MYB60_VITVI
ID MYB60_VITVI Reviewed; 321 AA.
AC B3VTV7;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Transcription factor MYB60 {ECO:0000303|PubMed:18647406};
DE AltName: Full=Myb domain protein 60 {ECO:0000303|PubMed:18647406};
DE Short=VvMYB60 {ECO:0000303|PubMed:18647406};
GN Name=MYB60 {ECO:0000303|PubMed:18647406};
GN OrderedLocusNames=VIT_08s0056g00800 {ECO:0000312|EMBL:CCB55976.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Pinot noir;
RX PubMed=18647406; DOI=10.1186/1471-2229-8-83;
RA Matus J.T., Aquea F., Arce-Johnson P.;
RT "Analysis of the grape MYB R2R3 subfamily reveals expanded wine quality-
RT related clades and conserved gene structure organization across Vitis and
RT Arabidopsis genomes.";
RL BMC Plant Biol. 8:83-83(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024;
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
RN [3]
RP FUNCTION, REPRESSION BY ABSCISIC ACID, INDUCTION BY OSMOTIC STRESS, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Cabernet Sauvignon;
RX PubMed=22018045; DOI=10.1186/1471-2229-11-142;
RA Galbiati M., Matus J.T., Francia P., Rusconi F., Canon P., Medina C.,
RA Conti L., Cominelli E., Tonelli C., Arce-Johnson P.;
RT "The grapevine guard cell-related VvMYB60 transcription factor is involved
RT in the regulation of stomatal activity and is differentially expressed in
RT response to ABA and osmotic stress.";
RL BMC Plant Biol. 11:142-142(2011).
CC -!- FUNCTION: Transcription factor involved in the regulation of gene (e.g.
CC drought-regulated and flavonoid biosynthetic genes) expression and
CC stomatal movements leading to negative regulation of responses to
CC drought and responses to other physiological stimuli (e.g. light).
CC {ECO:0000269|PubMed:22018045}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC -!- TISSUE SPECIFICITY: Restricted to stomatal guard cells. Mostly
CC expressed in leaves, cotyledons, hypocotyls, seeds and ripened berry
CC skins. {ECO:0000269|PubMed:22018045}.
CC -!- DEVELOPMENTAL STAGE: During seed development, gradually down-regulated
CC towards the onset of ripening (veraison). During berry skin
CC development, dramatic decrease to full repression at veraison, followed
CC by a slight increase towards ripening. In flowers, barely detectable in
CC stamens, at the interface of filaments and anthers.
CC {ECO:0000269|PubMed:22018045}.
CC -!- INDUCTION: Repressed by abscisic acid (ABA) and osmotic stress (salt
CC stress). {ECO:0000269|PubMed:22018045}.
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DR EMBL; EU816358; ACF21938.1; -; mRNA.
DR EMBL; FN595995; CCB55976.1; -; Genomic_DNA.
DR EMBL; FN597027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001268022.1; NM_001281093.1.
DR AlphaFoldDB; B3VTV7; -.
DR SMR; B3VTV7; -.
DR STRING; 29760.VIT_08s0056g00800.t01; -.
DR EnsemblPlants; Vitvi08g00069_t001; Vitvi08g00069_P001; Vitvi08g00069.
DR GeneID; 100233072; -.
DR Gramene; Vitvi08g00069_t001; Vitvi08g00069_P001; Vitvi08g00069.
DR KEGG; vvi:100233072; -.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_6_0_1; -.
DR InParanoid; B3VTV7; -.
DR OrthoDB; 1499244at2759; -.
DR Proteomes; UP000009183; Chromosome 8.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0010118; P:stomatal movement; IMP: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 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Reference proteome; Repeat; S-nitrosylation;
KW Transcription; Transcription regulation.
FT CHAIN 1..321
FT /note="Transcription factor MYB60"
FT /id="PRO_0000446252"
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 196..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SCU7"
FT MOD_RES 53
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9SCU7"
SQ SEQUENCE 321 AA; 36174 MW; DE251915F918B4FD CRC64;
MGRPPCCDKV GIKKGPWTPE EDIILVSYIQ EHGPGNWRSV PTNTGLLRCS KSCRLRWTNY
LRPGIKRGNF TPHEEGMIIH LQALLGNKWA AIASYLPQRT DNDIKNYWNT HLKKKIKKFQ
SALSPHMASD STTSTCTNHQ FVPRSYAGDD HHRRGSSFEV INGHSSAHPS LNSPISTYAS
STENISRLLE GWMRSSPKAT KEKLHQNSSL EEGSIDMTGN SMAVAAVTSV QCYRPKLEQG
GGELVANDEF ESILEYENLN DDHHQTTDAT IPSDDHDHDH EMKMDHDQKK HNPPLSFLEK
WLLDESAAQG EEMMDQLSPI F
