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 AT5G64220.2
Common NameCAMTA2, CMTA2, MSJ1.6, SR4
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: 1050aa    MW: 117258 Da    PI: 6.3873
Description Calmodulin-binding transcription activator protein with CG-1 and Ankyrin domains
Gene Model
Gene Model ID Type Source Coding Sequence
AT5G64220.2genomeTAIRView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1CG-1188.37.7e-59191362118
         CG-1   2 lke.kkrwlkneeiaaiLenfekheltlelktrpksgsliLynrkkvryfrkDGyswkkkkdgktvrEdhekLKvggvevlycyYahseenptfqrrc 98 
                  l+e ++rwl++ ei++iL n++k+++++e+++rp+sgsl+L++rk++ryfrkDG++w+kkkdgktv+E+hekLKvg+++vl+cyYah+e+n++fqrrc
  AT5G64220.2  19 LSEaQHRWLRPAEICEILRNHQKFHIASEPPNRPPSGSLFLFDRKVLRYFRKDGHNWRKKKDGKTVKEAHEKLKVGSIDVLHCYYAHGEDNENFQRRC 116
                  45559********************************************************************************************* PP

         CG-1  99 ywlLeeelekivlvhylevk 118
                  yw+Le++l +iv+vhylevk
  AT5G64220.2 117 YWMLEQDLMHIVFVHYLEVK 136
                  *****************985 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
PROSITE profilePS5143786.27515141IPR005559CG-1 DNA-binding domain
SMARTSM010763.6E-8718136IPR005559CG-1 DNA-binding domain
PfamPF038598.4E-5221135IPR005559CG-1 DNA-binding domain
SuperFamilySSF812966.65E-13463547IPR014756Immunoglobulin E-set
SuperFamilySSF484032.02E-19642755IPR020683Ankyrin repeat-containing domain
PROSITE profilePS5029720.022644755IPR020683Ankyrin repeat-containing domain
Gene3DG3DSA:1.25.40.201.2E-18645756IPR020683Ankyrin repeat-containing domain
PfamPF127964.5E-8645721IPR020683Ankyrin repeat-containing domain
CDDcd002042.22E-15650753No hitNo description
PROSITE profilePS500889.458661693IPR002110Ankyrin repeat
SMARTSM002481000661690IPR002110Ankyrin repeat
PROSITE profilePS5008810.873694726IPR002110Ankyrin repeat
SMARTSM002480.0029694723IPR002110Ankyrin repeat
SMARTSM000150.32869891IPR000048IQ motif, EF-hand binding site
SuperFamilySSF525401.17E-7870919IPR027417P-loop containing nucleoside triphosphate hydrolase
PROSITE profilePS500967.858871899IPR000048IQ motif, EF-hand binding site
PfamPF006120.002871890IPR000048IQ motif, EF-hand binding site
SMARTSM000150.0092892914IPR000048IQ motif, EF-hand binding site
PROSITE profilePS500969.304893917IPR000048IQ motif, EF-hand binding site
PfamPF006124.6E-4895914IPR000048IQ motif, EF-hand binding site
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0009409Biological Processresponse to cold
GO:0045893Biological Processpositive regulation of transcription, DNA-templated
GO:0045944Biological Processpositive regulation of transcription from RNA polymerase II promoter
GO:0071275Biological Processcellular response to aluminum ion
GO:0005634Cellular Componentnucleus
GO:0001077Molecular Functiontranscriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA 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: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:0025281anatomypollen
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: 1050 aa     Download sequence    Send to blast
MADRGSFGFA PRLDIKQLLS EAQHRWLRPA EICEILRNHQ KFHIASEPPN RPPSGSLFLF  60
DRKVLRYFRK DGHNWRKKKD GKTVKEAHEK LKVGSIDVLH CYYAHGEDNE NFQRRCYWML  120
EQDLMHIVFV HYLEVKGNRM STSGTKENHS NSLSGTGSVN VDSTATRSSI LSPLCEDADS  180
GDSRQASSSL QQNPEPQTVV PQIMHHQNAS TINSYNTTSV LGNRDGWTSA HGNRVKGSNS  240
QRSGDVPAWD ASFENSLARY QNLPYNAPLT QTQPSTFGLI PMEGKTEKGS LLTSEHLRNP  300
LQSQVNWQTP VQESVPLQKW PMDSHSGMTD ATDLALFGQG AHENFGTFSS LLGSQDQQSS  360
