MYBS1_ORYSJ
ID MYBS1_ORYSJ Reviewed; 306 AA.
AC Q8LH59;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Transcription factor MYBS1 {ECO:0000303|PubMed:12172034};
DE AltName: Full=Myb-related protein S1 {ECO:0000303|PubMed:12172034};
DE Short=OsMYBS1 {ECO:0000303|PubMed:12172034};
DE AltName: Full=Syringolide-induced protein 1-3-1B {ECO:0000312|EMBL:BAC05661.1};
GN Name=MYBS1 {ECO:0000303|PubMed:12172034};
GN OrderedLocusNames=Os01g0524500 {ECO:0000312|EMBL:BAS72473.1};
GN ORFNames=OJ1005_B10.31 {ECO:0000312|EMBL:BAC05661.1},
GN OSNPB_010524500 {ECO:0000312|EMBL:BAS72473.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, HOMODIMERIZATION,
RP AND INDUCTION BY SUCROSE AND GIBBERELLIC ACID.
RX PubMed=12172034; DOI=10.1105/tpc.001735;
RA Lu C.-A., Ho T.-H., Ho S.-L., Yu S.-M.;
RT "Three novel MYB proteins with one DNA binding repeat mediate sugar and
RT hormone regulation of alpha-amylase gene expression.";
RL Plant Cell 14:1963-1980(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP FUNCTION, INTERACTION WITH GAMYB, SUBCELLULAR LOCATION, NUCLEAR
RP LOCALIZATION SIGNAL, NUCLEAR EXPORT SIGNAL, AND MUTAGENESIS OF
RP 72-LEU--LEU-86; 133-LYS--LYS-140; 196-ARG--ARG-200 AND 203-ILE--VAL-215.
RX PubMed=22773748; DOI=10.1105/tpc.112.097741;
RA Hong Y.F., Ho T.H., Wu C.F., Ho S.L., Yeh R.H., Lu C.A., Chen P.W.,
RA Yu L.C., Chao A., Yu S.M.;
RT "Convergent starvation signals and hormone crosstalk in regulating nutrient
RT mobilization upon germination in cereals.";
RL Plant Cell 24:2857-2873(2012).
CC -!- FUNCTION: Transcription activator that binds to 5'-TATCCA-3' elements
CC in gene promoters. Derepresses strongly the sugar-repressed
CC transcription of promoters containing SRS or 5'-TATCCA-3' elements.
CC Functions with GAMYB to integrate diverse nutrient starvation and
CC gibberellin (GA) signaling pathways during germination of grains.
CC Sugar, nitrogen and phosphate starvation signals converge and
CC interconnect with GA to promote the co-nuclear import of MYBS1 and
CC GAMYB, resulting in the expression of a large set of GA-inducible
CC hydrolases, transporters, and regulators that are essential for
CC mobilization of nutrient reserves in the endosperm to support seedling
CC growth (PubMed:22773748). {ECO:0000269|PubMed:12172034,
CC ECO:0000269|PubMed:22773748}.
CC -!- SUBUNIT: Homodimer (PubMed:12172034). Interacts with GAMYB
CC (PubMed:22773748). {ECO:0000269|PubMed:12172034,
CC ECO:0000269|PubMed:22773748}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:22773748}. Cytoplasm {ECO:0000269|PubMed:22773748}.
CC Note=Preferentially localized to the nucleus under sugar starvation
CC conditions. Glucose inhibits nuclear localization.
CC {ECO:0000269|PubMed:22773748}.
CC -!- TISSUE SPECIFICITY: Expressed in aboveground tissues, with the highest
CC level in leaves. {ECO:0000269|PubMed:12172034}.
CC -!- INDUCTION: Repressed by sucrose and gibberellic acid (GA).
CC {ECO:0000269|PubMed:12172034}.
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; AY151042; AAN63152.1; -; mRNA.
DR EMBL; AP004611; BAC05661.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS72473.1; -; Genomic_DNA.
DR RefSeq; XP_015627636.1; XM_015772150.1.
DR AlphaFoldDB; Q8LH59; -.
DR STRING; 39947.Q8LH59; -.
DR PaxDb; Q8LH59; -.
DR PRIDE; Q8LH59; -.
DR EnsemblPlants; Os01t0524500-02; Os01t0524500-02; Os01g0524500.
DR GeneID; 4323963; -.
DR Gramene; Os01t0524500-02; Os01t0524500-02; Os01g0524500.
DR KEGG; osa:4323963; -.
DR OrthoDB; 1106382at2759; -.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q8LH59; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IBA:GO_Central.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR006447; Myb_dom_plants.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..306
FT /note="Transcription factor MYBS1"
FT /id="PRO_0000439173"
FT DOMAIN 18..73
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 136..192
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 164..188
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 89..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 72..86
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000269|PubMed:22773748"
FT MOTIF 133..140
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000269|PubMed:22773748"
FT MOTIF 196..200
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000269|PubMed:22773748"
FT MOTIF 203..215
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000269|PubMed:22773748"
FT COMPBIAS 109..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 72..86
FT /note="LVEDVAAIDAGRVPL->AAEDAAAADAGRAPA: Abolishes
FT cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:22773748"
FT MUTAGEN 133..140
FT /note="KAEQERRK->AAEQEAAA: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:22773748"
FT MUTAGEN 196..200
FT /note="RDRRR->ADAAA: Reduces nuclear localization."
FT /evidence="ECO:0000269|PubMed:22773748"
FT MUTAGEN 203..215
FT /note="IHDITSVTAGDQV->AHDATSATAGDQA: Reduces cytoplasmic
FT localization."
FT /evidence="ECO:0000269|PubMed:22773748"
SQ SEQUENCE 306 AA; 31913 MW; 13BE7EC1EA36FB38 CRC64;
MTSQAATTTT TAAAAAAWTR EDDKAFENAL AACAAPPPAD GGAPDDDWFA ALAASVPGAR
SAEEVRRHYE ALVEDVAAID AGRVPLPRYA GEESAAPPDG AGAAAAASKD GGHRRDERKG
GGGGYDGGKS CSKAEQERRK GIPWTEEEHR LFLLGLDKFG KGDWRSISRN FVISRTPTQV
ASHAQKYFIR LNSMNRDRRR SSIHDITSVT AGDQVAAQQG APITGHQATG NPAAAALGPP
GMKHHHHHHP GGAPPPMPMY SAAPMGHPVA GHMVPAAVGT PVVFPPGHAP YVVPVGYPAP
PAKMHQ
