MYB29_ARATH
ID MYB29_ARATH Reviewed; 336 AA.
AC Q9FLR1; O49765;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Transcription factor MYB29;
DE AltName: Full=Myb-related protein 29;
DE Short=AtMYB29;
DE AltName: Full=Protein HIGH ALIPHATIC GLUCOSINOLATE 3;
DE AltName: Full=Protein PRODUCTION OF METHIONINE-DERIVED GLUCOSINOLATE 2;
GN Name=MYB29; Synonyms=HAG3, PMG2; OrderedLocusNames=At5g07690;
GN ORFNames=MBK20.15;
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], TISSUE SPECIFICITY, INDUCTION BY NITROGEN
RP STARVATION AND UV LIGHT, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=9839469; DOI=10.1046/j.1365-313x.1998.00278.x;
RA Kranz H.D., Denekamp M., Greco R., Jin H.-L., Leyva A., Meissner R.C.,
RA Petroni K., Urzainqui A., Bevan M., Martin C., Smeekens S., Tonelli C.,
RA Paz-Ares J., Weisshaar B.;
RT "Towards functional characterisation of the members of the R2R3-MYB gene
RT family from Arabidopsis thaliana.";
RL Plant J. 16:263-276(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Qu L.-J., Gu H.;
RT "The MYB transcription factor family in Arabidopsis: a genome-wide cloning
RT and expression pattern analysis.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=11597504; DOI=10.1016/s1369-5266(00)00199-0;
RA Stracke R., Werber M., Weisshaar B.;
RT "The R2R3-MYB gene family in Arabidopsis thaliana.";
RL Curr. Opin. Plant Biol. 4:447-456(2001).
RN [7]
RP GENE FAMILY, AND INDUCTION BY GA; JA AND SA.
RX PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
RA Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y., Wang X.,
RA Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W., Chen Z., Gu H.,
RA Qu L.-J.;
RT "The MYB transcription factor superfamily of Arabidopsis: expression
RT analysis and phylogenetic comparison with the rice MYB family.";
RL Plant Mol. Biol. 60:107-124(2006).
RN [8]
RP FUNCTION IN GLUCOSINOLATES BIOSYNTHESIS.
RX PubMed=17420480; DOI=10.1073/pnas.0611629104;
RA Hirai M.Y., Sugiyama K., Sawada Y., Tohge T., Obayashi T., Suzuki A.,
RA Araki R., Sakurai N., Suzuki H., Aoki K., Goda H., Nishizawa O.I.,
RA Shibata D., Saito K.;
RT "Omics-based identification of Arabidopsis Myb transcription factors
RT regulating aliphatic glucosinolate biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:6478-6483(2007).
RN [9]
RP FUNCTION IN GLUCOSINOLATES BIOSYNTHESIS, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION BY WOUNDING; MEJA AND SA.
RX PubMed=18042203; DOI=10.1111/j.1469-8137.2007.02295.x;
RA Gigolashvili T., Engqvist M., Yatusevich R., Mueller C., Fluegge U.I.;
RT "HAG2/MYB76 and HAG3/MYB29 exert a specific and coordinated control on the
RT regulation of aliphatic glucosinolate biosynthesis in Arabidopsis
RT thaliana.";
RL New Phytol. 177:627-642(2008).
RN [10]
RP FUNCTION IN GLUCOSINOLATES BIOSYNTHESIS.
RC STRAIN=cv. Columbia;
RX PubMed=18446225; DOI=10.1371/journal.pone.0002068;
RA Beekwilder J., van Leeuwen W., van Dam N.M., Bertossi M., Grandi V.,
RA Mizzi L., Soloviev M., Szabados L., Molthoff J.W., Schipper B.,
RA Verbocht H., de Vos R.C.H., Morandini P., Aarts M.G.M., Bovy A.;
RT "The impact of the absence of aliphatic glucosinolates on insect herbivory
RT in Arabidopsis.";
RL PLoS ONE 3:E2068-E2068(2008).
