CMTA3_ARATH
ID CMTA3_ARATH Reviewed; 1032 AA.
AC Q8GSA7; Q0WW70; Q9FPR9; Q9SID7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=Calmodulin-binding transcription activator 3 {ECO:0000303|PubMed:11925432};
DE Short=AtCAMTA3 {ECO:0000303|PubMed:11925432};
DE AltName: Full=Ethylene-induced calmodulin-binding protein 1 {ECO:0000303|PubMed:11162426};
DE Short=EICBP1 {ECO:0000303|PubMed:11162426};
DE AltName: Full=Ethylene-induced calmodulin-binding protein a {ECO:0000303|PubMed:11782485};
DE Short=EICBP.a {ECO:0000303|PubMed:11782485};
DE AltName: Full=Protein SAR-DEFICIENT 3 {ECO:0000303|PubMed:21900483};
DE AltName: Full=Signal-responsive protein 1 {ECO:0000303|PubMed:12218065};
DE Short=AtSR1 {ECO:0000303|PubMed:12218065};
GN Name=CAMTA3 {ECO:0000303|PubMed:11925432};
GN Synonyms=CMTA3 {ECO:0000305}, SARD3 {ECO:0000303|PubMed:21900483},
GN SR1 {ECO:0000303|PubMed:12218065};
GN OrderedLocusNames=At2g22300 {ECO:0000312|Araport:AT2G22300};
GN ORFNames=T26C19.4 {ECO:0000312|EMBL:AAD23613.1};
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], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11162426; DOI=10.1006/bbrc.2000.4032;
RA Reddy A.S.N., Reddy V.S., Golovkin M.;
RT "A calmodulin binding protein from Arabidopsis is induced by ethylene and
RT contains a DNA-binding motif.";
RL Biochem. Biophys. Res. Commun. 279:762-769(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CALMODULIN-BINDING, INDUCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12218065; DOI=10.1074/jbc.m207941200;
RA Yang T., Poovaiah B.W.;
RT "A calmodulin-binding/CGCG box DNA-binding protein family involved in
RT multiple signaling pathways in plants.";
RL J. Biol. Chem. 277:45049-45058(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11925432; DOI=10.1074/jbc.m200268200;
RA Bouche N., Scharlat A., Snedden W., Bouchez D., Fromm H.;
RT "A novel family of calmodulin-binding transcription activators in
RT multicellular organisms.";
RL J. Biol. Chem. 277:21851-21861(2002).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=14581622; DOI=10.1093/pcp/pcg137;
RA Mitsuda N., Isono T., Sato M.H.;
RT "Arabidopsis CAMTA family proteins enhance V-PPase expression in pollen.";
RL Plant Cell Physiol. 44:975-981(2003).
RN [9]
RP IDENTIFICATION.
RX PubMed=11782485; DOI=10.1074/jbc.m111626200;
RA Reddy V.S., Ali G.S., Reddy A.S.N.;
RT "Genes encoding calmodulin-binding proteins in the Arabidopsis genome.";
RL J. Biol. Chem. 277:9840-9852(2002).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18298954; DOI=10.1016/j.febslet.2008.02.037;
RA Galon Y., Nave R., Boyce J.M., Nachmias D., Knight M.R., Fromm H.;
RT "Calmodulin-binding transcription activator (CAMTA) 3 mediates biotic
RT defense responses in Arabidopsis.";
RL FEBS Lett. 582:943-948(2008).
RN [11]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272,
RP AND 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 [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19122675; DOI=10.1038/nature07612;
RA Du L., Ali G.S., Simons K.A., Hou J., Yang T., Reddy A.S., Poovaiah B.W.;
RT "Ca(2+)/calmodulin regulates salicylic-acid-mediated plant immunity.";
RL Nature 457:1154-1158(2009).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19270186; DOI=10.1105/tpc.108.063958;
RA Doherty C.J., Van Buskirk H.A., Myers S.J., Thomashow M.F.;
RT "Roles for Arabidopsis CAMTA transcription factors in cold-regulated gene
RT expression and freezing tolerance.";
RL Plant Cell 21:972-984(2009).
