CMTA5_ARATH
ID CMTA5_ARATH Reviewed; 923 AA.
AC O23463; Q8L7R9;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Calmodulin-binding transcription activator 5 {ECO:0000303|PubMed:11925432};
DE Short=AtCAMTA5 {ECO:0000303|PubMed:11925432};
DE AltName: Full=Ethylene-induced calmodulin-binding protein f {ECO:0000303|PubMed:11782485};
DE Short=EICBP.f {ECO:0000303|PubMed:11782485};
DE AltName: Full=Signal-responsive protein 6 {ECO:0000303|PubMed:12218065};
DE Short=AtSR6 {ECO:0000303|PubMed:12218065};
GN Name=CAMTA5 {ECO:0000303|PubMed:11925432};
GN Synonyms=CMTA5 {ECO:0000305}, SR6 {ECO:0000303|PubMed:12218065};
GN OrderedLocusNames=At4g16150 {ECO:0000312|Araport:AT4G16150};
GN ORFNames=dl4115W {ECO:0000312|EMBL:CAB10394.1},
GN FCAALL.291 {ECO:0000312|EMBL:CAB78657.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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, 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 [6]
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 [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [8]
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 [9]
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 (PubMed:14581622). Binds to the DNA
CC consensus 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 response to cold. Contributes together with CAMTA3 to the
CC positive regulation of the cold-induced expression of DREB1A/CBF3,
CC DREB1B/CBF1 and DREB1C/CBF2 (PubMed:28351986).
CC {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:14581622,
CC ECO:0000269|PubMed:28351986, ECO:0000305|PubMed:11925432}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767,
CC ECO:0000269|PubMed:14581622, ECO:0000269|PubMed:28351986}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, pollen, top of
CC sepals and siliques. {ECO:0000269|PubMed:12218065,
CC ECO:0000269|PubMed:14581622}.
CC -!- INDUCTION: By heat shock, UVB, wounding, abscisic acid, H(2)O(2) and
CC salicylic acid. {ECO:0000269|PubMed:12218065}.
CC -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB10394.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB78657.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78657.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z97340; CAB10394.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161543; CAB78657.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83703.2; -; Genomic_DNA.
DR EMBL; AY128295; AAM91103.1; -; mRNA.
DR PIR; H71427; H71427.
DR RefSeq; NP_193255.6; NM_117608.5.
DR RefSeq; NP_193330.3; NM_117687.2.
DR RefSeq; NP_193350.6; NM_117710.6.
DR RefSeq; NP_193443.4; NM_117814.4.
DR RefSeq; NP_680766.6; NM_148400.6.
DR AlphaFoldDB; O23463; -.
DR SMR; O23463; -.
DR BioGRID; 12599; 1.
DR STRING; 3702.AT4G16150.1; -.
DR iPTMnet; O23463; -.
DR PaxDb; O23463; -.
DR PeptideAtlas; O23463; -.
DR PRIDE; O23463; -.
DR ProteomicsDB; 220532; -.
DR GeneID; 3770328; -.
DR GeneID; 827184; -.
DR GeneID; 827277; -.
DR GeneID; 827305; -.
DR GeneID; 829687; -.
DR KEGG; ath:AT4G15200; -.
DR KEGG; ath:AT4G15950; -.
DR KEGG; ath:AT4G16150; -.
DR KEGG; ath:AT4G17100; -.
DR KEGG; ath:AT4G35335; -.
DR Araport; AT4G16150; -.
DR TAIR; locus:2130125; AT4G16150.
DR eggNOG; KOG0520; Eukaryota.
DR HOGENOM; CLU_316342_0_0_1; -.
DR InParanoid; O23463; -.
DR OrthoDB; 140796at2759; -.
DR PhylomeDB; O23463; -.
DR PRO; PR:O23463; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23463; baseline and differential.
DR Genevisible; O23463; 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:0043565; F:sequence-specific DNA binding; IDA:TAIR.
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: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 Pfam; PF12796; Ank_2; 1.
DR Pfam; PF03859; CG-1; 1.
DR Pfam; PF00612; IQ; 1.
DR SMART; SM00248; ANK; 1.
DR SMART; SM01076; CG-1; 1.
DR SMART; SM00015; IQ; 3.
DR SUPFAM; SSF48403; SSF48403; 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; 3.
PE 2: Evidence at transcript level;
KW Activator; ANK repeat; Calcium; Calmodulin-binding; Coiled coil;
KW DNA-binding; Nucleus; Reference proteome; Repeat; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..923
FT /note="Calmodulin-binding transcription activator 5"
FT /id="PRO_0000114490"
FT REPEAT 611..640
FT /note="ANK"
FT DOMAIN 757..786
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 799..828
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 875..904
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DNA_BIND 25..151
FT /note="CG-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00767"
FT REGION 272..372
FT /note="Transcription activation"
FT /evidence="ECO:0000269|PubMed:14581622"
FT REGION 824..846
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9FY74"
FT COILED 887..914
FT /evidence="ECO:0000255"
SQ SEQUENCE 923 AA; 104847 MW; AAA73F4A14E9A5DA CRC64;
MAGVDSGKLI GSEIHGFHTL QDLDIQTMLD EAYSRWLRPN EIHALLCNHK FFTINVKPVN
LPKSGTIVLF DRKMLRNFRK DGHNWKKKKD GKTIKEAHEH LKVGNEERIH VYYAHGEDTP
TFVRRCYWLL DKSQEHIVLV HYRETHEVHA APATPGNSYS SSITDHLSPK IVAEDTSSGV
HNTCNTGFEV RSNSLGSRNH EIRLHEINTL DWDELLVPAD ISNQSHPTEE DMLYFTEQLQ
TAPRGSVKQG NHLAGYNGSV DIPSFPGLED PVYQNNNSCG AGEFSSQHSH CGVDPNLQRR
DFSATVTDQP GDALLNNGYG SQDSFGRWVN NFISDSPGSV DDPSLEAVYT PGQDSSTPPT
VFHSHSDIPE QVFNITDVSP AWAYSTEKTK ILVTGFFHDS FQHLGRSNLI CICGELRVPA
EFLQMGVYRC FLPPQSPGVV NLYLSVDGNK PISQLFSFEH RSVQFIEKAI PQDDQLYKWE
EFEFQVRLAH LLFTSSNKIS VLTSKISPEN LLEAKKLASR TSHLLNSWAY LMKSIQANEV
PFDQARDHLF ELTLKNRLKE WLLEKVIENR NTKEYDSKGL GVIHLCAVLG YTWSILLFSW
ANISLDFRDK QGWTALHWAA YYGREKMVAA LLSAGARPNL VTDPTKEFLG GCTAADLAQQ
KGYDGLAAFL AEKCLVAQFK DMQTAGNISG NLETIKAEKS SNPGNANEEE QSLKDTLAAY
RTAAEAAARI QGAFREHELK VRSSAVRFAS KEEEAKNIIA AMKIQHAFRN FEVRRKIAAA
ARIQYRFQTW KMRREFLNMR KKAIRIQAAF RGFQVRRQYQ KITWSVGVLE KAILRWRLKR
KGFRGLQVSQ PDEKEGSEAV EDFYKTSQKQ AEERLERSVV KVQAMFRSKK AQQDYRRMKL
AHEEAQLEYD GMQELDQMAT EES