RN [11]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=20348214; DOI=10.1104/pp.109.149286;
RA Soenderby I.E., Burow M., Rowe H.C., Kliebenstein D.J., Halkier B.A.;
RT "A complex interplay of three R2R3 MYB transcription factors determines the
RT profile of aliphatic glucosinolates in Arabidopsis.";
RL Plant Physiol. 153:348-363(2010).
RN [12]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=23115560; DOI=10.3389/fpls.2012.00242;
RA Frerigmann H., Boettcher C., Baatout D., Gigolashvili T.;
RT "Glucosinolates are produced in trichomes of Arabidopsis thaliana.";
RL Front. Plant Sci. 3:242-242(2012).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23580754; DOI=10.1093/jxb/ert094;
RA Guo R., Qian H., Shen W., Liu L., Zhang M., Cai C., Zhao Y., Qiao J.,
RA Wang Q.;
RT "BZR1 and BES1 participate in regulation of glucosinolate biosynthesis by
RT brassinosteroids in Arabidopsis.";
RL J. Exp. Bot. 64:2401-2412(2013).
RN [14]
RP FUNCTION, AND INDUCTION BY SULFUR.
RX PubMed=23792303; DOI=10.1093/pcp/pct085;
RA Li Y., Sawada Y., Hirai A., Sato M., Kuwahara A., Yan X., Hirai M.Y.;
RT "Novel insights into the function of Arabidopsis R2R3-MYB transcription
RT factors regulating aliphatic glucosinolate biosynthesis.";
RL Plant Cell Physiol. 54:1335-1344(2013).
RN [15]
RP FUNCTION, AND INTERACTION WITH MYC2; MYC3 AND MYC4.
RX PubMed=23943862; DOI=10.1105/tpc.113.115139;
RA Schweizer F., Fernandez-Calvo P., Zander M., Diez-Diaz M., Fonseca S.,
RA Glauser G., Lewsey M.G., Ecker J.R., Solano R., Reymond P.;
RT "Arabidopsis basic helix-loop-helix transcription factors MYC2, MYC3, and
RT MYC4 regulate glucosinolate biosynthesis, insect performance, and feeding
RT behavior.";
RL Plant Cell 25:3117-3132(2013).
CC -!- FUNCTION: Plays a minor rheostat role in aliphatic glucosinolates
CC (GLSs) biosynthesis, mostly short chained. Together with MYB28/HAG1 and
CC MYB76/HAG2, promotes aliphatic glucosinolate biosynthesis but represses
CC indolic glucosinolate biosynthesis. Prevents insect performance (e.g.
CC lepidopteran insect Mamestra brassicae) by promoting glucosinolates.
CC {ECO:0000269|PubMed:17420480, ECO:0000269|PubMed:18042203,
CC ECO:0000269|PubMed:18446225, ECO:0000269|PubMed:20348214,
CC ECO:0000269|PubMed:23580754, ECO:0000269|PubMed:23792303,
CC ECO:0000269|PubMed:23943862}.
CC -!- SUBUNIT: Can form complexes with MYC2, MYC3 or MYC4.
CC -!- INTERACTION:
CC Q9FLR1; Q9FJJ3: SRO5; NbExp=3; IntAct=EBI-15410392, EBI-4434999;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC -!- TISSUE SPECIFICITY: Expressed in both vegetative and generative organs.
CC Mostly present in seedlings, inflorescences, roots and stems, and, to a
CC lower extent, in leaves (in midvein and trichomes) and siliques.
CC {ECO:0000269|PubMed:18042203, ECO:0000269|PubMed:23115560,
CC ECO:0000269|PubMed:9839469}.
CC -!- DEVELOPMENTAL STAGE: Primarily present around the midvein in seedlings.
CC Accumulates gradually in expanding leaves, reaching a maximum in fully
CC expanded leaves in the primary vein. {ECO:0000269|PubMed:18042203}.
