IPP2_ARATH
ID IPP2_ARATH Reviewed; 191 AA.
AC Q9LTK0;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Protein phosphatase inhibitor 2 {ECO:0000305};
DE Short=AtI-2 {ECO:0000303|PubMed:21222654};
DE Short=IPP-2 {ECO:0000305};
GN Name=I-2 {ECO:0000303|PubMed:21222654};
GN OrderedLocusNames=At5g52200 {ECO:0000312|Araport:AT5G52200};
GN ORFNames=F17P19.10 {ECO:0000312|EMBL:AED96182.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-47, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH PROTEIN
RP PHOSPHATASE 1, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF
RP VAL-9 AND TRP-11.
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 [7]
RP FUNCTION, INTERACTION WITH TOPP1; SRK2D/SNRK2.2; SRK2I/SNRK2.3;
RP SRK2E/SNRK2.6; SRK2C/SNRK2.8 AND PYL11, TISSUE SPECIFICITY, AND DISRUPTION
RP 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: Inhibitor of protein-phosphatase 1 (PP1). Binds to and
CC inhibits PP1 activity (PubMed:21222654, PubMed:26943172). Acts as
CC negative regulator of abscisic acid (ABA) signaling. Enhances the
CC inhibition of SRK2E/SNRK2.6 by TOPP1. May promote the interaction
CC between TOPP1 and the ABA receptor PYL11 (PubMed:26943172).
CC {ECO:0000269|PubMed:21222654, ECO:0000269|PubMed:26943172}.
CC -!- SUBUNIT: Interacts with protein phosphatase 1 (PubMed:21222654).
CC Interacts with TOPP1, SRK2D/SNRK2.2, SRK2I/SNRK2.3, SRK2E/SNRK2.6,
CC SRK2C/SNRK2.8 and PYL11 (PubMed:26943172).
CC {ECO:0000269|PubMed:21222654, ECO:0000269|PubMed:26943172}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21222654}. Cytoplasm
CC {ECO:0000269|PubMed:21222654}. Note=Predominantly localizes in the
CC nucleus. {ECO:0000269|PubMed:21222654}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoform are produced. According to EST sequences.
CC {ECO:0000305};
CC Name=1;
CC IsoId=Q9LTK0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:26943172}.
CC -!- PTM: Phosphorylated in vivo. {ECO:0000269|PubMed:21222654}.
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}.
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DR EMBL; AB025603; BAA97463.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96182.1; -; Genomic_DNA.
DR EMBL; AY050347; AAK91364.1; -; mRNA.
DR EMBL; AY116938; AAM51572.1; -; mRNA.
DR RefSeq; NP_568768.1; NM_124599.5. [Q9LTK0-1]
DR AlphaFoldDB; Q9LTK0; -.
DR IntAct; Q9LTK0; 1.
DR STRING; 3702.AT5G52200.2; -.
DR iPTMnet; Q9LTK0; -.
DR MetOSite; Q9LTK0; -.
DR PRIDE; Q9LTK0; -.
DR ProteomicsDB; 247285; -. [Q9LTK0-1]
DR EnsemblPlants; AT5G52200.1; AT5G52200.1; AT5G52200. [Q9LTK0-1]
DR GeneID; 835296; -.
DR Gramene; AT5G52200.1; AT5G52200.1; AT5G52200. [Q9LTK0-1]
DR KEGG; ath:AT5G52200; -.
DR Araport; AT5G52200; -.
DR eggNOG; ENOG502RYGC; Eukaryota.
DR HOGENOM; CLU_099603_1_1_1; -.
DR OMA; SRRVKWN; -.
DR PhylomeDB; Q9LTK0; -.
DR PRO; PR:Q9LTK0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTK0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR InterPro; IPR007062; PPI-2.
DR PANTHER; PTHR12398; PTHR12398; 1.
DR Pfam; PF04979; IPP-2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..191
FT /note="Protein phosphatase inhibitor 2"
FT /id="PRO_0000442225"
FT REGION 20..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 9
FT /note="V->A: Loss of binding to protein-phosphatase 1
FT (PP1); when associated with A-11."
FT /evidence="ECO:0000269|PubMed:21222654"
FT MUTAGEN 11
FT /note="W->A: Loss of binding to protein-phosphatase 1
FT (PP1); when associated with A-9."
FT /evidence="ECO:0000269|PubMed:21222654"
SQ SEQUENCE 191 AA; 21097 MW; 697F451CF5C56CFB CRC64;
MTEPKRGRVQ WDEANIVEIE SNKPVRQKIT EPKTPYHPMM DDDGSLSPRG RAFDECVDDM
QRAEELRNVL NDAAASSSRN SSQGSGGGGW SSSDEEEEEA DPMDQDEEGS GSGKNERFNA
HRKAHYDEFR KVKELRSSGS FYEEEEEEDD GAKGSKSETT TNSRHTKGGN KELDATKTVS
GTSSSSSPEL I
