PlantTFDB
Plant Transcription Factor Database
v4.0
Previous version: v1.0, v2.0, v3.0
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID AT5G09410.1
Common NameCAMTA1, CMTA1, EICBP.B, SR2, T5E8.210
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
Family CAMTA
Protein Properties Length: 989aa    MW: 111987 Da    PI: 6.2294
Description ethylene induced calmodulin binding protein
Gene Model
Gene Model ID Type Source Coding Sequence
AT5G09410.1genomeTAIRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1188.27.9e-59221392118
         CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrc 98 
                  l+e ++rwl+++ei++iL+n++k+++++e++trp sgsl+L++rk++ryfrkDG++w+kkkdgkt+rE+hekLKvg+++vl+cyYah+e n++fqrrc
  AT5G09410.1  22 LSEaQHRWLRPTEICEILQNYHKFHIASESPTRPASGSLFLFDRKVLRYFRKDGHNWRKKKDGKTIREAHEKLKVGSIDVLHCYYAHGEANENFQRRC 119
                  45559********************************************************************************************* PP

         CG-1  99 ywlLeeelekivlvhylevk 118
                  yw+Le++l +iv+vhylevk
  AT5G09410.1 120 YWMLEQHLMHIVFVHYLEVK 139
                  *****************985 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143784.84418144IPR005559CG-1 DNA-binding domain
SMARTSM010761.3E-8321139IPR005559CG-1 DNA-binding domain
PfamPF038592.5E-5124138IPR005559CG-1 DNA-binding domain
Gene3DG3DSA:2.60.40.101.1E-4369473IPR013783Immunoglobulin-like fold
PfamPF018331.1E-4394469IPR002909IPT domain
SuperFamilySSF812967.28E-15394480IPR014756Immunoglobulin E-set
PfamPF127963.3E-7576654IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.208.1E-18577689IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029719.624577688IPR020683Ankyrin repeat-containing domain
SuperFamilySSF484031.51E-18578688IPR020683Ankyrin repeat-containing domain
CDDcd002042.99E-14583686No hitNo description
SMARTSM002480.0029627656IPR002110Ankyrin repeat
PROSITE profilePS5008811.22627659IPR002110Ankyrin repeat
SMARTSM000158.6802824IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525402.02E-7803852IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.327803832IPR000048IQ motif, EF-hand binding site
PfamPF006120.0032806823IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0092825847IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.395826850IPR000048IQ motif, EF-hand binding site
PfamPF006124.3E-4828847IPR000048IQ motif, EF-hand binding site
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0045893Biological Processpositive regulation of transcription, DNA-templated
GO:0045944Biological Processpositive regulation of transcription from RNA polymerase II promoter
GO:0050826Biological Processresponse to freezing
GO:0005634Cellular Componentnucleus
GO:0001077Molecular Functiontranscriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding
GO:0005516Molecular Functioncalmodulin binding
GO:0043565Molecular Functionsequence-specific DNA binding
Plant Ontology ? help Back to Top
PO Term PO Category PO Description
PO:0000005anatomycultured plant cell
PO:0000013anatomycauline leaf
PO:0000037anatomyshoot apex
PO:0000230anatomyinflorescence meristem
PO:0000293anatomyguard cell
PO:0008019anatomyleaf lamina base
PO:0009001anatomyfruit
PO:0009005anatomyroot
PO:0009006anatomyshoot system
PO:0009009anatomyplant embryo
PO:0009010anatomyseed
PO:0009025anatomyvascular leaf
PO:0009029anatomystamen
PO:0009030anatomycarpel
PO:0009031anatomysepal
PO:0009032anatomypetal
PO:0009046anatomyflower
PO:0009047anatomystem
PO:0009052anatomyflower pedicel
PO:0020030anatomycotyledon
PO:0020038anatomypetiole
PO:0020100anatomyhypocotyl
PO:0020137anatomyleaf apex
PO:0025022anatomycollective leaf structure
