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CMTA2_ARATH
ID   CMTA2_ARATH             Reviewed;        1050 AA.
AC   Q6NPP4; Q0WNN4; Q9FMG3;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Calmodulin-binding transcription activator 2 {ECO:0000303|PubMed:11925432};
DE            Short=AtCAMTA2 {ECO:0000303|PubMed:11925432};
DE   AltName: Full=AtER66 {ECO:0000303|PubMed:11162426};
DE   AltName: Full=Ethylene-induced calmodulin-binding protein c {ECO:0000303|PubMed:11782485};
DE            Short=EICBP.c {ECO:0000303|PubMed:11782485};
DE   AltName: Full=Signal-responsive protein 4 {ECO:0000303|PubMed:12218065};
DE            Short=AtSR4 {ECO:0000303|PubMed:12218065};
GN   Name=CAMTA2 {ECO:0000303|PubMed:11925432};
GN   Synonyms=CMTA2 {ECO:0000305}, SR4 {ECO:0000303|PubMed:12218065};
GN   OrderedLocusNames=At5g64220 {ECO:0000312|Araport:AT5G64220};
GN   ORFNames=MSJ1.6 {ECO:0000312|EMBL:BAB09853.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA   Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA   Shinozaki K., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA   Takagi M.;
RT   "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984,
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984, 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   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23581962; DOI=10.1111/tpj.12205;
RA   Kim Y., Park S., Gilmour S.J., Thomashow M.F.;
RT   "Roles of CAMTA transcription factors and salicylic acid in configuring the
RT   low-temperature transcriptome and freezing tolerance of Arabidopsis.";
RL   Plant J. 75:364-376(2013).
RN   [14]
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   [15]
RP   FUNCTION, AND INDUCTION BY ALUMINUM.
RX   PubMed=25627216; DOI=10.1104/pp.114.256552;
RA   Tokizawa M., Kobayashi Y., Saito T., Kobayashi M., Iuchi S., Nomoto M.,
RA   Tada Y., Yamamoto Y.Y., Koyama H.;
RT   "SENSITIVE TO PROTON RHIZOTOXICITY1, CALMODULIN BINDING TRANSCRIPTION
RT   ACTIVATOR2, and other transcription factors are involved in ALUMINUM-
RT   ACTIVATED MALATE TRANSPORTER1 expression.";
RL   Plant Physiol. 167:991-1003(2015).
RN   [16]
RP   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 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 in freezing tolerance in association with CAMTA1 and CAMTA3.
CC       Contributes together with CAMTA1 and CAMTA3 to the positive regulation
CC       of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and
CC       DREB1C/CBF2 (PubMed:23581962). Involved together with CAMTA3 and CAMTA4
CC       in the positive regulation of a general stress response
CC       (PubMed:25039701). Involved in tolerance to aluminum. Binds to the
CC       promoter of ALMT1 transporter and contributes to the positive
CC       regulation of aluminum-induced expression of ALMT1 (PubMed:25627216).
CC       {ECO:0000250|UniProtKB:Q8GSA7, ECO:0000269|PubMed:23581962,
CC       ECO:0000269|PubMed:25039701, ECO:0000269|PubMed:25627216,
CC       ECO:0000305|PubMed:11925432}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767,
CC       ECO:0000269|PubMed:19245862, ECO:0000269|PubMed:28351986}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, old leaves, petals,
CC       sepals, top of carpels, stigmas, stamen filaments, anthers and
CC       siliques, but not in pollen. {ECO:0000269|PubMed:12218065,
CC       ECO:0000269|PubMed:14581622}.
CC   -!- INDUCTION: By salt, wounding, abscisic acid, H(2)O(2) and salicylic
CC       acid (PubMed:12218065). Induced by aluminum (PubMed:25627216).
CC       {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:25627216}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but the double mutants camt2 and camt3 exhibit dwarf
CC       phenotypes. {ECO:0000269|PubMed:23581962}.
CC   -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB008268; BAB09853.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED97856.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97857.1; -; Genomic_DNA.
DR   EMBL; BT010874; AAR24652.1; -; mRNA.
DR   EMBL; AK229403; BAF01265.1; -; mRNA.
DR   EMBL; AB493811; BAH30649.1; -; mRNA.
DR   RefSeq; NP_001032135.1; NM_001037058.2.
DR   RefSeq; NP_201227.3; NM_125818.3.
DR   AlphaFoldDB; Q6NPP4; -.
DR   STRING; 3702.AT5G64220.2; -.
DR   iPTMnet; Q6NPP4; -.
DR   PaxDb; Q6NPP4; -.
DR   PRIDE; Q6NPP4; -.
DR   ProteomicsDB; 220479; -.
