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CMTA1_ARATH
ID   CMTA1_ARATH             Reviewed;        1007 AA.
AC   Q9FY74; F4KCL6; Q0WQF9;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=Calmodulin-binding transcription activator 1 {ECO:0000303|PubMed:11925432};
DE            Short=AtCAMTA1 {ECO:0000303|PubMed:11925432};
DE   AltName: Full=Ethylene-induced calmodulin-binding protein b {ECO:0000303|PubMed:11782485};
DE            Short=EICBP.b {ECO:0000303|PubMed:11782485};
DE   AltName: Full=Signal-responsive protein 2 {ECO:0000303|PubMed:12218065};
DE            Short=AtSR2 {ECO:0000303|PubMed:12218065};
GN   Name=CAMTA1 {ECO:0000303|PubMed:11925432};
GN   Synonyms=CMTA1 {ECO:0000305}, SR2 {ECO:0000303|PubMed:12218065};
GN   OrderedLocusNames=At5g09410 {ECO:0000312|Araport:AT5G09410};
GN   ORFNames=T5E8.210 {ECO:0000312|EMBL:CAC05467.1};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
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] (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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, CALMODULIN-BINDING, GENE FAMILY, AND
RP   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   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   [6]
RP   FUNCTION, AND 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   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19270186; DOI=10.1105/tpc.108.063958;
RA   Doherty C.J., Van Buskirk H.A., Myers S.J., Thomashow M.F.;
RT   "Roles for Arabidopsis CAMTA transcription factors in cold-regulated gene
RT   expression and freezing tolerance.";
RL   Plant Cell 21:972-984(2009).
RN   [8]
RP   FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20383645; DOI=10.1007/s00425-010-1153-6;
RA   Galon Y., Aloni R., Nachmias D., Snir O., Feldmesser E., Scrase-Field S.,
RA   Boyce J.M., Bouche N., Knight M.R., Fromm H.;
RT   "Calmodulin-binding transcription activator 1 mediates auxin signaling and
RT   responds to stresses in Arabidopsis.";
RL   Planta 232:165-178(2010).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23547968; DOI=10.1186/1471-2164-14-216;
RA   Pandey N., Ranjan A., Pant P., Tripathi R.K., Ateek F., Pandey H.P.,
RA   Patre U.V., Sawant S.V.;
RT   "CAMTA 1 regulates drought responses in Arabidopsis thaliana.";
RL   BMC Genomics 14:216-216(2013).
RN   [10]
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   [11]
RP   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   [12]
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   [13]
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:11925432). 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       Involved in freezing tolerance (PubMed:19270186). Involved in freezing
CC       tolerance in association with CAMTA2 and CAMTA3. Contributes together
CC       with CAMTA2 and CAMTA3 to the positive regulation of the cold-induced
CC       expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2
CC       (PubMed:23581962). Involved in drought stress responses by regulating
CC       several drought-responsive genes (PubMed:23547968). Involved in auxin
CC       signaling and responses to abiotic stresses (PubMed:20383645).
CC       Activates the expression of the V-PPase proton pump AVP1 in pollen
CC       (PubMed:14581622). {ECO:0000250|UniProtKB:Q8GSA7,
CC       ECO:0000269|PubMed:11925432, ECO:0000269|PubMed:14581622,
CC       ECO:0000269|PubMed:19270186, ECO:0000269|PubMed:20383645,
CC       ECO:0000269|PubMed:23547968, ECO:0000269|PubMed:23581962,
CC       ECO:0000305|PubMed:11925432}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767,
CC       ECO:0000269|PubMed:11925432}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FY74-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FY74-2; Sequence=VSP_040640;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, pollen and
CC       siliques. {ECO:0000269|PubMed:12218065, ECO:0000269|PubMed:14581622}.
CC   -!- DEVELOPMENTAL STAGE: During leaf developlement, expressed in young leaf
CC       primordia, hydathodes of young leaf tips, hydathodes of the lobes in
CC       maturating leaves and lamina within the minor veins in adult leaves.
CC       During flower development, expressed in developing stamens, germinating
CC       pollen grains, ovules and developing seeds.
CC       {ECO:0000269|PubMed:20383645}.
CC   -!- INDUCTION: Induced by UVB, wounding, ethylene and methyl jasmonate
CC       (PubMed:12218065). Induced by salt stress and heat shock
CC       (PubMed:12218065, PubMed:20383645). Induced by aluminum
CC       (PubMed:25627216). {ECO:0000269|PubMed:12218065,
CC       ECO:0000269|PubMed:20383645, ECO:0000269|PubMed:25627216}.
CC   -!- DOMAIN: The two IQ domains are probably not interacting with
CC       calcium/calmodulin.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant seedling are hyper-responsive to auxin in
CC       hypocotyl growth inhibition (PubMed:20383645). No visible phenotype
CC       under normal growth conditions, but mutant seedling exhibit reduced
CC       drought tolerance (PubMed:23547968). No visible phenotype under normal
CC       growth conditions, but the double mutants camta1 and camta3 are
CC       impaired in freezing tolerance (PubMed:19270186). No visible phenotype
CC       under normal growth conditions, but the double mutants camt1 and camt3
CC       exhibit semi-dwarf phenotypes (PubMed:19270186, PubMed:23581962).
CC       {ECO:0000269|PubMed:19270186, ECO:0000269|PubMed:20383645,
CC       ECO:0000269|PubMed:23547968, ECO:0000269|PubMed:23581962}.