PO:0025195anatomypollen tube cell
PO:0025281anatomypollen
PO:0001016developmental stageL mature pollen stage
PO:0001017developmental stageM germinated pollen stage
PO:0001054developmental stagevascular leaf senescent stage
PO:0001078developmental stageplant embryo cotyledonary stage
PO:0001081developmental stagemature plant embryo stage
PO:0001185developmental stageplant embryo globular stage
PO:0004507developmental stageplant embryo bilateral stage
PO:0007064developmental stageLP.12 twelve leaves visible stage
PO:0007095developmental stageLP.08 eight leaves visible stage
PO:0007098developmental stageLP.02 two leaves visible stage
PO:0007103developmental stageLP.10 ten leaves visible stage
PO:0007115developmental stageLP.04 four leaves visible stage
PO:0007123developmental stageLP.06 six leaves visible stage
PO:0007611developmental stagepetal differentiation and expansion stage
PO:0007616developmental stageflowering stage
Sequence ? help Back to Top
Protein Sequence    Length: 989 aa     Download sequence    Send to blast
MVDRRSFGSI TPPLQLDMEQ LLSEAQHRWL RPTEICEILQ NYHKFHIASE SPTRPASGSL  60
FLFDRKVLRY FRKDGHNWRK KKDGKTIREA HEKLKVGSID VLHCYYAHGE ANENFQRRCY  120
WMLEQHLMHI VFVHYLEVKG NRTSIGMKEN NSNSVNGTAS VNIDSTASPT STLSSLCEDA  180
DTGNRYGWTP APGMRNVSQV HGNRVRESDS QRLVDVRALD TVGNSLTRFH DQPYCNNLLT  240
QMQPSNTDSM LVEENSEKGG RLKAEHIRNP LQTQFNWQDD TDLALFEQSA QDNFETFSSL  300
LGSENLQPFG ISYQAPPSNM DSEYMPVMKI LRRSEDSLKK VDSFSKWAIK ELGEMEDLQM  360
QSSRGDIAWT TVECETAAAG ISLSPSLSED QRFTIVDFWP KSAKTDAEVE VMVIGTFLLS  420
PQEVTKYNWS CMFGEVEVPA EILVDGVLCC HAPPHTAGHV PFYVTCSNRF ACSEVREFDF  480
LSGSTQKINA TDVYGTYTNE ASLQLRFEKM LAHRDFVHEH HIFEDVGDKR RQISKIMLLK  540
EEKEYLLPGT YQRDSTKQEP KGQLFRELFE EELYIWLIHK VTEEGKGPNI LDEDGQGILH  600
FVAALGYDWA IKPVLAAGVN INFRDANGWS ALHWAAFSGR EETVAVLVSL GADAGALTDP  660
SPELPLGKTA ADLAYANGHR GISGFLAESS LTSYLEKLTV DSKENSPANS CGEKAVQTVS  720
ERTAAPMTYG DVPEKLSLKD SLTAVRNATQ AADRLHQVFR MQSFQRKQLC DIGDDEKIDI  780
SDQLAVSFAA SKTKNPGQGD VSLSCAATHI QKKYRGWKKR KEFLLIRQRI VKIQAHVRGH  840
QVRKQYRTVI WSVGLLEKII LRWRRKGNGL RGFKRNAVAK TVEPEPPVSA ICPRIPQEDE  900
YDYLKEGRKQ TEERLQKALT RVKSMVQYPE ARDQYRRLLT VVEGFRENEA SSSASINNKE  960
EEAVNCEEDD FIDIESLLND DTLMMSISP
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
At.267620.0flower| seed| silique
Expression -- Microarray ? help Back to Top
Source ID E-value
Genevisible245910_at0.0
Expression AtlasAT5G09410-
AtGenExpressAT5G09410-
ATTED-IIAT5G09410-
Expression -- Description ? help Back to Top
Source Description
UniprotTISSUE SPECIFICITY: Expressed in roots, stems, leaves, pollen and siliques. {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:14581622}.
Functional Description ? help Back to Top
Source Description
TAIRcalmodulin-binding protein, similar to another ethylene-upregulated calmodulin-binding protein ER1 GI:11612392 from (Nicotiana tabacum)
UniProtRegulates transcriptional activity in response to calcium signals. Binds to the consensus sequence 5'-[ACG]CGCG[GTC]-3'. Activates the expression of the V-PPase proton pump in pollen. {ECO:0000269|PubMed:11925432, ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:14581622}.
Function -- GeneRIF ? help Back to Top
  1. CAMTA1 regulates several stress responsive genes including RD26, ERD7, RAB18, LTPs, COR78, CBF1, HSPs etc. and promoter of these genes were enriched with CAMTA recognition cis-element.
    [PMID: 23547968]
  2. CAMTA1, CAMTA2 and CAMTA3 function together to inhibit salicylic acid biosynthesis at warm temperature (22 degrees C).CAMTA1, CAMTA2 and CAMTA3 function together to positively regulate CBF1, CBF2 and CBF3 and freezing tolerance.
