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   27-MAR-2024, entry version 150.
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.Q9FN02; -.
DR   iPTMnet; Q9FN02; -.
DR   PaxDb; 3702-AT5G63870-2; -.
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; AT5G63870; PP7.
DR   eggNOG; KOG0376; Eukaryota.
DR   HOGENOM; CLU_004962_1_1_1; -.
DR   InParanoid; Q9FN02; -.
DR   OMA; PPWEGTN; -.
DR   OrthoDB; 20002at2759; -.
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   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   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF9; SERINE_THREONINE-PROTEIN PHOSPHATASE 7; 1.
DR   Pfam; PF00149; Metallophos; 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; Q9FN02; AT.
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
//