CMTA2_ARATH
ID CMTA2_ARATH Reviewed; 1050 AA.
AC Q6NPP4; Q0WNN4; Q9FMG3;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Calmodulin-binding transcription activator 2 {ECO:0000303|PubMed:11925432};
DE Short=AtCAMTA2 {ECO:0000303|PubMed:11925432};
DE AltName: Full=AtER66 {ECO:0000303|PubMed:11162426};
DE AltName: Full=Ethylene-induced calmodulin-binding protein c {ECO:0000303|PubMed:11782485};
DE Short=EICBP.c {ECO:0000303|PubMed:11782485};
DE AltName: Full=Signal-responsive protein 4 {ECO:0000303|PubMed:12218065};
DE Short=AtSR4 {ECO:0000303|PubMed:12218065};
GN Name=CAMTA2 {ECO:0000303|PubMed:11925432};
GN Synonyms=CMTA2 {ECO:0000305}, SR4 {ECO:0000303|PubMed:12218065};
GN OrderedLocusNames=At5g64220 {ECO:0000312|Araport:AT5G64220};
GN ORFNames=MSJ1.6 {ECO:0000312|EMBL:BAB09853.1};
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;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP INDUCTION, AND TISSUE SPECIFICITY.
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 [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=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 [10]
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 [11]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984,
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984, AND IDENTIFICATION BY
RP 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 [13]
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 [14]
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 [15]
RP FUNCTION, AND INDUCTION BY ALUMINUM.
RX PubMed=25627216; DOI=10.1104/pp.114.256552;
RA Tokizawa M., Kobayashi Y., Saito T., Kobayashi M., Iuchi S., Nomoto M.,
RA Tada Y., Yamamoto Y.Y., Koyama H.;
RT "SENSITIVE TO PROTON RHIZOTOXICITY1, CALMODULIN BINDING TRANSCRIPTION
RT ACTIVATOR2, and other transcription factors are involved in ALUMINUM-
RT ACTIVATED MALATE TRANSPORTER1 expression.";
RL Plant Physiol. 167:991-1003(2015).
RN [16]
RP 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' (By similarity). Regulates
CC transcriptional activity in response to calcium signals (Probable).
CC Binds calmodulin in a calcium-dependent manner (By similarity).
CC Involved in freezing tolerance in association with CAMTA1 and CAMTA3.
CC Contributes together with CAMTA1 and CAMTA3 to the positive regulation
CC of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and
CC DREB1C/CBF2 (PubMed:23581962). Involved together with CAMTA3 and CAMTA4
CC in the positive regulation of a general stress response
CC (PubMed:25039701). Involved in tolerance to aluminum. Binds to the
CC promoter of ALMT1 transporter and contributes to the positive
CC regulation of aluminum-induced expression of ALMT1 (PubMed:25627216).
CC {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:23581962,
CC ECO:0000269|PubMed:25039701, ECO:0000269|PubMed:25627216,
CC ECO:0000305|PubMed:11925432}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767,
CC ECO:0000269|PubMed:19245862, ECO:0000269|PubMed:28351986}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, old leaves, petals,
CC sepals, top of carpels, stigmas, stamen filaments, anthers and
CC siliques, but not in pollen. {ECO:0000269|PubMed:12218065,
CC ECO:0000269|PubMed:14581622}.
CC -!- INDUCTION: By salt, wounding, abscisic acid, H(2)O(2) and salicylic
CC acid (PubMed:12218065). Induced by aluminum (PubMed:25627216).
CC {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:25627216}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants camt2 and camt3 exhibit dwarf
CC phenotypes. {ECO:0000269|PubMed:23581962}.
CC -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB008268; BAB09853.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97856.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97857.1; -; Genomic_DNA.
DR EMBL; BT010874; AAR24652.1; -; mRNA.
DR EMBL; AK229403; BAF01265.1; -; mRNA.
DR EMBL; AB493811; BAH30649.1; -; mRNA.
DR RefSeq; NP_001032135.1; NM_001037058.2.
DR RefSeq; NP_201227.3; NM_125818.3.
DR AlphaFoldDB; Q6NPP4; -.
DR STRING; 3702.AT5G64220.2; -.
DR iPTMnet; Q6NPP4; -.
DR PaxDb; Q6NPP4; -.
DR PRIDE; Q6NPP4; -.
DR ProteomicsDB; 220479; -.
