNames=At5g63870; ORFNames=MGI19.7;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=9584984; DOI=10.1080/15216549800201752;
RA Andreeva A.V., Evans D.E., Hawes C.R., Bennett N., Kutuzov M.A.;
RT "PP7, a plant phosphatase representing a novel evolutionary branch of
RT eukaryotic protein Ser/Thr phosphatases.";
RL Biochem. Mol. Biol. Int. 44:703-715(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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] (ISOFORM 2).
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 [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION, DISULFIDE BOND, AND
RP COFACTOR.
RX PubMed=9862444; DOI=10.1016/s0014-5793(98)01428-8;
RA Kutuzov M.A., Evans D.E., Andreeva A.V.;
RT "Expression and characterization of PP7, a novel plant protein Ser/Thr
RT phosphatase distantly related to RdgC/PPEF and PP5.";
RL FEBS Lett. 440:147-152(1998).
RN [6]
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=11716463; DOI=10.1006/abbi.2001.2582;
RA Andreeva A.V., Solov'eva O.V., Kakuev D.L., Kutuzov M.A.;
RT "Purification of plant protein phosphatase PP7 and evidence for its redox
RT regulation.";
RL Arch. Biochem. Biophys. 396:65-70(2001).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITION BY INORGANIC PHOSPHATE.
RX PubMed=11322772; DOI=10.1006/bbrc.2001.4751;
RA Kutuzov M.A., Andreeva A.V.;
RT "Noncompetitive inhibition of plant protein Ser/Thr phosphatase PP7 by
RT phosphate.";
RL Biochem. Biophys. Res. Commun. 283:93-96(2001).
RN [8]
RP INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF 209-ARG--LEU-231 AND
RP 369-PRO--SER-413.
RX PubMed=11716523; DOI=10.1006/bbrc.2001.6020;
RA Kutuzov M.A., Bennett N., Andreeva A.V.;
RT "Interaction of plant protein Ser/Thr phosphatase PP7 with calmodulin.";
RL Biochem. Biophys. Res. Commun. 289:634-640(2001).
RN [9]
RP MUTAGENESIS OF 207-PRO--LEU-231 AND 369-PRO--SER-413, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11703093; DOI=10.1006/mcbr.2001.0302;
RA Andreeva A.V., Kutuzov M.A.;
RT "Nuclear localization of the plant protein Ser/Thr phosphatase PP7.";
RL Mol. Cell Biol. Res. Commun. 4:345-352(2001).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12724537; DOI=10.1105/tpc.008649;
RA Moeller S.G., Kim Y.-S., Kunkel T., Chua N.-H.;
RT "PP7 is a positive regulator of blue light signaling in Arabidopsis.";
RL Plant Cell 15:1111-1119(2003).
RN [11]
RP FUNCTION, INTERACTION WITH CALMODULIN AND HSFA1A, AND INDUCTION BY HEAT
RP SHOCK.
RX PubMed=17238907; DOI=10.1111/j.1365-3040.2006.01613.x;
RA Liu H.-T., Li G.-L., Chang H., Sun D.-Y., Zhou R.-G., Li B.;
RT "Calmodulin-binding protein phosphatase PP7 is involved in thermotolerance
RT in Arabidopsis.";
RL Plant Cell Environ. 30:156-164(2007).
RN [12]
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).
CC -!- FUNCTION: Phosphatase active on para-nitrophenylphosphate (pNPP) and on
CC various phosphoproteins such as myelin basic protein. Seems to act as a
CC positive regulator of cryptochrome signaling involved in hypocotyl
CC growth inhibition and cotyledon expansion under white and blue light
CC conditions. Confers thermotolerance. Required for heat shock mediated-
CC signaling pathway that leads to the expression of heat shock proteins
CC (HSPs). {ECO:0000269|PubMed:12724537, ECO:0000269|PubMed:17238907,
CC ECO:0000269|PubMed:9862444}.
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;
CC Evidence={ECO:0000269|PubMed:9862444};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:9862444};
CC -!- ACTIVITY REGULATION: Inhibited by NaF and orthovanadate, as well as by
CC divalent cations such as Ni(2+) and Zn(2+). Inhibited by polylysine
CC with myelin basic protein as substrate, but activated by polylysine
CC with pNPP as substrate. Reversibly regulated by redox agents. Inhibited
CC by submillimolar Pi concentrations. Slightly repressed by calmodulin
CC (CaM). {ECO:0000269|PubMed:11716463}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for pNPP (at pH 7.8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:11322772, ECO:0000269|PubMed:9862444};
CC pH dependence:
CC Optimum pH is around 7. {ECO:0000269|PubMed:11322772,
CC ECO:0000269|PubMed:9862444};
CC -!- SUBUNIT: Monomer, homodimer, and heteromer. Interacts with calmodulin
CC (CaM3 and CaM4) and HSFA1A/HSF1. {ECO:0000269|PubMed:11716463,
CC ECO:0000269|PubMed:11716523, ECO:0000269|PubMed:17238907}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11703093}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FN02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FN02-2; Sequence=VSP_029088, VSP_029089;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, and, to a lower extent, in
CC stems and flowers. {ECO:0000269|PubMed:12724537}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:17238907}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-7 subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ000057; CAA03886.1; -; mRNA.
