TON2_ARATH
ID TON2_ARATH Reviewed; 480 AA.
AC Q9FEE2;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit TON2;
DE AltName: Full=Protein EMBRYO DEFFECTIVE 40;
DE AltName: Full=Protein GORDO;
DE AltName: Full=Protein TONNEAU 2;
GN Name=TON2; Synonyms=EMB40, FASS, FASS1, FASS2, FS1, GDO;
GN OrderedLocusNames=At5g18580; ORFNames=T28N17;
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 / MRNA], FUNCTION, INTERACTION WITH
RP PP2AA1, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11971138; DOI=10.1105/tpc.010402;
RA Camilleri C., Azimzadeh J., Pastuglia M., Bellini C., Grandjean O.,
RA Bouchez D.;
RT "The Arabidopsis TONNEAU2 gene encodes a putative novel protein phosphatase
RT 2A regulatory subunit essential for the control of the cortical
RT cytoskeleton.";
RL Plant Cell 14:833-845(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22395485; DOI=10.1105/tpc.111.094367;
RA Kirik A., Ehrhardt D.W., Kirik V.;
RT "TONNEAU2/FASS regulates the geometry of microtubule nucleation and
RT cortical array organization in interphase Arabidopsis cells.";
RL Plant Cell 24:1158-1170(2012).
CC -!- FUNCTION: Probable regulatory subunit of type 2A protein phosphatase
CC involved in the control of the dynamic organization of the cortical
CC cytoskeleton. Plays an important role in the organization of interphase
CC microtubule arrays in part through the regulation of nucleation
CC geometry. Required for the reorganization of cortical arrays in
CC response to light. {ECO:0000269|PubMed:11971138,
CC ECO:0000269|PubMed:22395485}.
CC -!- SUBUNIT: Interacts with PP2AA1. {ECO:0000269|PubMed:11971138}.
CC -!- INTERACTION:
CC Q9FEE2; A0A384L363: AXX17_At3g19340; NbExp=4; IntAct=EBI-4452426, EBI-25511057;
CC Q9FEE2; Q9LRH6: GATA25; NbExp=3; IntAct=EBI-4452426, EBI-2460434;
CC Q9FEE2; Q8H1G0: GATA28; NbExp=3; IntAct=EBI-4452426, EBI-4435064;
CC Q9FEE2; Q38830: IAA12; NbExp=3; IntAct=EBI-4452426, EBI-617608;
CC Q9FEE2; Q9XFM0: IAA28; NbExp=3; IntAct=EBI-4452426, EBI-3133404;
CC Q9FEE2; Q9FNV9: MYB113; NbExp=3; IntAct=EBI-4452426, EBI-1546246;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22395485}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22395485}.
CC Note=Predominantly cytoplasmic, but at the late G2 phase localizes at
CC the cortical region corresponding to the preprophase band.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11971138}.
CC -!- DISRUPTION PHENOTYPE: Extreme phenotype with disrupted cell elongation
CC and a highly compressed apical-basal axis due to disorganization of the
CC interphase microtubule array and lack of the preprophase band before
CC mitosis. Sterile flowers. {ECO:0000269|PubMed:11971138}.
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DR EMBL; AF280057; AAG35778.1; -; mRNA.
DR EMBL; AF290025; AAG35792.1; -; Genomic_DNA.
DR EMBL; AC069328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92581.1; -; Genomic_DNA.
DR EMBL; AF360316; AAK26026.1; -; mRNA.
DR EMBL; AY113888; AAM44936.1; -; mRNA.
DR RefSeq; NP_568364.1; NM_121863.4.
DR AlphaFoldDB; Q9FEE2; -.
DR SMR; Q9FEE2; -.
DR BioGRID; 17252; 11.
DR IntAct; Q9FEE2; 9.
DR STRING; 3702.AT5G18580.1; -.
DR iPTMnet; Q9FEE2; -.
DR PaxDb; Q9FEE2; -.
DR PRIDE; Q9FEE2; -.
DR ProteomicsDB; 234324; -.
DR EnsemblPlants; AT5G18580.1; AT5G18580.1; AT5G18580.
DR GeneID; 831976; -.
DR Gramene; AT5G18580.1; AT5G18580.1; AT5G18580.
DR KEGG; ath:AT5G18580; -.
DR Araport; AT5G18580; -.
DR TAIR; locus:2183003; AT5G18580.
DR eggNOG; KOG2562; Eukaryota.
DR HOGENOM; CLU_035365_2_0_1; -.
DR OMA; HKFWAYE; -.
DR OrthoDB; 541286at2759; -.
DR PhylomeDB; Q9FEE2; -.
DR PRO; PR:Q9FEE2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FEE2; baseline and differential.
DR Genevisible; Q9FEE2; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0005819; C:spindle; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0000913; P:preprophase band assembly; IMP:UniProtKB.
DR GO; GO:0035303; P:regulation of dephosphorylation; IEA:InterPro.
DR GO; GO:0009826; P:unidimensional cell growth; TAS:TAIR.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR039865; PPP2R3C.
DR PANTHER; PTHR12085; PTHR12085; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Cytoskeleton; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..480
FT /note="Probable serine/threonine-protein phosphatase 2A
FT regulatory subunit B'' subunit TON2"
FT /id="PRO_0000420915"
FT DOMAIN 186..221
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 294..329
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 369..404
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 480 AA; 55070 MW; 2568ABC3E898574A CRC64;
MYSGSSDGES HDTSTQRKIP PASSMLWVRN LRRYIGSGAG LGSEALMELE TKRILLEIFK
EKQQKSQEAG TIPSFYKKKP EEGSISQRVQ KLAKYRFLKK QSDLLLNADD LAAMWVCLRE
NCVIDDATGA EKMNYEDFCH IASVCTEQIG PKCRRFFSPS NFMKFEKDEA GRIAILPFYL
YVMRTVSLTQ ARIDMSELDE DSDGFLHSDE MESYIGGLIP NLAQLRDMPP AFNQMYCRIA
SQKFFFFCDP HRRGRACIKK ILLSNCLQEL MELHQESEEE VTDTEQAENW FSLTSAQRIC
DMFLALDKDM SGSLCKQELK EYADGTLTEI FIERVFDEHV RRGKIVAGNS REMDFDSFLD
FVLALENKDT PEGLTYLFRC LDLQGRGFLT TADIHSLFRD VHQKWIEGGN YELCIEDVRD
EIWDMVKPSD PLKITLGDLL GCKQGGTVAS MLIDVRGFWA HDNRENLLQE EEEPPEEESQ