CC -!- INDUCTION: Slightly induced by gibberellic acid (GA), jasmonic acid
CC (JA, MeJA), nitrogen starvation and UV LIGHT treatment. Transiently
CC repressed by salicylic acid (SA). Accumulates upon mechanical stimuli
CC (e.g. wounding) in inflorescence. Down-regulated by sulfur-deficient
CC stress. {ECO:0000269|PubMed:16463103, ECO:0000269|PubMed:18042203,
CC ECO:0000269|PubMed:23792303, ECO:0000269|PubMed:9839469}.
CC -!- DISRUPTION PHENOTYPE: Low levels of aliphatic glucosinolates.
CC {ECO:0000269|PubMed:23580754}.
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DR EMBL; AF062872; AAC83594.1; -; mRNA.
DR EMBL; AB010070; BAB11448.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91194.1; -; Genomic_DNA.
DR EMBL; AY035145; AAK59649.1; -; mRNA.
DR EMBL; AY059078; AAL15184.1; -; mRNA.
DR EMBL; AY519617; AAS10087.1; -; mRNA.
DR PIR; T51644; T51644.
DR RefSeq; NP_196386.1; NM_120851.2.
DR AlphaFoldDB; Q9FLR1; -.
DR SMR; Q9FLR1; -.
DR BioGRID; 15941; 6.
DR IntAct; Q9FLR1; 2.
DR STRING; 3702.AT5G07690.1; -.
DR PaxDb; Q9FLR1; -.
DR PRIDE; Q9FLR1; -.
DR ProteomicsDB; 251210; -.
DR EnsemblPlants; AT5G07690.1; AT5G07690.1; AT5G07690.
DR GeneID; 830662; -.
DR Gramene; AT5G07690.1; AT5G07690.1; AT5G07690.
DR KEGG; ath:AT5G07690; -.
DR Araport; AT5G07690; -.
DR TAIR; locus:2160339; AT5G07690.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_0_0_1; -.
DR InParanoid; Q9FLR1; -.
DR OMA; CLNDMDE; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q9FLR1; -.
DR PRO; PR:Q9FLR1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLR1; baseline and differential.
DR Genevisible; Q9FLR1; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0010438; P:cellular response to sulfur starvation; TAS:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IGI:TAIR.
DR GO; GO:0009819; P:drought recovery; IMP:TAIR.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IMP:TAIR.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IMP:TAIR.
DR GO; GO:0010439; P:regulation of glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:2000070; P:regulation of response to water deprivation; IDA:TAIR.
DR GO; GO:1905255; P:regulation of RNA binding transcription factor activity; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
DR GO; GO:0009644; P:response to high light intensity; IDA:TAIR.
DR GO; GO:0009625; P:response to insect; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..336
FT /note="Transcription factor MYB29"
FT /id="PRO_0000415437"
FT DOMAIN 9..65
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 66..116
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 37..61
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 89..112
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 127..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 34
FT /note="E -> G (in Ref. 1; AAC83594)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="D -> N (in Ref. 1; AAC83594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 37966 MW; AE5DAC67FF961C0B CRC64;
MSRKPCCVGE GLKKGAWTAE EDKKLISYIH EHGEGGWRDI PQKAGLKRCG KSCRLRWANY
LKPDIKRGEF SYEEEQIIIM LHASRGNKWS VIARHLPKRT DNEIKNYWNT HLKKLLIDKG
IDPVTHKPLA YDSNPDEQSQ SGSISPKSLP PSSSKNVPEI TSSDETPKYD ASLSSKKRCF
KRSSSTSKLL NKVAARASSM GTILGASIEG TLISSTPLSS CLNDDFSETS QFQMEEFDPF
YQSSEHIIDH MKEDISINNS EYDFSQFLEQ FSNNEGEEAD NTGGGYNQDL LMSDVSSTSV
DEDEMMQNIT GWSNYLLDHS DFNYDTSQDY DDKNFI