DR EMBL; AB007646; BAB11035.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97806.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97807.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97808.1; -; Genomic_DNA.
DR EMBL; AY050898; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T51611; T51611.
DR RefSeq; NP_568979.1; NM_125782.3. [Q9FN02-2]
DR RefSeq; NP_851258.2; NM_180927.4. [Q9FN02-1]
DR RefSeq; NP_851259.1; NM_180928.2. [Q9FN02-1]
DR AlphaFoldDB; Q9FN02; -.
DR SMR; Q9FN02; -.
DR BioGRID; 21749; 5.
DR IntAct; Q9FN02; 1.
DR MINT; Q9FN02; -.
DR STRING; 3702.AT5G63870.2; -.
DR iPTMnet; Q9FN02; -.
DR PaxDb; Q9FN02; -.
DR PRIDE; Q9FN02; -.
DR ProteomicsDB; 226292; -. [Q9FN02-1]
DR EnsemblPlants; AT5G63870.1; AT5G63870.1; AT5G63870. [Q9FN02-1]
DR EnsemblPlants; AT5G63870.2; AT5G63870.2; AT5G63870. [Q9FN02-1]
DR EnsemblPlants; AT5G63870.3; AT5G63870.3; AT5G63870. [Q9FN02-2]
DR GeneID; 836507; -.
DR Gramene; AT5G63870.1; AT5G63870.1; AT5G63870. [Q9FN02-1]
DR Gramene; AT5G63870.2; AT5G63870.2; AT5G63870. [Q9FN02-1]
DR Gramene; AT5G63870.3; AT5G63870.3; AT5G63870. [Q9FN02-2]
DR KEGG; ath:AT5G63870; -.
DR Araport; AT5G63870; -.
DR TAIR; locus:2163991; AT5G63870.
DR eggNOG; KOG0376; Eukaryota.
DR HOGENOM; CLU_004962_1_1_1; -.
DR OMA; FVDRGAW; -.
DR PhylomeDB; Q9FN02; -.
DR BRENDA; 3.1.3.16; 399.
DR PRO; PR:Q9FN02; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN02; baseline and differential.
DR Genevisible; Q9FN02; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA: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:0009785; P:blue light signaling pathway; IMP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR CDD; cd07418; MPP_PP7; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041754; MPP_PP7.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 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 Alternative splicing; Disulfide bond; Hydrolase; Manganese; Metal-binding;
KW Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..413
FT /note="Serine/threonine-protein phosphatase 7"
FT /id="PRO_0000308991"
FT REGION 391..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT DISULFID 28..67
FT /evidence="ECO:0000305|PubMed:9862444"
FT VAR_SEQ 298..301
FT /note="LIIR -> VTPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_029088"
FT VAR_SEQ 302..413
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_029089"
FT MUTAGEN 207..231
FT /note="PKRTTRGKKNRRVVLLEPEPSSMKL->GGGGGGGGGGGGGGGGGGGGGGGGG
FT : Normal subcellular location."
FT /evidence="ECO:0000269|PubMed:11703093"
FT MUTAGEN 209..231
FT /note="Missing: Reduced activity, but enhanced inducibility
FT by polylysine with pNPP as substrate; reduced binding with
FT calmodulin."
FT /evidence="ECO:0000269|PubMed:11716523"
FT MUTAGEN 369..413
FT /note="Missing: Loss of activity; normal binding with
FT calmodulin; cytoplasmic instead of nuclear subcellular
FT location."
FT /evidence="ECO:0000269|PubMed:11703093,
FT ECO:0000269|PubMed:11716523"
FT CONFLICT 266
FT /note="M -> I (in Ref. 1; CAA03886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46619 MW; 111A9E01A222A058 CRC64;
METVPPSPIT WPDGGALTND WVHGLMSCFE WSSWNLPPSQ LPSLLPVNVF DSLVLTAHKI
LHKERNCVHI DDLDSVSNVV VVGDIHGQLH DLLFLLKDTG FPCQNRCYVF NGDYVDRGAW
GLETFLVLLS WKVLMPDRVY LLRGNHESKY CTSMYGFEKE VLTKYGDKGK HVYRKCLGCF
EGLPLASIIS GRVYTAHGGL FRSPVLPKRT TRGKKNRRVV LLEPEPSSMK LGTLDELMQA
RRSVLDPPWE GSNLIPGDVL WSDPSMTPGL SPNEQRGIGL LWGPDCTEDF LKKYELKLII
RSHEGPDARE KRTGLGGMDN GYTIDHNVES GKLITIFSAP DYPQFQATEE RYKNKGAYII
LQAPDFSDPQ FHSFEAVKPR PKAHPYYDFE NVIDSDDEMD KSAMDTNNEQ PNS
