CMTA6_ARATH
ID CMTA6_ARATH Reviewed; 838 AA.
AC Q9LSP8; F4J3Y2; Q56WD5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Calmodulin-binding transcription activator 6 {ECO:0000303|PubMed:11925432};
DE Short=AtCAMTA6 {ECO:0000303|PubMed:11925432};
DE AltName: Full=Ethylene-induced calmodulin-binding protein 5 {ECO:0000312|EMBL:AAR98748.1};
DE Short=EICBP5 {ECO:0000312|EMBL:AAR98748.1};
DE AltName: Full=Ethylene-induced calmodulin-binding protein e {ECO:0000303|PubMed:11782485};
DE Short=EICBP.e {ECO:0000303|PubMed:11782485};
DE AltName: Full=Signal-responsive protein 3 {ECO:0000303|PubMed:12218065};
DE Short=AtSR3 {ECO:0000303|PubMed:12218065};
GN Name=CAMTA6 {ECO:0000303|PubMed:11925432};
GN Synonyms=CMTA6 {ECO:0000305}, SR3 {ECO:0000303|PubMed:12218065};
GN OrderedLocusNames=At3g16940 {ECO:0000312|Araport:AT3G16940};
GN ORFNames=K14A17.5 {ECO:0000312|EMBL:BAA94977.1}, K14A17_6;
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 [MRNA] (ISOFORM 1).
RA Reddy V.S., Reddy A.S.N.;
RT "A calmodulin-binding protein from Arabidopsis.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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] OF 625-838 (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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, CALMODULIN-BINDING, 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.
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=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 [9]
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:12218065). 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 {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:12218065,
CC ECO:0000305|PubMed:11925432}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LSP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LSP8-2; Sequence=VSP_017016;
CC Name=3;
CC IsoId=Q9LSP8-3; Sequence=VSP_042264, VSP_017016;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, sepals, petals,
CC stamen filaments, top of carpels, anthers and siliques, but not in
CC stigmas. {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:14581622}.
CC -!- INDUCTION: By heat shock, UVB, salt, wounding, abscisic acid, H(2)O(2)
CC and salicylic acid. {ECO:0000269|PubMed:12218065}.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD95048.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY510027; AAR98748.1; -; mRNA.
DR EMBL; AB026636; BAA94977.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75886.1; -; Genomic_DNA.
DR EMBL; AK222107; BAD95048.1; ALT_INIT; mRNA.
DR RefSeq; NP_188319.2; NM_112570.4. [Q9LSP8-3]
DR AlphaFoldDB; Q9LSP8; -.
DR SMR; Q9LSP8; -.
DR STRING; 3702.AT3G16940.1; -.
DR iPTMnet; Q9LSP8; -.
DR PaxDb; Q9LSP8; -.
DR PeptideAtlas; Q9LSP8; -.
DR PRIDE; Q9LSP8; -.
DR EnsemblPlants; AT3G16940.1; AT3G16940.1; AT3G16940. [Q9LSP8-3]
DR GeneID; 820950; -.
DR Gramene; AT3G16940.1; AT3G16940.1; AT3G16940. [Q9LSP8-3]
DR KEGG; ath:AT3G16940; -.
DR Araport; AT3G16940; -.
DR TAIR; locus:2086172; AT3G16940.
DR eggNOG; KOG0520; Eukaryota.
DR HOGENOM; CLU_005708_1_0_1; -.
DR InParanoid; Q9LSP8; -.
DR PhylomeDB; Q9LSP8; -.
DR PRO; PR:Q9LSP8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSP8; baseline and differential.
DR Genevisible; Q9LSP8; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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:0009651; P:response to salt stress; 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; IPR002909; IPT_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
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; 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 1: Evidence at protein level;
KW Activator; Alternative splicing; ANK repeat; Calcium; Calmodulin-binding;
KW Coiled coil; DNA-binding; Nucleus; Reference proteome; Repeat;
KW Stress response; Transcription.
FT CHAIN 1..838
FT /note="Calmodulin-binding transcription activator 6"
FT /id="PRO_0000114491"
FT REPEAT 525..554
FT /note="ANK"
FT DOMAIN 671..700
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 713..742
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 788..817
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DNA_BIND 25..134
FT /note="CG-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00767"
FT REGION 738..760
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:12218065"
FT COILED 802..822
FT /evidence="ECO:0000255"
FT VAR_SEQ 47
FT /note="C -> YNPKYFTINVKPVNLPNS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042264"
FT VAR_SEQ 820..838
FT /note="VNHLTFLNLSFGKKNSNRR -> LEYGCLEDI (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_017016"
SQ SEQUENCE 838 AA; 95382 MW; A5DE9C698E633900 CRC64;
MDGDGLGRLI GSEIHGFHTL QDLDVQTMLE EAKSRWLRPN EIHAILCGRI ILFDRKMLRN
FRKDGHNWKK KKDGRTVKEA HEHLKVGNEE RIHVYYAHGE DNTTFVRRCY WLLDKARENI
VLVHYRDTQE AATTSGDSIS SPISVSEQTF PNRVAAEDID TVVRNHDISL HDINTLDWDE
LLVPTDLNNQ SAPTVDNLSY FTEPLQNAAN GTAEHGNATV ADGSLDALLN DGPQSRESFG
RWMNSFISES NGSLEDPSFE PMVMPRQDPL APQAVFHSHS NIPEQVFNIT DVSPAWAYSS
EKTKILVTGF LHDSYQHLER SNLYCVCGDF CVPAEYLQAG VYRCIIPPHS PGMVNLYLSA
DGHKPISQCF RFEHRAVPVL DKTVPEDNQD SKWEEFEFQV RLSHLLFTSS NKLNVLSSKI
SPHNLRDAKK LASKTNHLLN SWAYLVKSIQ GNKVSFDQAK DHLFELSLKN RLKEWLMEKV
LEGRNTLDYD SKGLGVIHLC ASLGYTWSVQ LFSLSGLSLN FRDKQGWTAL HWAAYYGREK
MVAALLSAGA RPNLVTDSTK DNLGGCMAAD LAQQNGYDGL AAYLAEKCLV AQFRDMKIAG
NITGDLEACK AEMLNQGTLP EDEQSLKDAL AAYRTAAEAA ARIQGAFREK ALKAARSSVI
QFANKEEEAK SIIAAMKIQN AFRKYDTRRK IEAAYRIQCR FQTWKIRREY LNMRRQAIRI
QAAFRGLQAR RQYKKILWSV GVLEKAVLRW RQKRKGFRGL QVAAEEDSPG EAQEDFYKTS
QRQAEERLER SVVRVQAMFR SKKAQQDYRR MKLTHEEAQV NHLTFLNLSF GKKNSNRR
