MYB76_ARATH
ID MYB76_ARATH Reviewed; 338 AA.
AC Q9SPG5; A0MFE7; Q6R062;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Transcription factor MYB76;
DE AltName: Full=Myb-related protein 76;
DE Short=AtMYB76;
DE AltName: Full=Protein HIGH ALIPHATIC GLUCOSINOLATE 2;
GN Name=MYB76; Synonyms=HAG2; OrderedLocusNames=At5g07700; ORFNames=MBK20.16;
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], 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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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 IAA AND JA.
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, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION BY MECHANICAL STIMULI.
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 [9]
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 [10]
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 [11]
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 [12]
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 role in determining the spatial distribution of
CC aliphatic glucosinolates (AGLSs) within the leaf, mostly short chained.
CC Together with MYB28/HAG1 and MYB29/HAG3, promotes aliphatic
CC glucosinolate biosynthesis and represses indolic glucosinolate
CC biosynthesis, but could not activate AGSL biosynthesis on its own.
CC {ECO:0000269|PubMed:18042203, ECO:0000269|PubMed:20348214,
CC ECO:0000269|PubMed:23792303, ECO:0000269|PubMed:23943862}.
CC -!- SUBUNIT: Can form complexes with MYC2, MYC3 or MYC4.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC -!- TISSUE SPECIFICITY: Expressed in both vegetative and generative organs.
CC Mostly present in inflorescences, flowers and seedlings, in the
CC transition zone between roots and the foliar part, and stems, and, to a
CC lower extent, in leaves (in midvein and trichomes).
CC {ECO:0000269|PubMed:18042203, ECO:0000269|PubMed:23115560}.
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 both primary and secondary veins.
CC {ECO:0000269|PubMed:18042203}.
CC -!- INDUCTION: Slightly induced by auxin (IAA) and jasmonic acid (JA).
CC Accumulates upon mechanical stimuli (e.g. wounding) in inflorescence.
CC Down-regulated by sulfur-deficient stress.
CC {ECO:0000269|PubMed:16463103, ECO:0000269|PubMed:18042203,
CC ECO:0000269|PubMed:23792303}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28689.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF175992; AAD53097.1; -; mRNA.
DR EMBL; AB010070; BAB11449.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91195.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69764.1; -; Genomic_DNA.
DR EMBL; DQ446930; ABE66141.1; -; mRNA.
DR EMBL; DQ653273; ABK28689.1; ALT_SEQ; mRNA.
DR EMBL; AY519618; AAS10088.1; -; mRNA.
DR RefSeq; NP_001318501.1; NM_001342956.1.
DR RefSeq; NP_196387.1; NM_120852.2.
DR AlphaFoldDB; Q9SPG5; -.
DR SMR; Q9SPG5; -.
DR BioGRID; 15942; 4.
DR STRING; 3702.AT5G07700.1; -.
DR PaxDb; Q9SPG5; -.
DR PRIDE; Q9SPG5; -.
DR EnsemblPlants; AT5G07700.1; AT5G07700.1; AT5G07700.
DR EnsemblPlants; AT5G07700.2; AT5G07700.2; AT5G07700.
DR GeneID; 830663; -.
DR Gramene; AT5G07700.1; AT5G07700.1; AT5G07700.
DR Gramene; AT5G07700.2; AT5G07700.2; AT5G07700.
DR KEGG; ath:AT5G07700; -.
DR Araport; AT5G07700; -.
DR TAIR; locus:2160349; AT5G07700.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_0_0_1; -.
DR InParanoid; Q9SPG5; -.
DR OMA; ITSWSTY; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q9SPG5; -.
DR PRO; PR:Q9SPG5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SPG5; baseline and differential.
DR Genevisible; Q9SPG5; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0010439; P:regulation of glucosinolate biosynthetic process; IMP: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..338
FT /note="Transcription factor MYB76"
FT /id="PRO_0000415438"
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 123..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 61
FT /note="L -> S (in Ref. 5; AAS10088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38194 MW; E3FD91F906DCB877 CRC64;
MSKRPYCIGE GLKKGAWTTE EDKKLISYIH DHGEGGWRDI PEKAGLKRCG KSCRLRWTNY
LKPDIKRGEF SYEEEQIIIM LHASRGNKWS VIARHLPKRT DNEVKNYWNT HLKKRLIDDG
IDPVTHKPLA SSNPNPVEPM KFDFQKKSNQ DEHSSQSSST TPASLPLSSN LNSVKSKISS
GETQIESGHV SCKKRFGRSS STSRLLNKVA ARASSIGNIL STSIEGTLRS PASSSGLPDS
FSQSYEYMID NKEDLGTSID LNIPEYDFPQ FLEQLINDDD ENENIVGPEQ DLLMSDFPST
FVDEDDILGD ITSWSTYLLD HPNFMYESDQ DSDEKNFL