DR EnsemblPlants; AT5G64220.1; AT5G64220.1; AT5G64220.
DR EnsemblPlants; AT5G64220.2; AT5G64220.2; AT5G64220.
DR GeneID; 836543; -.
DR Gramene; AT5G64220.1; AT5G64220.1; AT5G64220.
DR Gramene; AT5G64220.2; AT5G64220.2; AT5G64220.
DR KEGG; ath:AT5G64220; -.
DR Araport; AT5G64220; -.
DR TAIR; locus:2173368; AT5G64220.
DR eggNOG; KOG0520; Eukaryota.
DR HOGENOM; CLU_005708_1_0_1; -.
DR InParanoid; Q6NPP4; -.
DR OMA; WDASFEN; -.
DR OrthoDB; 89428at2759; -.
DR PhylomeDB; Q6NPP4; -.
DR PRO; PR:Q6NPP4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NPP4; baseline and differential.
DR Genevisible; Q6NPP4; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0071275; P:cellular response to aluminum ion; IEP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:TAIR.
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:TAIR.
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; PF12796; Ank_2; 1.
DR Pfam; PF03859; CG-1; 1.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM00248; ANK; 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; 2.
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; Reference proteome; Repeat;
KW Stress response; Transcription; Transcription regulation.
FT CHAIN 1..1050
FT /note="Calmodulin-binding transcription activator 2"
FT /id="PRO_0000114487"
FT REPEAT 661..690
FT /note="ANK 1"
FT REPEAT 694..723
FT /note="ANK 2"
FT DOMAIN 870..899
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 893..922
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 141..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..940
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9FY74"
FT COILED 957..985
FT /evidence="ECO:0000255"
FT COMPBIAS 141..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 1050 AA; 117258 MW; 318050B641D646F9 CRC64;
MADRGSFGFA PRLDIKQLLS EAQHRWLRPA EICEILRNHQ KFHIASEPPN RPPSGSLFLF
DRKVLRYFRK DGHNWRKKKD GKTVKEAHEK LKVGSIDVLH CYYAHGEDNE NFQRRCYWML
EQDLMHIVFV HYLEVKGNRM STSGTKENHS NSLSGTGSVN VDSTATRSSI LSPLCEDADS
GDSRQASSSL QQNPEPQTVV PQIMHHQNAS TINSYNTTSV LGNRDGWTSA HGNRVKGSNS
QRSGDVPAWD ASFENSLARY QNLPYNAPLT QTQPSTFGLI PMEGKTEKGS LLTSEHLRNP
LQSQVNWQTP VQESVPLQKW PMDSHSGMTD ATDLALFGQG AHENFGTFSS LLGSQDQQSS
SFQAPFTNNE AAYIPKLGPE DLIYEASANQ TLPLRKALLK KEDSLKKVDS FSRWVSKELG
EMEDLQMQSS SGGIAWTSVE CENAAAGSSL SPSLSEDQRF TMIDFWPKWT QTDSEVEVMV
IGTFLLSPQE VTSYSWSCMF GEVEVPADIL VDGVLCCHAP PHEVGRVPFY ITCSDRFSCS
EVREFDFLPG STRKLNATDI YGANTIETSL HLRFENLLAL RCSVQEHHIF ENVGEKRRKI
SKIMLLKDEK EPPLPGTIEK DLTELEAKER LIREEFEDKL YLWLIHKVTE EGKGPNILDE
DGQGVLHLAA ALGYDWAIKP ILAAGVSINF RDANGWSALH WAAFSGREDT VAVLVSLGAD
AGALADPSPE HPLGKTAADL AYGNGHRGIS GFLAESSLTS YLEKLTVDAK ENSSADSSGA
KAVLTVAERT ATPMSYGDVP ETLSMKDSLT AVLNATQAAD RLHQVFRMQS FQRKQLSELG
GDNKFDISDE LAVSFAAAKT KKSGHSSGAV HAAAVQIQKK YRGWKKRKEF LLIRQRIVKI
QAHVRGHQVR KQYRAIIWSV GLLEKIILRW RRKGSGLRGF KRDTISKPTE PVCPAPQEDD
YDFLKEGRKQ TEERLQKALT RVKSMAQYPE ARAQYRRLLT VVEGFRENEA SSSSALKNNT
EEAANYNEED DLIDIDSLLD DDTFMSLAFE