    [PMID: 23581962]
Binding Motif ? help Back to Top
Motif ID Method Source Motif file
MP00501DAP27203113Download
Motif logo
Cis-element ? help Back to Top
SourceLink
PlantRegMapAT5G09410.1
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By temperature, UVB, salt, wounding, ethylene and methyl jasmonate. {ECO:0000269|PubMed:12218065}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieveRetrieve
Phenotype -- Mutation ? help Back to Top
Source ID
T-DNA ExpressAT5G09410
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAK2287400.0AK228740.1 Arabidopsis thaliana mRNA for Calmodulin-binding transcription activator 1, complete cds, clone: RAFL16-07-H14.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqNP_196503.30.0calmodulin-binding transcription activator 1
SwissprotQ9FY740.0CMTA1_ARATH; Calmodulin-binding transcription activator 1
TrEMBLF4KCL40.0F4KCL4_ARATH; Calmodulin-binding transcription activator 1
STRINGAT5G09410.30.0(Arabidopsis thaliana)
Publications ? help Back to Top
  1. Reddy AS,Reddy VS,Golovkin M
    A calmodulin binding protein from Arabidopsis is induced by ethylene and contains a DNA-binding motif.
    Biochem. Biophys. Res. Commun., 2000. 279(3): p. 762-9
    [PMID:11162426]
  2. Reddy VS,Ali GS,Reddy AS
    Genes encoding calmodulin-binding proteins in the Arabidopsis genome.
    J. Biol. Chem., 2002. 277(12): p. 9840-52
    [PMID:11782485]
  3. Bouch
    A novel family of calmodulin-binding transcription activators in multicellular organisms.
    J. Biol. Chem., 2002. 277(24): p. 21851-61
    [PMID:11925432]
  4. Yang T,Poovaiah BW
    A calmodulin-binding/CGCG box DNA-binding protein family involved in multiple signaling pathways in plants.
    J. Biol. Chem., 2002. 277(47): p. 45049-58
    [PMID:12218065]
  5. Mitsuda N,Isono T,Sato MH
    Arabidopsis CAMTA family proteins enhance V-PPase expression in pollen.
    Plant Cell Physiol., 2003. 44(10): p. 975-81
    [PMID:14581622]
  6. Kamauchi S,Nakatani H,Nakano C,Urade R
    Gene expression in response to endoplasmic reticulum stress in Arabidopsis thaliana.
    FEBS J., 2005. 272(13): p. 3461-76
    [PMID:15978049]
  7. Choi MS, et al.
    Isolation of a calmodulin-binding transcription factor from rice (Oryza sativa L.).
    J. Biol. Chem., 2005. 280(49): p. 40820-31
    [PMID:16192280]
  8. Laskowski M,Biller S,Stanley K,Kajstura T,Prusty R
    Expression profiling of auxin-treated Arabidopsis roots: toward a molecular analysis of lateral root emergence.
    Plant Cell Physiol., 2006. 47(6): p. 788-92
    [PMID:16621846]
  9. Wang Y, et al.
    Transcriptome analyses show changes in gene expression to accompany pollen germination and tube growth in Arabidopsis.
    Plant Physiol., 2008. 148(3): p. 1201-11
    [PMID:18775970]
  10. Doherty CJ,Van Buskirk HA,Myers SJ,Thomashow MF
    Roles for Arabidopsis CAMTA transcription factors in cold-regulated gene expression and freezing tolerance.
    Plant Cell, 2009. 21(3): p. 972-84
    [PMID:19270186]
  11. Galon Y, et al.
    Calmodulin-binding transcription activator 1 mediates auxin signaling and responds to stresses in Arabidopsis.
    Planta, 2010. 232(1): p. 165-78
    [PMID:20383645]
  12. Galon Y,Snir O,Fromm H
    How calmodulin binding transcription activators (CAMTAs) mediate auxin responses.
    Plant Signal Behav, 2010. 5(10): p. 1311-4
    [PMID:20930517]
  13. Tamura K,Fukao Y,Iwamoto M,Haraguchi T,Hara-Nishimura I
    Identification and characterization of nuclear pore complex components in Arabidopsis thaliana.
    Plant Cell, 2010. 22(12): p. 4084-97
    [PMID:21189294]
  14. Curran A, et al.
    Calcium-dependent protein kinases from Arabidopsis show substrate specificity differences in an analysis of 103 substrates.
    Front Plant Sci, 2011. 2: p. 36
    [PMID:22645532]
  15. Pandey N, et al.
    CAMTA 1 regulates drought responses in Arabidopsis thaliana.
    BMC Genomics, 2013. 14: p. 216
    [PMID:23547968]
  16. Kim Y,Park S,Gilmour SJ,Thomashow MF
    Roles of CAMTA transcription factors and salicylic acid in configuring the low-temperature transcriptome and freezing tolerance of Arabidopsis.
    Plant J., 2013. 75(3): p. 364-76
    [PMID:23581962]