RN [14]
RP FUNCTION.
RX PubMed=21900483; DOI=10.1104/pp.111.182089;
RA Jing B., Xu S., Xu M., Li Y., Li S., Ding J., Zhang Y.;
RT "Brush and spray: a high-throughput systemic acquired resistance assay
RT suitable for large-scale genetic screening.";
RL Plant Physiol. 157:973-980(2011).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23072934; DOI=10.1093/pcp/pcs143;
RA Laluk K., Prasad K.V., Savchenko T., Celesnik H., Dehesh K., Levy M.,
RA Mitchell-Olds T., Reddy A.S.;
RT "The calmodulin-binding transcription factor SIGNAL RESPONSIVE1 is a novel
RT regulator of glucosinolate metabolism and herbivory tolerance in
RT Arabidopsis.";
RL Plant Cell Physiol. 53:2008-2015(2012).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22371088; DOI=10.1007/s11103-012-9896-z;
RA Qiu Y., Xi J., Du L., Suttle J.C., Poovaiah B.W.;
RT "Coupling calcium/calmodulin-mediated signaling and herbivore-induced plant
RT response through calmodulin-binding transcription factor AtSR1/CAMTA3.";
RL Plant Mol. Biol. 79:89-99(2012).
RN [17]
RP FUNCTION, INDUCTION, AND MUTAGENESIS OF ALA-855.
RX PubMed=22345509; DOI=10.1104/pp.111.192310;
RA Nie H., Zhao C., Wu G., Wu Y., Chen Y., Tang D.;
RT "SR1, a calmodulin-binding transcription factor, modulates plant defense
RT and ethylene-induced senescence by directly regulating NDR1 and EIN3.";
RL Plant Physiol. 158:1847-1859(2012).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23581962; DOI=10.1111/tpj.12205;
RA Kim Y., Park S., Gilmour S.J., Thomashow M.F.;
RT "Roles of CAMTA transcription factors and salicylic acid in configuring the
RT low-temperature transcriptome and freezing tolerance of Arabidopsis.";
RL Plant J. 75:364-376(2013).
RN [19]
RP INTERACTION WITH SR1IP1, AND UBIQUITINATION.
RX PubMed=24528504; DOI=10.1111/tpj.12473;
RA Zhang L., Du L., Shen C., Yang Y., Poovaiah B.W.;
RT "Regulation of plant immunity through ubiquitin-mediated modulation of
RT Ca(2+) -calmodulin-AtSR1/CAMTA3 signaling.";
RL Plant J. 78:269-281(2014).
RN [20]
RP FUNCTION.
RX PubMed=25039701; DOI=10.1111/tpj.12620;
RA Benn G., Wang C.Q., Hicks D.R., Stein J., Guthrie C., Dehesh K.;
RT "A key general stress response motif is regulated non-uniformly by CAMTA
RT transcription factors.";
RL Plant J. 80:82-92(2014).
RN [21]
RP FUNCTION.
RX PubMed=25157030; DOI=10.1104/pp.114.245944;
RA Bjornson M., Benn G., Song X., Comai L., Franz A.K., Dandekar A.M.,
RA Drakakaki G., Dehesh K.;
RT "Distinct roles for mitogen-activated protein kinase signaling and
RT CALMODULIN-BINDING TRANSCRIPTIONAL ACTIVATOR3 in regulating the peak time
RT and amplitude of the plant general stress response.";
RL Plant Physiol. 166:988-996(2014).
RN [22]
RP FUNCTION, INTERACTION WITH DSC1, AND DISRUPTION PHENOTYPE.
RX PubMed=28407487; DOI=10.1016/j.chom.2017.03.005;
RA Lolle S., Greeff C., Petersen K., Roux M., Jensen M.K., Bressendorff S.,
RA Rodriguez E., Soemark K., Mundy J., Petersen M.;
RT "Matching NLR immune receptors to autoimmunity in camta3 mutants using
RT antimorphic NLR alleles.";
RL Cell Host Microbe 21:518-529(2017).
