TAP46_ARATH
ID TAP46_ARATH Reviewed; 405 AA.
AC Q8LDQ4; Q9LVV2; Q9XHD0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=PP2A regulatory subunit TAP46 {ECO:0000303|PubMed:10517853};
DE AltName: Full=2A phosphatase-associated protein of 46 kDa {ECO:0000305};
GN Name=TAP46 {ECO:0000303|PubMed:10517853};
GN OrderedLocusNames=At5g53000 {ECO:0000312|Araport:AT5G53000};
GN ORFNames=MNB8.6 {ECO:0000312|EMBL:BAA97140.1};
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], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP INTERACTION WITH PP2A.
RX PubMed=10517853; DOI=10.1104/pp.121.2.609;
RA Harris D.M., Myrick T.L., Rundle S.J.;
RT "The Arabidopsis homolog of yeast TAP42 and mammalian alpha4 binds to the
RT catalytic subunit of protein phosphatase 2A and is induced by chilling.";
RL Plant Physiol. 121:609-617(1999).
RN [2]
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 [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;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISRUPTION PHENOTYPE, INTERACTION WITH PP2A3; PPX1 AND FYPP1, FUNCTION, AND
RP PHOSPHORYLATION.
RX PubMed=21216945; DOI=10.1105/tpc.110.074005;
RA Ahn C.S., Han J.-A., Lee H.-S., Lee S., Pai H.-S.;
RT "The PP2A regulatory subunit Tap46, a component of the TOR signaling
RT pathway, modulates growth and metabolism in plants.";
RL Plant Cell 23:185-209(2011).
RN [7]
RP ADDENDUM.
RX PubMed=21597327; DOI=10.4161/psb.6.7.15651;
RA Ahn C.S., Lee H.S., Pai H.S.;
RT "Molecular functions of the PP2A regulatory subunit Tap46 in plants.";
RL Plant Signal. Behav. 6:1067-1068(2011).
RN [8]
RP REVIEW.
RX PubMed=24810976; DOI=10.1111/pce.12364;
RA Lillo C., Kataya A.R., Heidari B., Creighton M.T., Nemie-Feyissa D.,
RA Ginbot Z., Jonassen E.M.;
RT "Protein phosphatases PP2A, PP4 and PP6: mediators and regulators in
RT development and responses to environmental cues.";
RL Plant Cell Environ. 37:2631-2648(2014).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ABA, INTERACTION WITH PP2A1;
RP PP2A2; PP2A3; PPX1; FYPP1; FYPP3 AND ABI5, AND DEVELOPMENTAL STAGE.
RX PubMed=24357600; DOI=10.1104/pp.113.233684;
RA Hu R., Zhu Y., Shen G., Zhang H.;
RT "TAP46 plays a positive role in the ABSCISIC ACID INSENSITIVE5-regulated
RT gene expression in Arabidopsis.";
RL Plant Physiol. 164:721-734(2014).
RN [10]
RP FUNCTION, AND INTERACTION WITH ATPK1 AND ATPK2.
RX PubMed=25399018; DOI=10.1093/jxb/eru438;
RA Ahn C.S., Ahn H.K., Pai H.S.;
RT "Overexpression of the PP2A regulatory subunit Tap46 leads to enhanced
RT plant growth through stimulation of the TOR signalling pathway.";
RL J. Exp. Bot. 66:827-840(2015).
CC -!- FUNCTION: Involved in the positive regulation of the TOR signaling
CC pathway (PubMed:21216945, PubMed:25399018). Acts as a negative
CC regulator of PP2A catalytic activity (PubMed:10517853, PubMed:21216945,
CC PubMed:24357600). Plays a positive role in the ABA-regulated inhibition
CC of germination, probably throught its interaction with ABI5
CC (PubMed:24357600). {ECO:0000269|PubMed:10517853,
CC ECO:0000269|PubMed:21216945, ECO:0000269|PubMed:24357600,
CC ECO:0000269|PubMed:25399018}.
CC -!- SUBUNIT: Interacts with the 36 kDa catalytic subunit (subunit C) of
CC PP2A (PubMed:10517853). Interacts with PP2A1 and PP2A2
CC (PubMed:24357600). Interacts with PP2A3, PPX1 and FYPP1
CC (PubMed:21216945, PubMed:24357600). Interacts with FYPP3 and ABI5
CC (PubMed:24357600). Interacts with ATPK1/S6K1 and ATPK2/S6K2
CC (PubMed:25399018). Interacts with TIP41L (By similarity).
CC {ECO:0000250|UniProtKB:Q04372, ECO:0000269|PubMed:10517853,
CC ECO:0000269|PubMed:21216945, ECO:0000269|PubMed:24357600,
CC ECO:0000269|PubMed:25399018}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:10517853). Highly expressed in
CC seed, and particularly in the embryo (PubMed:24357600).
