PHL2_ARATH
ID PHL2_ARATH Reviewed; 295 AA.
AC Q94A57; F4J5D9; Q9LRN5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein PHR1-LIKE 2 {ECO:0000303|PubMed:26586833};
DE AltName: Full=Myb family transcription factor PHL2 {ECO:0000303|PubMed:26586833};
GN Name=PHL2 {ECO:0000303|PubMed:26586833};
GN OrderedLocusNames=At3g24120 {ECO:0000312|Araport:AT3G24120};
GN ORFNames=MUJ8.3 {ECO:0000312|EMBL:BAB01353.1};
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 {ECO:0000312|EMBL:AAK91372.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 ALTERNATIVE SPLICING.
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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PHL3, SUBUNIT, AND
RP INDUCTION BY PHOSPHATE.
RX PubMed=26586833; DOI=10.1104/pp.15.01336;
RA Sun L., Song L., Zhang Y., Zheng Z., Liu D.;
RT "Arabidopsis PHL2 and PHR1 act redundantly as the key components of the
RT central regulatory system controlling transcriptional responses to
RT phosphate starvation.";
RL Plant Physiol. 170:499-514(2016).
CC -!- FUNCTION: Transcriptional activator (PubMed:26586833). Acts redundantly
CC with PHR1 as a key component of the central regulatory system
CC controlling transcriptional responses to Pi starvation
CC (PubMed:26586833). Binds in a sequence-specific manner to phosphate
CC starvation-regulated promoters (PubMed:26586833).
CC {ECO:0000269|PubMed:26586833}.
CC -!- SUBUNIT: Homo- and heterodimers (PubMed:26586833). Interacts with PHL3,
CC but not with PHR1 (PubMed:26586833). {ECO:0000269|PubMed:26586833}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26586833}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94A57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94A57-2; Sequence=VSP_058429;
CC -!- INDUCTION: Up-regulated in roots by low Pi.
CC {ECO:0000269|PubMed:26586833}.
CC -!- SIMILARITY: Belongs to the MYB-CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01353.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB028621; BAB01353.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76859.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76860.1; -; Genomic_DNA.
DR EMBL; AY050355; AAK91372.1; -; mRNA.
DR EMBL; AY094046; AAM16202.1; -; mRNA.
DR EMBL; AY088428; AAM65964.1; -; mRNA.
DR RefSeq; NP_566744.1; NM_113317.5. [Q94A57-1]
DR RefSeq; NP_974356.1; NM_202627.1. [Q94A57-2]
DR AlphaFoldDB; Q94A57; -.
DR SMR; Q94A57; -.
DR IntAct; Q94A57; 5.
DR STRING; 3702.AT3G24120.2; -.
DR PRIDE; Q94A57; -.
DR ProteomicsDB; 236727; -. [Q94A57-1]
DR EnsemblPlants; AT3G24120.1; AT3G24120.1; AT3G24120. [Q94A57-1]
DR EnsemblPlants; AT3G24120.2; AT3G24120.2; AT3G24120. [Q94A57-2]
DR GeneID; 821998; -.
DR Gramene; AT3G24120.1; AT3G24120.1; AT3G24120. [Q94A57-1]
DR Gramene; AT3G24120.2; AT3G24120.2; AT3G24120. [Q94A57-2]
DR KEGG; ath:AT3G24120; -.
DR Araport; AT3G24120; -.
DR TAIR; locus:2093726; AT3G24120.
DR eggNOG; ENOG502QVJ9; Eukaryota.
DR HOGENOM; CLU_053944_2_2_1; -.
DR OMA; QACKETT; -.
DR OrthoDB; 1021540at2759; -.
DR PhylomeDB; Q94A57; -.
DR PRO; PR:Q94A57; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94A57; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS: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..295
FT /note="Protein PHR1-LIKE 2"
FT /id="PRO_0000436859"
FT DOMAIN 38..98
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 69..94
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 96..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 141..161
FT /evidence="ECO:0000255"
FT MOTIF 154..159
FT /note="LHEQLE"
FT /evidence="ECO:0000305"
FT COMPBIAS 105..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 159
FT /note="E -> EYGQ (in isoform 2)"
FT /id="VSP_058429"
SQ SEQUENCE 295 AA; 32205 MW; C9407461F35B76B0 CRC64;
MYSAIRSLPL DGGHVGGDYH GPLDGTNLPG DACLVLTTDP KPRLRWTTEL HERFVDAVTQ
LGGPDKATPK TIMRTMGVKG LTLYHLKSHL QKFRLGRQAG KESTENSKDA SCVGESQDTG
SSSTSSMRMA QQEQNEGYQV TEALRAQMEV QRRLHDQLEV QRRLQLRIEA QGKYLQSILE
KACKAFDEQA ATFAGLEAAR EELSELAIKV SNSSQGTSVP YFDATKMMMM PSLSELAVAI
DNKNNITTNC SVESSLTSIT HGSSISAASM KKRQRGDNLG VGYESGWIMP SSTIG
