CMTA4_ARATH
ID CMTA4_ARATH Reviewed; 1016 AA.
AC Q9FYG2;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Calmodulin-binding transcription activator 4 {ECO:0000303|PubMed:11925432};
DE Short=AtCAMTA4 {ECO:0000303|PubMed:11925432};
DE AltName: Full=AtFIN21 {ECO:0000303|PubMed:11162426};
DE AltName: Full=Ethylene-induced calmodulin-binding protein 4 {ECO:0000312|EMBL:AAR98747.1};
DE Short=EICBP4 {ECO:0000312|EMBL:AAR98747.1};
DE AltName: Full=Ethylene-induced calmodulin-binding protein d {ECO:0000303|PubMed:11782485};
DE Short=EICBP.d {ECO:0000303|PubMed:11782485};
DE AltName: Full=Signal-responsive protein 5 {ECO:0000303|PubMed:12218065};
DE Short=AtSR5 {ECO:0000303|PubMed:12218065};
GN Name=CAMTA4 {ECO:0000303|PubMed:11925432};
GN Synonyms=CMTA4 {ECO:0000305}, SR5 {ECO:0000303|PubMed:12218065};
GN OrderedLocusNames=At1g67310 {ECO:0000312|Araport:AT1G67310};
GN ORFNames=F1N21.13 {ECO:0000312|EMBL:AAG00250.1};
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 [MRNA].
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
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 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-935, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [9]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-935,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP FUNCTION.
RX PubMed=25039701; DOI=10.1111/tpj.12620;
RA Benn G., Wang C.Q., Hicks D.R., Stein J., Guthrie C., Dehesh K.;
RT "A key general stress response motif is regulated non-uniformly by CAMTA
RT transcription factors.";
RL Plant J. 80:82-92(2014).
RN [12]
RP INDUCTION BY COLD.
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 that 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 Binds calmodulin in a calcium-dependent manner (By similarity).
CC Involved together with CAMTA2 and CAMTA3 in the positive regulation of
CC a general stress response (PubMed:25039701).
CC {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:25039701,
CC ECO:0000305|PubMed:11925432}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767,
CC ECO:0000269|PubMed:19245862}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:12218065}.
CC -!- INDUCTION: By heat shock, UVB, salt, wounding, ethylene, methyl
CC jasmonate, abscisic acid, H(2)O(2) and salicylic acid
CC (PubMed:12218065). Induced by cold stress (PubMed:28351986).
CC {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:28351986}.
CC -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}.
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DR EMBL; AY510026; AAR98747.1; -; mRNA.
DR EMBL; AC002130; AAG00250.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34626.1; -; Genomic_DNA.
DR RefSeq; NP_176899.2; NM_105399.2.
DR AlphaFoldDB; Q9FYG2; -.
DR SMR; Q9FYG2; -.
DR BioGRID; 28272; 1.
DR STRING; 3702.AT1G67310.1; -.
DR iPTMnet; Q9FYG2; -.
DR PaxDb; Q9FYG2; -.
DR PRIDE; Q9FYG2; -.
DR ProteomicsDB; 241235; -.
DR EnsemblPlants; AT1G67310.1; AT1G67310.1; AT1G67310.
DR GeneID; 843051; -.
DR Gramene; AT1G67310.1; AT1G67310.1; AT1G67310.
DR KEGG; ath:AT1G67310; -.
DR Araport; AT1G67310; -.
DR TAIR; locus:2019534; AT1G67310.
DR eggNOG; KOG0520; Eukaryota.
DR HOGENOM; CLU_005708_1_0_1; -.
DR InParanoid; Q9FYG2; -.
DR OMA; ESAWACM; -.
DR OrthoDB; 140171at2759; -.
DR PhylomeDB; Q9FYG2; -.
DR PRO; PR:Q9FYG2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FYG2; baseline and differential.
DR Genevisible; Q9FYG2; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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 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 InterPro; IPR027417; P-loop_NTPase.
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; 2.
DR SMART; SM01076; CG-1; 1.
DR SMART; SM00015; IQ; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 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; ANK repeat; Calcium; Calmodulin-binding; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..1016
FT /note="Calmodulin-binding transcription activator 4"
FT /id="PRO_0000114489"
FT REPEAT 647..676
FT /note="ANK 1"
FT REPEAT 680..709
FT /note="ANK 2"
FT REPEAT 719..748
FT /note="ANK 3"
FT DOMAIN 798..827
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 855..884
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 878..907
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DNA_BIND 38..164
FT /note="CG-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00767"
FT REGION 324..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..925
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9FY74"
FT COMPBIAS 324..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 1016 AA; 113064 MW; 006C87DAA303D08F CRC64;
MSSVAEDNSF TCDIATIFVA ICRNPPANPS DSLFQYEIST LYQEAHSRWL KPPEVLFILQ
NHESLTLTNT APQRPTSGSL LLFNKRVLKF FRKDGHQWRR KRDGRAIAEA HERLKVGNAE
ALNCYYAHGE QDPTFRRRIY WMLDPEYEHI VLVHYRDVSE REEGQQTGGQ VYQFAPILST
QNVSYNQYIG DSSDIYQQSS TSPGVAEVNS NLEGSASSSE FGQALKMLKE QLSIGDEHVN
SVDPHYIQPE SLDSLQFLEY SDIDHLAQPT TVYQRPENNK LERCYGGNFG AQYSAKNDSN
KLERCYGGYV GGAEYHSSNL MLVKNGSGPS GGTGGSGDQG SESWKDVLEA CEASIPLNSE
GSTPSSAKGL LAGLQEDSNW SYSNQVDQST FLLPQDLGSF QLPASYSALV APENNGEYCG
MMEDGMKIGL PFEQEMRVTG AHNQKFTIQD ISPDWGYANE TTKVIIIGSF LCDPTESTWS
CMFGNAQVPF EIIKEGVIRC EAPQCGPGKV NLCITSGDGL LCSEIREFEY REKPDTCCPK
CSEPQTSDMS TSPNELILLV RFVQTLLSDR SSERKSNLES GNDKLLTKLK ADDDQWRHVI
GTIIDGSASS TSTVDWLLQE LLKDKLDTWL SSRSCDEDYI TCSLSKQEQG IIHMVAGLGF
EWAFYPILAH GVNVDFRDIK GWSALHWAAQ FGSEKMVAAL IASGASAGAV TDPSRQDPNG
KTAASIAASN GHKGLAGYLS EVALTNHLSS LTLEETENSK DTAQVQTEKT LNSISEQSPS
GNEDQVSLKD TLAAVRNAAQ AAARIQAAFR AHSFRKRKQR EAALVACLQE YGMYCEDIEG
ISAMSKLTFG KGRNYNSAAL SIQKNFRGYK DRKCFLELRQ KVVKIQAHVR GYQIRKNYKV
ICWAVRILDK VVLRWRRKGV GLRGFRQDVE STEDSEDEDI LKVFRKQKVD VAVNEAFSRV
LSMSNSPEAR QQYHRVLKRY CQTKAELGKT ETLVGEDDDG LFDIADMEYD TLFSLP