CC {ECO:0000269|PubMed:10517853, ECO:0000269|PubMed:24357600}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during seed maturation.
CC {ECO:0000269|PubMed:24357600}.
CC -!- INDUCTION: By chilling (PubMed:10517853). By abscisic acid (ABA)
CC (PubMed:24357600). {ECO:0000269|PubMed:10517853,
CC ECO:0000269|PubMed:24357600}.
CC -!- PTM: Phosphorylated by TOR kinase in vitro.
CC {ECO:0000269|PubMed:21216945}.
CC -!- DISRUPTION PHENOTYPE: RNAi plants show the formation of spontaneous
CC disease-like nectrotic lesions leading to premature cell death. The
CC defective plants also display a strong reduction in protein synthesis,
CC the induction of autophagy and nitrogen mobilization.
CC {ECO:0000269|PubMed:21216945}.
CC -!- MISCELLANEOUS: Plants over-expressing TAP46 exhibit an increased
CC abscisic acid (ABA) sensitivity in seed germination and a reduced PP2A
CC activity (PubMed:24357600). Over-expression of TAP46 also leads to the
CC stimulation of the overall plant growth and the increased nitrogen-
CC assimilating activities (PubMed:25399018).
CC {ECO:0000269|PubMed:24357600, ECO:0000269|PubMed:25399018}.
CC -!- SIMILARITY: Belongs to the IGBP1/TAP42 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97140.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF133708; AAD39930.1; -; mRNA.
DR EMBL; AB018116; BAA97140.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96288.1; -; Genomic_DNA.
DR EMBL; BT004072; AAO42099.1; -; mRNA.
DR EMBL; BT006150; AAP04135.1; -; mRNA.
DR EMBL; AY085863; AAM63076.1; -; mRNA.
DR PIR; T52307; T52307.
DR RefSeq; NP_568783.1; NM_124679.3.
DR AlphaFoldDB; Q8LDQ4; -.
DR SMR; Q8LDQ4; -.
DR BioGRID; 20624; 38.
DR IntAct; Q8LDQ4; 34.
DR STRING; 3702.AT5G53000.1; -.
DR PaxDb; Q8LDQ4; -.
DR PRIDE; Q8LDQ4; -.
DR ProteomicsDB; 234181; -.
DR EnsemblPlants; AT5G53000.1; AT5G53000.1; AT5G53000.
DR GeneID; 835379; -.
DR Gramene; AT5G53000.1; AT5G53000.1; AT5G53000.
DR KEGG; ath:AT5G53000; -.
DR Araport; AT5G53000; -.
DR TAIR; locus:2168392; AT5G53000.
DR eggNOG; KOG2830; Eukaryota.
DR HOGENOM; CLU_041824_0_0_1; -.
DR InParanoid; Q8LDQ4; -.
DR OMA; RAWDEFT; -.
DR OrthoDB; 1348942at2759; -.
DR PhylomeDB; Q8LDQ4; -.
DR PRO; PR:Q8LDQ4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LDQ4; baseline and differential.
DR Genevisible; Q8LDQ4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0010187; P:negative regulation of seed germination; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:0035303; P:regulation of dephosphorylation; IBA:GO_Central.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0031929; P:TOR signaling; IMP:UniProtKB.
DR Gene3D; 1.25.40.540; -; 1.
DR InterPro; IPR038511; TAP42/TAP46-like_sf.
DR InterPro; IPR007304; TAP46-like.
DR PANTHER; PTHR10933; PTHR10933; 1.
DR Pfam; PF04177; TAP42; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..405
FT /note="PP2A regulatory subunit TAP46"
FT /id="PRO_0000218622"
FT REGION 159..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 376..378
FT /note="EEA -> DEP (in Ref. 5; AAM63076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 45663 MW; E31201DC5BECADB0 CRC64;
MGGLAMEEMP LSVLFEQARK IHLAASESGV DQDVVKKGCE MFQKCEDMIG KLALFSSNET
KEDISTNNLK YLLVPYYLAE LTEKIIQEDR IQIVKASYAK LKEFFSFCEA MELVPDEELE
ASSRGGSGAP ADRRALKIAR FKRQKAAEAK LLEIKERKER RGRSTKASAL STPVESGEDD
IPDDDSEEER EAWLSSINLA ICKAIDLLEM LKREEEMLSA IKERQLKDGE GGFSRDALDD
RTKKAETWHR DAAARIQYSK PAQPITCATF AQDVLEGRAS VSQGHEHKNQ PLIFGPASIV
GGPLSTERER MIAQVFQPSH RMPTMCIEDA GLTEMNIMND WQEQTKKAIE EATTSWYNDK
PLRRKEEDEE DDDEDEEAVM KARAFDDWKD DNPRGAGNKK LTPCG