RN [23]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28351986; DOI=10.1105/tpc.16.00669;
RA Kidokoro S., Yoneda K., Takasaki H., Takahashi F., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Different cold-signaling pathways function in the responses to rapid and
RT gradual decreases in temperature.";
RL Plant Cell 29:760-774(2017).
CC -!- FUNCTION: Transcription activator that binds to the DNA consensus
CC sequence 5'-[ACG]CGCG[GTC]-3'. Binds calmodulin in a calcium-dependent
CC manner in vitro (PubMed:12218065). Regulates transcriptional activity
CC in response to calcium signals (Probable). Involved in freezing
CC tolerance in association with CAMTA1 and CAMTA2 (PubMed:23581962).
CC Required for the cold-induced expression of DREB1B/CBF1, DREB1C/CBF2,
CC ZAT12 and GOLS3 (PubMed:19270186). Involved in response to cold.
CC Contributes together with CAMTA5 to the positive regulation of the
CC cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2
CC (PubMed:28351986). Involved together with CAMTA2 and CAMTA4 in the
CC positive regulation of a general stress response (GSR)
CC (PubMed:25039701). Involved in the regulation of GSR amplitude
CC downstream of MEKK1 (PubMed:25157030). Involved in the regulation of a
CC set of genes involved in defense responses against pathogens
CC (PubMed:18298954). Involved in the regulation of both basal resistance
CC and systemic acquired resistance (SAR) (PubMed:21900483). Acts as
CC negative regulator of plant immunity (PubMed:19122675, PubMed:21900483,
CC PubMed:22345509, PubMed:28407487). Binds to the promoter of the
CC defense-related gene EDS1 and represses its expression
CC (PubMed:19122675). Binds to the promoter of the defense-related gene
CC NDR1 and represses its expression (PubMed:22345509). Involved in
CC defense against insects (PubMed:23072934, PubMed:22371088). Required
CC for tolerance to the generalist herbivore Trichoplusia ni, and
CC contributes to the positive regulation of genes associated with
CC glucosinolate metabolism (PubMed:23072934). Required for tolerance to
CC Bradysia impatiens larvae. Mediates herbivore-induced wound response
CC (PubMed:22371088). Required for wound-induced jasmonate accumulation
CC (PubMed:23072934, PubMed:22371088). Involved in the regulation of
CC ethylene-induced senescence by binding to the promoter of the
CC senescence-inducer gene EIN3 and repressing its expression
CC (PubMed:22345509). {ECO:0000269|PubMed:12218065,
CC ECO:0000269|PubMed:18298954, ECO:0000269|PubMed:19122675,
CC ECO:0000269|PubMed:19270186, ECO:0000269|PubMed:21900483,
CC ECO:0000269|PubMed:22345509, ECO:0000269|PubMed:22371088,
CC ECO:0000269|PubMed:23072934, ECO:0000269|PubMed:23581962,
CC ECO:0000269|PubMed:25039701, ECO:0000269|PubMed:25157030,
CC ECO:0000269|PubMed:28351986, ECO:0000269|PubMed:28407487,
CC ECO:0000305|PubMed:11925432}.
CC -!- SUBUNIT: Interacts with SR1IP1 (PubMed:24528504). Interacts with DSC1
CC (PubMed:28407487). {ECO:0000269|PubMed:24528504,
CC ECO:0000269|PubMed:28407487}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767,
CC ECO:0000269|PubMed:11925432, ECO:0000269|PubMed:12218065,
CC ECO:0000269|PubMed:19245862, ECO:0000269|PubMed:28351986}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, carpels, and
CC siliques, but not in stigmas or other parts of the flower.
CC {ECO:0000269|PubMed:11162426, ECO:0000269|PubMed:12218065,
CC ECO:0000269|PubMed:14581622}.
