ID CMTA1_ARATH Reviewed; 1007 AA.
AC Q9FY74; F4KCL6; Q0WQF9;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Calmodulin-binding transcription activator 1 {ECO:0000303|PubMed:11925432};
DE Short=AtCAMTA1 {ECO:0000303|PubMed:11925432};
DE AltName: Full=Ethylene-induced calmodulin-binding protein b {ECO:0000303|PubMed:11782485};
DE Short=EICBP.b {ECO:0000303|PubMed:11782485};
DE AltName: Full=Signal-responsive protein 2 {ECO:0000303|PubMed:12218065};
DE Short=AtSR2 {ECO:0000303|PubMed:12218065};
GN Name=CAMTA1 {ECO:0000303|PubMed:11925432};
GN Synonyms=CMTA1 {ECO:0000305}, SR2 {ECO:0000303|PubMed:12218065};
GN OrderedLocusNames=At5g09410 {ECO:0000312|Araport:AT5G09410};
GN ORFNames=T5E8.210 {ECO:0000312|EMBL:CAC05467.1};
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=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 [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] (ISOFORM 2).
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, CALMODULIN-BINDING, GENE FAMILY, AND
RP 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 [5]
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 [6]
RP FUNCTION, AND 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 [7]
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 [8]
RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20383645; DOI=10.1007/s00425-010-1153-6;
RA Galon Y., Aloni R., Nachmias D., Snir O., Feldmesser E., Scrase-Field S.,
RA Boyce J.M., Bouche N., Knight M.R., Fromm H.;
RT "Calmodulin-binding transcription activator 1 mediates auxin signaling and
RT responds to stresses in Arabidopsis.";
RL Planta 232:165-178(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23547968; DOI=10.1186/1471-2164-14-216;
RA Pandey N., Ranjan A., Pant P., Tripathi R.K., Ateek F., Pandey H.P.,
RA Patre U.V., Sawant S.V.;
RT "CAMTA 1 regulates drought responses in Arabidopsis thaliana.";
RL BMC Genomics 14:216-216(2013).
RN [10]
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 [11]
RP 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 [12]
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 [13]
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).
CC -!- FUNCTION: Transcription activator that binds calmodulin in a calcium-
CC dependent manner in vitro (PubMed:11925432). 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 Involved in freezing tolerance (PubMed:19270186). Involved in freezing
CC tolerance in association with CAMTA2 and CAMTA3. Contributes together
CC with CAMTA2 and CAMTA3 to the positive regulation of the cold-induced
CC expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2
CC (PubMed:23581962). Involved in drought stress responses by regulating
CC several drought-responsive genes (PubMed:23547968). Involved in auxin
CC signaling and responses to abiotic stresses (PubMed:20383645).
CC Activates the expression of the V-PPase proton pump AVP1 in pollen
CC (PubMed:14581622). {ECO:0000250|UniProtKB:Q8GSA7,
CC ECO:0000269|PubMed:11925432, ECO:0000269|PubMed:14581622,
CC ECO:0000269|PubMed:19270186, ECO:0000269|PubMed:20383645,
CC ECO:0000269|PubMed:23547968, ECO:0000269|PubMed:23581962,
CC ECO:0000305|PubMed:11925432}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767,
CC ECO:0000269|PubMed:11925432}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FY74-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FY74-2; Sequence=VSP_040640;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, pollen and
CC siliques. {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:14581622}.
CC -!- DEVELOPMENTAL STAGE: During leaf development, expressed in young leaf
CC primordia, hydathodes of young leaf tips, hydathodes of the lobes in
CC maturating leaves and lamina within the minor veins in adult leaves.
CC During flower development, expressed in developing stamens, germinating
CC pollen grains, ovules and developing seeds.
CC {ECO:0000269|PubMed:20383645}.
CC -!- INDUCTION: Induced by UVB, wounding, ethylene and methyl jasmonate
CC (PubMed:12218065). Induced by salt stress and heat shock
CC (PubMed:12218065, PubMed:20383645). Induced by aluminum
CC (PubMed:25627216). {ECO:0000269|PubMed:12218065,
CC ECO:0000269|PubMed:20383645, ECO:0000269|PubMed:25627216}.
CC -!- DOMAIN: The two IQ domains are probably not interacting with
CC calcium/calmodulin.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedling are hyper-responsive to auxin in
CC hypocotyl growth inhibition (PubMed:20383645). No visible phenotype
CC under normal growth conditions, but mutant seedling exhibit reduced
CC drought tolerance (PubMed:23547968). No visible phenotype under normal
CC growth conditions, but the double mutants camta1 and camta3 are
CC impaired in freezing tolerance (PubMed:19270186). No visible phenotype
CC under normal growth conditions, but the double mutants camt1 and camt3
CC exhibit semi-dwarf phenotypes (PubMed:19270186, PubMed:23581962).
CC {ECO:0000269|PubMed:19270186, ECO:0000269|PubMed:20383645,
CC ECO:0000269|PubMed:23547968, ECO:0000269|PubMed:23581962}.
CC -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}.
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DR EMBL; AL391712; CAC05467.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91388.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91389.1; -; Genomic_DNA.
DR EMBL; AK228740; BAF00640.1; -; mRNA.
