MYB28_ARATH
ID MYB28_ARATH Reviewed; 366 AA.
AC Q9SPG2; F4K3H4;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Transcription factor MYB28;
DE AltName: Full=Myb-related protein 28;
DE Short=AtMYB28;
DE AltName: Full=Protein HIGH ALIPHATIC GLUCOSINOLATE 1;
DE AltName: Full=Protein PRODUCTION OF METHIONINE-DERIVED GLUCOSINOLATE 1;
GN Name=MYB28; Synonyms=HAG1, PMG1; OrderedLocusNames=At5g61420;
GN ORFNames=MFB13.22;
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=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 [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 1), GENE FAMILY, AND
RP 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY MECHANICAL STIMULI AND GLUCOSE,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=17521412; DOI=10.1111/j.1365-313x.2007.03133.x;
RA Gigolashvili T., Yatusevich R., Berger B., Mueller C., Fluegge U.-I.;
RT "The R2R3-MYB transcription factor HAG1/MYB28 is a regulator of methionine-
RT derived glucosinolate biosynthesis in Arabidopsis thaliana.";
RL Plant J. 51:247-261(2007).
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.
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, AND INDUCTION BY WOUNDING.
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: Major regulator of short-chained aliphatic glucosinolates
CC (GLSs) biosynthesis. Together with MYB29/HAG3 and MYB76/HAG2, promotes
CC aliphatic glucosinolate biosynthesis but represses indolic
CC glucosinolate biosynthesis. Prevents insect performance (e.g.
CC lepidopteran insect Mamestra brassicae and Spodoptera exigua) by
CC promoting glucosinolates. {ECO:0000269|PubMed:17420480,
CC ECO:0000269|PubMed:17521412, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:17521412}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SPG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SPG2-2; Sequence=VSP_042252;
CC -!- TISSUE SPECIFICITY: Expressed in generative organs, mature leaves and
CC trichomes. {ECO:0000269|PubMed:17521412, ECO:0000269|PubMed:23115560}.
CC -!- DEVELOPMENTAL STAGE: First present in stems, petioles and the main
CC veins of true leaves in young seedlings. Later accumulates in leaves
CC and present in lateral roots. During transition from the vegetative to
CC the generative stage, preferentially expressed in inflorescence.
CC {ECO:0000269|PubMed:17521412}.
CC -!- INDUCTION: Slightly induced by glucose, gibberellic acid (GA), jasmonic
CC acid (JA) and salicylic acid (SA). Transiently induced in inflorescence
CC by mechanical stimuli such as touch or wounding, including herbivory-
CC wounding. Up-regulated by sulfur-deficient stress.
CC {ECO:0000269|PubMed:16463103, ECO:0000269|PubMed:17521412,
CC ECO:0000269|PubMed:23115560, ECO:0000269|PubMed:23792303}.
CC -!- DISRUPTION PHENOTYPE: Low levels of aliphatic glucosinolates and
CC decreased repressing effect of brassinosteroid on glucosinolates.
CC {ECO:0000269|PubMed:23580754}.
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DR EMBL; AB010073; BAB08498.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97466.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97467.1; -; Genomic_DNA.
DR EMBL; AF175998; AAD53103.1; -; mRNA.
DR EMBL; AY519643; AAS10113.1; -; mRNA.
DR EMBL; BT028959; ABI54334.1; -; mRNA.
DR RefSeq; NP_200950.1; NM_125535.4. [Q9SPG2-1]
DR RefSeq; NP_851241.1; NM_180910.2. [Q9SPG2-2]
DR AlphaFoldDB; Q9SPG2; -.
DR SMR; Q9SPG2; -.
DR BioGRID; 21507; 8.
DR IntAct; Q9SPG2; 4.
DR STRING; 3702.AT5G61420.2; -.
DR PaxDb; Q9SPG2; -.
DR PRIDE; Q9SPG2; -.
DR ProteomicsDB; 251330; -. [Q9SPG2-1]
DR EnsemblPlants; AT5G61420.1; AT5G61420.1; AT5G61420. [Q9SPG2-2]
DR EnsemblPlants; AT5G61420.2; AT5G61420.2; AT5G61420. [Q9SPG2-1]
DR GeneID; 836263; -.
DR Gramene; AT5G61420.1; AT5G61420.1; AT5G61420. [Q9SPG2-2]
DR Gramene; AT5G61420.2; AT5G61420.2; AT5G61420. [Q9SPG2-1]
DR KEGG; ath:AT5G61420; -.
DR Araport; AT5G61420; -.
DR TAIR; locus:2163233; AT5G61420.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_0_1_1; -.
DR InParanoid; Q9SPG2; -.
DR OMA; YSEHEIN; -.
DR PhylomeDB; Q9SPG2; -.
DR PRO; PR:Q9SPG2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SPG2; baseline and differential.
DR Genevisible; Q9SPG2; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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; IMP:TAIR.
DR GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR GO; GO:0010439; P:regulation of glucosinolate biosynthetic process; 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:0009625; P:response to insect; IEP:TAIR.
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 Alternative splicing; DNA-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..366
FT /note="Transcription factor MYB28"
FT /id="PRO_0000415436"
FT DOMAIN 9..61
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 62..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 124..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042252"
SQ SEQUENCE 366 AA; 41134 MW; DD7533DCB1857D0B CRC64;
MSRKPCCVGE GLKKGAWTTE EDKKLISYIH DHGEGGWRDI PQKAGLKRCG KSCRLRWTNY
LKPEIKRGEF SSEEEQIIIM LHASRGNKWS VIARHLPRRT DNEIKNYWNT HLKKRLMEQG
IDPVTHKPLA SSSNPTVDEN LNSPNASSSD KQYSRSSSMP FLSRPPPSSC NMVSKVSELS
SNDGTPIQGS SLSCKKRFKK SSSTSRLLNK VAAKATSIKD ILSASMEGSL SATTISHASF
FNGFTEQIRN EEDSSNTSLT NTLAEFDPFS PSSLYPEHEI NATSDLNMDQ DYDFSQFFEK
FGGDNHNEEN SMNDLLMSDV SQEVSSTSVD DQDNMVGNFE GWSNYLLDHT NFMYDTDSDS
LEKHFI