CC -!- INDUCTION: By heat shock, UVB, salt, wounding, ethylene and methyl
CC jasmonate (PubMed:11162426, PubMed:12218065). Induced by infection with
CC the fungal pathogen Golovinomyces cichoracearum (powdery mildew) and
CC the bacterial pathogen Pseudomonas syringae pv tomato strain DC3000
CC (PubMed:22345509). {ECO:0000269|PubMed:11162426,
CC ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:22345509}.
CC -!- PTM: Ubiquinated during pathogen infection. Ubiquitination leads to its
CC subsequent proteasome-dependent degradation, thus allowing the
CC establishment of plant defense response. {ECO:0000269|PubMed:24528504}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants camta1 and camta3 are impaired in
CC freezing tolerance (PubMed:19270186). No visible phenotype under normal
CC growth conditions, but the double mutants camt1 and camt3 exhibit semi-
CC dwarf phenotypes (PubMed:19270186, PubMed:23581962). No visible
CC phenotype under normal growth conditions, but the double mutants camt2
CC and camt3 exhibit dwarf phenotypes (PubMed:23581962). Reduced growth,
CC chlorosis, spontaneous lesions and constitutive expression of defense-
CC related genes when grown under 22 degrees Celsius (PubMed:18298954,
CC PubMed:19122675, PubMed:28407487). Enhanced sensitivity to insect
CC herbivores (PubMed:23072934, PubMed:22371088).
CC {ECO:0000269|PubMed:18298954, ECO:0000269|PubMed:19122675,
CC ECO:0000269|PubMed:19270186, ECO:0000269|PubMed:22371088,
CC ECO:0000269|PubMed:23072934, ECO:0000269|PubMed:23581962,
CC ECO:0000269|PubMed:28407487}.
CC -!- MISCELLANEOUS: The camta3-3D activation tagging mutant plants exhibit
CC compromised systemic acquired resistance (SAR) and enhanced
CC susceptibility to virulent pathogens. {ECO:0000269|PubMed:21900483}.
CC -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD23613.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY510025; AAR98746.1; -; mRNA.
DR EMBL; AF303397; AAG37879.1; -; mRNA.
DR EMBL; AF506697; AAN74651.1; -; mRNA.
DR EMBL; AC007168; AAD23613.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07289.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07290.1; -; Genomic_DNA.
DR EMBL; BT002459; AAO00819.1; -; mRNA.
DR EMBL; AK226486; BAE98628.1; -; mRNA.
DR PIR; A84611; A84611.
DR RefSeq; NP_001118361.1; NM_001124889.2.
DR RefSeq; NP_850023.1; NM_179692.3.
DR AlphaFoldDB; Q8GSA7; -.
DR SMR; Q8GSA7; -.
DR BioGRID; 2115; 2.
DR DIP; DIP-59735N; -.
DR IntAct; Q8GSA7; 1.
DR STRING; 3702.AT2G22300.1; -.
DR iPTMnet; Q8GSA7; -.
DR PaxDb; Q8GSA7; -.
DR PRIDE; Q8GSA7; -.
DR ProteomicsDB; 220531; -.
DR EnsemblPlants; AT2G22300.1; AT2G22300.1; AT2G22300.
DR EnsemblPlants; AT2G22300.2; AT2G22300.2; AT2G22300.
DR GeneID; 816762; -.
DR Gramene; AT2G22300.1; AT2G22300.1; AT2G22300.
DR Gramene; AT2G22300.2; AT2G22300.2; AT2G22300.
DR KEGG; ath:AT2G22300; -.
DR Araport; AT2G22300; -.
DR TAIR; locus:2060405; AT2G22300.
DR eggNOG; KOG0520; Eukaryota.
DR HOGENOM; CLU_005708_1_1_1; -.
DR InParanoid; Q8GSA7; -.
DR OrthoDB; 224822at2759; -.
DR PhylomeDB; Q8GSA7; -.
DR PRO; PR:Q8GSA7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GSA7; baseline and differential.
DR Genevisible; Q8GSA7; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0070417; P:cellular response to cold; IGI:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IGI:TAIR.
