PHLA_ARATH
ID PHLA_ARATH Reviewed; 402 AA.
AC Q9FK47; F4JWK0; Q84WH5; Q94B34; Q9C5Y6;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Myb-related protein 1 {ECO:0000303|PubMed:12008900};
DE AltName: Full=Myb family transcription factor PHL10 {ECO:0000305};
DE AltName: Full=Protein PHR1-LIKE 10 {ECO:0000305};
GN Name=MYR1 {ECO:0000303|PubMed:12008900}; Synonyms=PHL10 {ECO:0000305};
GN OrderedLocusNames=At5g18240 {ECO:0000312|Araport:AT5G18240};
GN ORFNames=MRG7.20 {ECO:0000312|EMBL:BAB09482.1};
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] (ISOFORM 3).
RX PubMed=12008900; DOI=10.1023/a:1014440531842;
RA Thelander M., Fredriksson D., Schouten J., Hoge J.H.C., Ronne H.;
RT "Cloning by pathway activation in yeast: identification of an Arabidopsis
RT thaliana F-box protein that can turn on glucose repression.";
RL Plant Mol. Biol. 49:69-79(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(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] (ISOFORM 1).
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 GENE FAMILY.
RX PubMed=11511543; DOI=10.1101/gad.204401;
RA Rubio V., Linhares F., Solano R., Martin A.C., Iglesias J., Leyva A.,
RA Paz-Ares J.;
RT "A conserved MYB transcription factor involved in phosphate starvation
RT signaling both in vascular plants and in unicellular algae.";
RL Genes Dev. 15:2122-2133(2001).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15923329; DOI=10.1104/pp.105.060202;
RA Zhao C., Craig J.C., Petzold H.E., Dickerman A.W., Beers E.P.;
RT "The xylem and phloem transcriptomes from secondary tissues of the
RT Arabidopsis root-hypocotyl.";
RL Plant Physiol. 138:803-818(2005).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=21255164; DOI=10.1111/j.1365-313x.2011.04508.x;
RA Zhao C., Hanada A., Yamaguchi S., Kamiya Y., Beers E.P.;
RT "The Arabidopsis Myb genes MYR1 and MYR2 are redundant negative regulators
RT of flowering time under decreased light intensity.";
RL Plant J. 66:502-515(2011).
RN [8]
RP ALTERNATIVE SPLICING, AND SUBUNIT.
RX PubMed=24309816; DOI=10.4161/psb.27325;
RA Zhao C., Beers E.;
RT "Alternative splicing of Myb-related genes MYR1 and MYR2 may modulate
RT activities through changes in dimerization, localization, or protein
RT folding.";
RL Plant Signal. Behav. 8:E27325-E27325(2013).
CC -!- FUNCTION: Transcription factor that may act on the GAL1 promoter
CC (PubMed:12008900). Acts redundantly with MYR2 as a repressor of
CC flowering and organ elongation under decreased light intensity
CC (PubMed:21255164). Represses gibberellic acid (GA)-dependent responses
CC and affects levels of bioactive GA (PubMed:21255164).
CC {ECO:0000269|PubMed:21255164, ECO:0000305|PubMed:12008900}.
CC -!- SUBUNIT: Isoforms 1 and 2: homodimer. Isoform 3: loss of dimerization.
CC {ECO:0000269|PubMed:24309816}.
CC -!- INTERACTION:
CC Q9FK47; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-25523464, EBI-2000137;
CC Q9FK47; P93830: IAA17; NbExp=3; IntAct=EBI-25523464, EBI-632243;
CC Q9FK47; Q9FNZ4: NIMIN-3; NbExp=3; IntAct=EBI-25523464, EBI-541115;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21255164}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9FK47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FK47-2; Sequence=VSP_058439;
CC Name=3;
CC IsoId=Q9FK47-3; Sequence=VSP_058438;
CC -!- TISSUE SPECIFICITY: Expressed in phloem and/or cambium.
CC {ECO:0000269|PubMed:15923329}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under long days
CC conditions, but early flowering when grown under short days conditions.
CC {ECO:0000269|PubMed:21255164}.
CC -!- SIMILARITY: Belongs to the MYB-CC family. {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; AF291817; AAK01148.1; -; mRNA.
DR EMBL; AB012246; BAB09482.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92523.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92524.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92525.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92526.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92527.1; -; Genomic_DNA.
DR EMBL; BT003421; AAO30084.1; -; mRNA.
DR EMBL; AY042878; AAK68818.1; -; mRNA.