SFQAPFTNNE AAYIPKLGPE DLIYEASANQ TLPLRKALLK KEDSLKKVDS FSRWVSKELG  420
EMEDLQMQSS SGGIAWTSVE CENAAAGSSL SPSLSEDQRF TMIDFWPKWT QTDSEVEVMV  480
IGTFLLSPQE VTSYSWSCMF GEVEVPADIL VDGVLCCHAP PHEVGRVPFY ITCSDRFSCS  540
EVREFDFLPG STRKLNATDI YGANTIETSL HLRFENLLAL RCSVQEHHIF ENVGEKRRKI  600
SKIMLLKDEK EPPLPGTIEK DLTELEAKER LIREEFEDKL YLWLIHKVTE EGKGPNILDE  660
DGQGVLHLAA ALGYDWAIKP ILAAGVSINF RDANGWSALH WAAFSGREDT VAVLVSLGAD  720
AGALADPSPE HPLGKTAADL AYGNGHRGIS GFLAESSLTS YLEKLTVDAK ENSSADSSGA  780
KAVLTVAERT ATPMSYGDVP ETLSMKDSLT AVLNATQAAD RLHQVFRMQS FQRKQLSELG  840
GDNKFDISDE LAVSFAAAKT KKSGHSSGAV HAAAVQIQKK YRGWKKRKEF LLIRQRIVKI  900
QAHVRGHQVR KQYRAIIWSV GLLEKIILRW RRKGSGLRGF KRDTISKPTE PVCPAPQEDD  960
YDFLKEGRKQ TEERLQKALT RVKSMAQYPE ARAQYRRLLT VVEGFRENEA SSSSALKNNT  1020
EEAANYNEED DLIDIDSLLD DDTFMSLAFE
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
At.289630.0flower| root| silique
Expression -- Microarray ? help Back to Top
Source ID E-value
Genevisible247270_at0.0
Expression AtlasAT5G64220-
AtGenExpressAT5G64220-
ATTED-IIAT5G64220-
Expression -- Description ? help Back to Top
Source Description
UniprotTISSUE SPECIFICITY: Expressed in roots, stems, old leaves, petals, sepals, top of carpels, stigmas, stamen filaments, anthers and siliques, but not in pollen. {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:14581622}.
Functional Description ? help Back to Top
Source Description
UniProtRegulates transcriptional activity in response to calcium signals. Binds to the consensus sequence 5'-[ACG]CGCG[GTC]-3'. {ECO:0000269|PubMed:11925432, ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:14581622}.
Function -- GeneRIF ? help Back to Top
  1. 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]
  2. CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR2 was found to be an activator of AtALMT1 expression.
    [PMID: 25627216]
Binding Motif ? help Back to Top
Motif ID Method Source Motif file
MP00043PBM25215497Download
Motif logo
Cis-element ? help Back to Top
SourceLink
PlantRegMapAT5G64220.2
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By salt, wounding, abscisic acid, H(2)O(2) and salicylic acid. {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 ExpressAT5G64220
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankBT0108740.0BT010874.1 Arabidopsis thaliana At5g64220 gene, complete cds.
GenBankAK2294030.0AK229403.1 Arabidopsis thaliana mRNA for Calmodulin-binding transcription activator 2, complete cds, clone: RAFL16-66-C08.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqNP_001032135.10.0calmodulin-binding transcription activator 2
RefseqNP_201227.30.0calmodulin-binding transcription activator 2
SwissprotQ6NPP40.0CMTA2_ARATH; Calmodulin-binding transcription activator 2
TrEMBLQ0WNN40.0Q0WNN4_ARATH; Calmodulin-binding transcription activator 2
STRINGAT5G64220.10.0(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. 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]
  7. Jones AM, et al.
    Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana.
    J Proteomics, 2009. 72(3): p. 439-51
    [PMID:19245862]
  8. Reiland S, et al.
    Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks.
    Plant Physiol., 2009. 150(2): p. 889-903
    [PMID:19376835]
  9. 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]
  10. Tokizawa M, et al.
    SENSITIVE TO PROTON RHIZOTOXICITY1, CALMODULIN BINDING TRANSCRIPTION ACTIVATOR2, and other transcription factors are involved in ALUMINUM-ACTIVATED MALATE TRANSPORTER1 expression.
    Plant Physiol., 2015. 167(3): p. 991-1003
    [PMID:25627216]