DR GO; GO:0106167; P:extracellular ATP signaling; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:1900367; P:positive regulation of defense response to insect; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005559; CG-1_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF03859; CG-1; 1.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM01076; CG-1; 1.
DR SMART; SM00015; IQ; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51437; CG_1; 1.
DR PROSITE; PS50096; IQ; 2.
PE 1: Evidence at protein level;
KW Activator; ANK repeat; Calcium; Calmodulin-binding; Coiled coil;
KW DNA-binding; Nucleus; Phosphoprotein; Plant defense; Reference proteome;
KW Repeat; Repressor; Stress response; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1032
FT /note="Calmodulin-binding transcription activator 3"
FT /id="PRO_0000114488"
FT REPEAT 661..690
FT /note="ANK 1"
FT REPEAT 694..723
FT /note="ANK 2"
FT REPEAT 733..762
FT /note="ANK 3"
FT DOMAIN 852..881
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 875..904
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DNA_BIND 15..141
FT /note="CG-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00767"
FT REGION 146..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..922
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:12218065"
FT COILED 945..987
FT /evidence="ECO:0000255"
FT COMPBIAS 170..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NPP4"
FT MUTAGEN 855
FT /note="A->V: Gain-of-function mutant."
FT /evidence="ECO:0000269|PubMed:22345509"
FT CONFLICT 382
FT /note="Q -> E (in Ref. 6; BAE98628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1032 AA; 116111 MW; 4C5E9775A3795862 CRC64;
MAEARRFSPV HELDVGQILS EARHRWLRPP EICEILQNYQ RFQISTEPPT TPSSGSVFMF
DRKVLRYFRK DGHNWRKKKD GKTVKEAHER LKAGSVDVLH CYYAHGQDNE NFQRRSYWLL
QEELSHIVFV HYLEVKGSRV STSFNRMQRT EDAARSPQET GDALTSEHDG YASCSFNQND
HSNHSQTTDS ASVNGFHSPE LEDAESAYNQ HGSSTAYSHQ ELQQPATGGN LTGFDPYYQI
SLTPRDSYQK ELRTIPVTDS SIMVDKSKTI NSPGVTNGLK NRKSIDSQTW EEILGNCGSG
VEALPLQPNS EHEVLDQILE SSFTMQDFAS LQESMVKSQN QELNSGLTSD RTVWFQGQDM
ELNAISNLAS NEKAPYLSTM KQHLLHGALG EEGLKKMDSF NRWMSKELGD VGVIADANES
FTQSSSRTYW EEVESEDGSN GHNSRRDMDG YVMSPSLSKE QLFSINDFSP SWAYVGCEVV
VFVTGKFLKT REETEIGEWS CMFGQTEVPA DVISNGILQC VAPMHEAGRV PFYVTCSNRL
ACSEVREFEY KVAESQVFDR EADDESTIDI LEARFVKLLC SKSENTSPVS GNDSDLSQLS
EKISLLLFEN DDQLDQMLMN EISQENMKNN LLQEFLKESL HSWLLQKIAE GGKGPSVLDE
GGQGVLHFAA SLGYNWALEP TIIAGVSVDF RDVNGWTALH WAAFFGRERI IGSLIALGAA
PGTLTDPNPD FPSGSTPSDL AYANGHKGIA GYLSEYALRA HVSLLSLNDK NAETVEMAPS
PSSSSLTDSL TAVRNATQAA ARIHQVFRAQ SFQKKQLKEF GDKKLGMSEE RALSMLAPKT
HKSGRAHSDD SVQAAAIRIQ NKFRGYKGRK DYLITRQRII KIQAHVRGYQ FRKNYRKIIW
SVGVLEKVIL RWRRKGAGLR GFKSEALVEK MQDGTEKEED DDFFKQGRKQ TEDRLQKALA
RVKSMVQYPE ARDQYRRLLN VVNDIQESKV EKALENSEAT CFDDDDDLID IEALLEDDDT
LMLPMSSSLW TS