DR RefSeq; NP_197325.1; NM_121829.2. [Q9FK47-1]
DR RefSeq; NP_850842.1; NM_180511.1. [Q9FK47-3]
DR RefSeq; NP_974797.1; NM_203068.2. [Q9FK47-3]
DR RefSeq; NP_974798.1; NM_203069.2. [Q9FK47-1]
DR RefSeq; NP_974799.1; NM_203070.2. [Q9FK47-2]
DR AlphaFoldDB; Q9FK47; -.
DR SMR; Q9FK47; -.
DR IntAct; Q9FK47; 3.
DR STRING; 3702.AT5G18240.1; -.
DR PaxDb; Q9FK47; -.
DR PRIDE; Q9FK47; -.
DR ProteomicsDB; 235058; -. [Q9FK47-1]
DR EnsemblPlants; AT5G18240.1; AT5G18240.1; AT5G18240. [Q9FK47-1]
DR EnsemblPlants; AT5G18240.2; AT5G18240.2; AT5G18240. [Q9FK47-3]
DR EnsemblPlants; AT5G18240.3; AT5G18240.3; AT5G18240. [Q9FK47-3]
DR EnsemblPlants; AT5G18240.4; AT5G18240.4; AT5G18240. [Q9FK47-1]
DR EnsemblPlants; AT5G18240.5; AT5G18240.5; AT5G18240. [Q9FK47-2]
DR GeneID; 831942; -.
DR Gramene; AT5G18240.1; AT5G18240.1; AT5G18240. [Q9FK47-1]
DR Gramene; AT5G18240.2; AT5G18240.2; AT5G18240. [Q9FK47-3]
DR Gramene; AT5G18240.3; AT5G18240.3; AT5G18240. [Q9FK47-3]
DR Gramene; AT5G18240.4; AT5G18240.4; AT5G18240. [Q9FK47-1]
DR Gramene; AT5G18240.5; AT5G18240.5; AT5G18240. [Q9FK47-2]
DR KEGG; ath:AT5G18240; -.
DR Araport; AT5G18240; -.
DR TAIR; locus:2172394; AT5G18240.
DR eggNOG; ENOG502QT7M; Eukaryota.
DR HOGENOM; CLU_053944_3_0_1; -.
DR InParanoid; Q9FK47; -.
DR OMA; DPLMHHQ; -.
DR OrthoDB; 828397at2759; -.
DR PhylomeDB; Q9FK47; -.
DR PRO; PR:Q9FK47; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK47; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR025756; Myb_CC_LHEQLE.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR006447; Myb_dom_plants.
DR InterPro; IPR044848; PHR1-like.
DR PANTHER; PTHR31499; PTHR31499; 1.
DR Pfam; PF14379; Myb_CC_LHEQLE; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..402
FT /note="Myb-related protein 1"
FT /id="PRO_0000436867"
FT DOMAIN 42..102
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 73..98
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 238..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 148..168
FT /evidence="ECO:0000255"
FT MOTIF 161..166
FT /note="LHEQLE"
FT /evidence="ECO:0000305"
FT COMPBIAS 238..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 167..172
FT /note="Missing (in isoform 3)"
FT /id="VSP_058438"
FT VAR_SEQ 167..168
FT /note="Missing (in isoform 2)"
FT /id="VSP_058439"
FT CONFLICT 377
FT /note="L -> I (in Ref. 4; AAO30084/AAK68818)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="T -> A (in Ref. 4; AAK68818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 45574 MW; 4DA87252F3C455A9 CRC64;
MYYHNQHQGK SILSSSRMPI SSERHPFLRG NGTGDSGLIL STDAKPRLKW TPDLHERFVE
AVNQLGGGDK ATPKTIMKVM GIPGLTLYHL KSHLQKYRLS KNLNGQANSS LNKTSVMTMV
EENPPEVDES HSESLSIGPQ PSMNLPISDA LQMQIEVQRR LHEQLEVQRH LQLRIEAQGK
YLQSILEKAQ ETLGRQNLGA AGIEATKAQL SELVSKVSAD YPDSSFLEPK ELQNLHHQQM
QKTYPPNSSL DSCLTSSEGT QKAPKMLDNR LGLRTYIGDS TSEQKEIMEE PFFHRMELTW
AEEESLRENH NRPYLSTMVN NAEPRISSSR RSPGRLSIGV GLHEHRGRSS NNSEYTEERF
NENNEDCKLE THTRTALDLN THDENYGTTR PKQFDLNGFS WN