DR   EnsemblPlants; AT5G64220.1; AT5G64220.1; AT5G64220.
DR   EnsemblPlants; AT5G64220.2; AT5G64220.2; AT5G64220.
DR   GeneID; 836543; -.
DR   Gramene; AT5G64220.1; AT5G64220.1; AT5G64220.
DR   Gramene; AT5G64220.2; AT5G64220.2; AT5G64220.
DR   KEGG; ath:AT5G64220; -.
DR   Araport; AT5G64220; -.
DR   TAIR; locus:2173368; AT5G64220.
DR   eggNOG; KOG0520; Eukaryota.
DR   HOGENOM; CLU_005708_1_0_1; -.
DR   InParanoid; Q6NPP4; -.
DR   OMA; WDASFEN; -.
DR   OrthoDB; 89428at2759; -.
DR   PhylomeDB; Q6NPP4; -.
DR   PRO; PR:Q6NPP4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q6NPP4; baseline and differential.
DR   Genevisible; Q6NPP4; 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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0071275; P:cellular response to aluminum ion; IEP:TAIR.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP: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: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; 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   SMART; SM00248; ANK; 2.
DR   SMART; SM01076; CG-1; 1.
DR   SMART; SM00015; IQ; 2.
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; 2.
DR   PROSITE; PS51437; CG_1; 1.
DR   PROSITE; PS50096; IQ; 2.
PE   1: Evidence at protein level;
KW   Activator; ANK repeat; Calcium; Calmodulin-binding; Coiled coil;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Stress response; Transcription; Transcription regulation.
FT   CHAIN           1..1050
FT                   /note="Calmodulin-binding transcription activator 2"
FT                   /id="PRO_0000114487"
FT   REPEAT          661..690
FT                   /note="ANK 1"
FT   REPEAT          694..723
FT                   /note="ANK 2"
FT   DOMAIN          870..899
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          893..922
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DNA_BIND        15..141
FT                   /note="CG-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00767"
FT   REGION          141..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          918..940
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FY74"
FT   COILED          957..985
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        141..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         984
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862,
FT                   ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   1050 AA;  117258 MW;  318050B641D646F9 CRC64;
     MADRGSFGFA PRLDIKQLLS EAQHRWLRPA EICEILRNHQ KFHIASEPPN RPPSGSLFLF
     DRKVLRYFRK DGHNWRKKKD GKTVKEAHEK LKVGSIDVLH CYYAHGEDNE NFQRRCYWML
     EQDLMHIVFV HYLEVKGNRM STSGTKENHS NSLSGTGSVN VDSTATRSSI LSPLCEDADS
     GDSRQASSSL QQNPEPQTVV PQIMHHQNAS TINSYNTTSV LGNRDGWTSA HGNRVKGSNS
     QRSGDVPAWD ASFENSLARY QNLPYNAPLT QTQPSTFGLI PMEGKTEKGS LLTSEHLRNP
     LQSQVNWQTP VQESVPLQKW PMDSHSGMTD ATDLALFGQG AHENFGTFSS LLGSQDQQSS
     SFQAPFTNNE AAYIPKLGPE DLIYEASANQ TLPLRKALLK KEDSLKKVDS FSRWVSKELG
     EMEDLQMQSS SGGIAWTSVE CENAAAGSSL SPSLSEDQRF TMIDFWPKWT QTDSEVEVMV
     IGTFLLSPQE VTSYSWSCMF GEVEVPADIL VDGVLCCHAP PHEVGRVPFY ITCSDRFSCS
     EVREFDFLPG STRKLNATDI YGANTIETSL HLRFENLLAL RCSVQEHHIF ENVGEKRRKI
     SKIMLLKDEK EPPLPGTIEK DLTELEAKER LIREEFEDKL YLWLIHKVTE EGKGPNILDE
     DGQGVLHLAA ALGYDWAIKP ILAAGVSINF RDANGWSALH WAAFSGREDT VAVLVSLGAD
     AGALADPSPE HPLGKTAADL AYGNGHRGIS GFLAESSLTS YLEKLTVDAK ENSSADSSGA
     KAVLTVAERT ATPMSYGDVP ETLSMKDSLT AVLNATQAAD RLHQVFRMQS FQRKQLSELG
     GDNKFDISDE LAVSFAAAKT KKSGHSSGAV HAAAVQIQKK YRGWKKRKEF LLIRQRIVKI
     QAHVRGHQVR KQYRAIIWSV GLLEKIILRW RRKGSGLRGF KRDTISKPTE PVCPAPQEDD
     YDFLKEGRKQ TEERLQKALT RVKSMAQYPE ARAQYRRLLT VVEGFRENEA SSSSALKNNT
     EEAANYNEED DLIDIDSLLD DDTFMSLAFE
 
 
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