DR RefSeq; NP_001119195.1; NM_001125723.2. [Q9FY74-1]
DR RefSeq; NP_196503.3; NM_120978.5. [Q9FY74-2]
DR AlphaFoldDB; Q9FY74; -.
DR SMR; Q9FY74; -.
DR BioGRID; 16078; 1.
DR STRING; 3702.Q9FY74; -.
DR iPTMnet; Q9FY74; -.
DR PaxDb; 3702-AT5G09410-3; -.
DR EnsemblPlants; AT5G09410.1; AT5G09410.1; AT5G09410. [Q9FY74-2]
DR EnsemblPlants; AT5G09410.2; AT5G09410.2; AT5G09410. [Q9FY74-1]
DR GeneID; 830800; -.
DR Gramene; AT5G09410.1; AT5G09410.1; AT5G09410. [Q9FY74-2]
DR Gramene; AT5G09410.2; AT5G09410.2; AT5G09410. [Q9FY74-1]
DR KEGG; ath:AT5G09410; -.
DR Araport; AT5G09410; -.
DR TAIR; AT5G09410; EICBP.B.
DR eggNOG; KOG0520; Eukaryota.
DR InParanoid; Q9FY74; -.
DR OMA; EMVLHLR; -.
DR PRO; PR:Q9FY74; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FY74; baseline and differential.
DR Genevisible; Q9FY74; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IMP:UniProtKB.
DR GO; GO:0050826; P:response to freezing; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR002909; IPT_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23335:SF42; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR 1; 1.
DR PANTHER; PTHR23335; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR CAMTA; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF03859; CG-1; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF01833; TIG; 1.
DR SMART; SM00248; ANK; 1.
DR SMART; SM01076; CG-1; 1.
DR SMART; SM00015; IQ; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Alternative splicing; ANK repeat; Calcium; Calmodulin-binding;
KW Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Stress response; Transcription; Transcription regulation.
FT CHAIN 1..1007
FT /note="Calmodulin-binding transcription activator 1"
FT /id="PRO_0000114486"
FT REPEAT 612..641
FT /note="ANK 1"
FT REPEAT 645..674
FT /note="ANK 2"
FT DOMAIN 821..850
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 844..873
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DNA_BIND 18..144
FT /note="CG-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00767"
FT REGION 148..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..398
FT /note="Transcription activation"
FT /evidence="ECO:0000269|PubMed:11925432"
FT REGION 869..891
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:11925432"
FT COILED 915..943
FT /evidence="ECO:0000255"
FT COMPBIAS 148..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NPP4"
FT VAR_SEQ 184..201
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_040640"
FT CONFLICT 137
FT /note="E -> Q (in Ref. 1; CAC05467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1007 AA; 113853 MW; 73FAB1EC5F746E06 CRC64;
MVDRRSFGSI TPPLQLDMEQ LLSEAQHRWL RPTEICEILQ NYHKFHIASE SPTRPASGSL
FLFDRKVLRY FRKDGHNWRK KKDGKTIREA HEKLKVGSID VLHCYYAHGE ANENFQRRCY
WMLEQHLMHI VFVHYLEVKG NRTSIGMKEN NSNSVNGTAS VNIDSTASPT STLSSLCEDA
DTGDSQQASS VLRPSPEPQT GNRYGWTPAP GMRNVSQVHG NRVRESDSQR LVDVRALDTV
GNSLTRFHDQ PYCNNLLTQM QPSNTDSMLV EENSEKGGRL KAEHIRNPLQ TQFNWQDDTD
LALFEQSAQD NFETFSSLLG SENLQPFGIS YQAPPSNMDS EYMPVMKILR RSEDSLKKVD
SFSKWAIKEL GEMEDLQMQS SRGDIAWTTV ECETAAAGIS LSPSLSEDQR FTIVDFWPKS
AKTDAEVEVM VIGTFLLSPQ EVTKYNWSCM FGEVEVPAEI LVDGVLCCHA PPHTAGHVPF
YVTCSNRFAC SEVREFDFLS GSTQKINATD VYGTYTNEAS LQLRFEKMLA HRDFVHEHHI
FEDVGDKRRQ ISKIMLLKEE KEYLLPGTYQ RDSTKQEPKG QLFRELFEEE LYIWLIHKVT
EEGKGPNILD EDGQGILHFV AALGYDWAIK PVLAAGVNIN FRDANGWSAL HWAAFSGREE
TVAVLVSLGA DAGALTDPSP ELPLGKTAAD LAYANGHRGI SGFLAESSLT SYLEKLTVDS
KENSPANSCG EKAVQTVSER TAAPMTYGDV PEKLSLKDSL TAVRNATQAA DRLHQVFRMQ
SFQRKQLCDI GDDEKIDISD QLAVSFAASK TKNPGQGDVS LSCAATHIQK KYRGWKKRKE
FLLIRQRIVK IQAHVRGHQV RKQYRTVIWS VGLLEKIILR WRRKGNGLRG FKRNAVAKTV
EPEPPVSAIC PRIPQEDEYD YLKEGRKQTE ERLQKALTRV KSMVQYPEAR DQYRRLLTVV
EGFRENEASS SASINNKEEE AVNCEEDDFI DIESLLNDDT LMMSISP
//