CC   -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}.
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DR   EMBL; AL391712; CAC05467.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91388.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91389.1; -; Genomic_DNA.
DR   EMBL; AK228740; BAF00640.1; -; mRNA.
DR   RefSeq; NP_001119195.1; NM_001125723.2. [Q9FY74-1]
DR   RefSeq; NP_196503.3; NM_120978.5. [Q9FY74-2]
DR   AlphaFoldDB; Q9FY74; -.
DR   SMR; Q9FY74; -.
DR   BioGRID; 16078; 1.
DR   STRING; 3702.AT5G09410.3; -.
DR   iPTMnet; Q9FY74; -.
DR   PRIDE; Q9FY74; -.
DR   EnsemblPlants; AT5G09410.1; AT5G09410.1; AT5G09410. [Q9FY74-2]
DR   EnsemblPlants; AT5G09410.2; AT5G09410.2; AT5G09410. [Q9FY74-1]
DR   GeneID; 830800; -.
DR   Gramene; AT5G09410.1; AT5G09410.1; AT5G09410. [Q9FY74-2]
DR   Gramene; AT5G09410.2; AT5G09410.2; AT5G09410. [Q9FY74-1]
DR   KEGG; ath:AT5G09410; -.
DR   Araport; AT5G09410; -.
DR   eggNOG; KOG0520; Eukaryota.
DR   InParanoid; Q9FY74; -.
DR   OMA; EMVLHLR; -.
DR   PRO; PR:Q9FY74; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FY74; baseline and differential.
DR   Genevisible; Q9FY74; AT.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009733; P:response to auxin; IMP:UniProtKB.
DR   GO; GO:0050826; P:response to freezing; IMP:UniProtKB.
DR   GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
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; 1.
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; 1.
DR   PROSITE; PS51437; CG_1; 1.
DR   PROSITE; PS50096; IQ; 2.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; ANK repeat; Calcium; Calmodulin-binding;
KW   Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Stress response; Transcription; Transcription regulation.
FT   CHAIN           1..1007
FT                   /note="Calmodulin-binding transcription activator 1"
FT                   /id="PRO_0000114486"
FT   REPEAT          612..641
FT                   /note="ANK 1"
FT   REPEAT          645..674
FT                   /note="ANK 2"
FT   DOMAIN          821..850
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          844..873
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DNA_BIND        18..144
FT                   /note="CG-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00767"
FT   REGION          148..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..398
FT                   /note="Transcription activation"
FT                   /evidence="ECO:0000269|PubMed:11925432"
FT   REGION          869..891
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000269|PubMed:11925432"
FT   COILED          915..943
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        148..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         942
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NPP4"
FT   VAR_SEQ         184..201
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_040640"
FT   CONFLICT        137
FT                   /note="E -> Q (in Ref. 1; CAC05467)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1007 AA;  113853 MW;  73FAB1EC5F746E06 CRC64;
     MVDRRSFGSI TPPLQLDMEQ LLSEAQHRWL RPTEICEILQ NYHKFHIASE SPTRPASGSL
     FLFDRKVLRY FRKDGHNWRK KKDGKTIREA HEKLKVGSID VLHCYYAHGE ANENFQRRCY
     WMLEQHLMHI VFVHYLEVKG NRTSIGMKEN NSNSVNGTAS VNIDSTASPT STLSSLCEDA
     DTGDSQQASS VLRPSPEPQT GNRYGWTPAP GMRNVSQVHG NRVRESDSQR LVDVRALDTV
     GNSLTRFHDQ PYCNNLLTQM QPSNTDSMLV EENSEKGGRL KAEHIRNPLQ TQFNWQDDTD
     LALFEQSAQD NFETFSSLLG SENLQPFGIS YQAPPSNMDS EYMPVMKILR RSEDSLKKVD
     SFSKWAIKEL GEMEDLQMQS SRGDIAWTTV ECETAAAGIS LSPSLSEDQR FTIVDFWPKS
     AKTDAEVEVM VIGTFLLSPQ EVTKYNWSCM FGEVEVPAEI LVDGVLCCHA PPHTAGHVPF
     YVTCSNRFAC SEVREFDFLS GSTQKINATD VYGTYTNEAS LQLRFEKMLA HRDFVHEHHI
     FEDVGDKRRQ ISKIMLLKEE KEYLLPGTYQ RDSTKQEPKG QLFRELFEEE LYIWLIHKVT
     EEGKGPNILD EDGQGILHFV AALGYDWAIK PVLAAGVNIN FRDANGWSAL HWAAFSGREE
     TVAVLVSLGA DAGALTDPSP ELPLGKTAAD LAYANGHRGI SGFLAESSLT SYLEKLTVDS
     KENSPANSCG EKAVQTVSER TAAPMTYGDV PEKLSLKDSL TAVRNATQAA DRLHQVFRMQ
     SFQRKQLCDI GDDEKIDISD QLAVSFAASK TKNPGQGDVS LSCAATHIQK KYRGWKKRKE
     FLLIRQRIVK IQAHVRGHQV RKQYRTVIWS VGLLEKIILR WRRKGNGLRG FKRNAVAKTV
     EPEPPVSAIC PRIPQEDEYD YLKEGRKQTE ERLQKALTRV KSMVQYPEAR DQYRRLLTVV
     EGFRENEASS SASINNKEEE AVNCEEDDFI DIESLLNDDT LMMSISP
 
 
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