PP17_ARATH
ID PP17_ARATH Reviewed; 331 AA.
AC O82733; O48641; Q2V319; Q8L761;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein phosphatase PP1 isozyme 7 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:21222654};
DE AltName: Full=Type one protein phosphatase 7 {ECO:0000303|PubMed:17368080};
GN Name=TOPP7 {ECO:0000303|PubMed:17368080};
GN Synonyms=TOPP6 {ECO:0000303|PubMed:21222654};
GN OrderedLocusNames=At5g43380 {ECO:0000312|Araport:AT5G43380};
GN ORFNames=MWF20.7 {ECO:0000312|EMBL:BAA97417.1};
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 [GENOMIC DNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Mitsukawa N., Okumura S., Shibata D.;
RT "Isolation of a gene that encode a protein phosphatase 1 catalytic subunit
RT in Arabidopsis thaliana.";
RL Soil Sci. Plant Nutr. 43:971-974(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9617814; DOI=10.1023/a:1005912413555;
RA Lin Q., Li J., Smith R.D., Walker J.C.;
RT "Molecular cloning and chromosomal mapping of type one serine/threonine
RT protein phosphatases in Arabidopsis thaliana.";
RL Plant Mol. Biol. 37:471-481(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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] (ISOFORM 1).
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 FUNCTION, CATALYTIC ACTIVITY, AND 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).
CC -!- FUNCTION: Serine/threonine-protein phosphatase that possesses
CC phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro.
CC {ECO:0000269|PubMed:21222654}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm
CC {ECO:0000269|PubMed:19329567}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O82733-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O82733-2; Sequence=VSP_009006;
CC Name=3;
CC IsoId=O82733-3; Sequence=VSP_028726;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosettes and flowers.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39459.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB000094; BAA24283.1; -; Genomic_DNA.
DR EMBL; U80920; AAC39459.1; ALT_FRAME; mRNA.
DR EMBL; AB025638; BAA97417.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94952.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94953.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94954.1; -; Genomic_DNA.
DR EMBL; AY136464; AAM97129.1; -; mRNA.
DR EMBL; BT002143; AAN72154.1; -; mRNA.
DR RefSeq; NP_001032000.1; NM_001036923.1. [O82733-3]
DR RefSeq; NP_568625.1; NM_123704.3. [O82733-2]
DR RefSeq; NP_851123.1; NM_180792.3. [O82733-1]
DR AlphaFoldDB; O82733; -.
DR SMR; O82733; -.
DR BioGRID; 19606; 4.
DR IntAct; O82733; 3.
DR STRING; 3702.AT5G43380.1; -.
DR PaxDb; O82733; -.
DR PRIDE; O82733; -.
DR ProteomicsDB; 249148; -. [O82733-1]
DR EnsemblPlants; AT5G43380.1; AT5G43380.1; AT5G43380. [O82733-1]
DR EnsemblPlants; AT5G43380.2; AT5G43380.2; AT5G43380. [O82733-2]
DR EnsemblPlants; AT5G43380.3; AT5G43380.3; AT5G43380. [O82733-3]
DR GeneID; 834356; -.
DR Gramene; AT5G43380.1; AT5G43380.1; AT5G43380. [O82733-1]
DR Gramene; AT5G43380.2; AT5G43380.2; AT5G43380. [O82733-2]
DR Gramene; AT5G43380.3; AT5G43380.3; AT5G43380. [O82733-3]
DR KEGG; ath:AT5G43380; -.
DR Araport; AT5G43380; -.
DR TAIR; locus:3356119; AT5G43380.
DR eggNOG; KOG0374; Eukaryota.
DR InParanoid; O82733; -.
DR OMA; MGWSDND; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; O82733; -.
DR PRO; PR:O82733; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O82733; baseline and differential.
DR Genevisible; O82733; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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; Alternative splicing; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..331
FT /note="Serine/threonine-protein phosphatase PP1 isozyme 7"
FT /id="PRO_0000058803"
FT ACT_SITE 121
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P48486"
FT VAR_SEQ 320..331
FT /note="SILSSQNSKEYN -> VCINHITF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9617814"
FT /id="VSP_009006"
FT VAR_SEQ 320..331
FT /note="SILSSQNSKEYN -> DCNW (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_028726"
FT CONFLICT 7
FT /note="N -> I (in Ref. 2; AAC39459)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="G -> E (in Ref. 2; AAC39459)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="Missing (in Ref. 2; AAC39459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 37705 MW; 2D351A1C368B0CA2 CRC64;
MDPGTLNSVI NRLLEAREKP GKIVQLSETE IKQLCFVSRD IFLRQPNLLE LEAPVKICGD
IHGQYPDLLR LFEHGGYPPN SNYLFLGDYV DRGKQSLETI CLLLAYKIKF PENFFLLRGN
HESASINRIY GFYDECKRRF SVKIWRIFTD CFNCLPVAAL IDERIFCMHG GLSPELLSLR
QIRDIRRPTD IPDRGLLCDL LWSDPDKDVR GWGPNDRGVS YTFGSDIVSG FLKRLDLDLI
CRAHQVVEDG FEFFANKQLV TIFSAPNYCG EFDNAGAMMS VSEDLTCSFQ ILKSNDKKSK
FSFGSRGGAK TSFPYPKVKS ILSSQNSKEY N
