PHL1_ARATH
ID PHL1_ARATH Reviewed; 413 AA.
AC Q8GUN5; B3H6E5; F4KBG7; Q8LEY3;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein PHR1-LIKE 1;
DE AltName: Full=Myb-like transcription factor 1;
GN Name=PHL1; OrderedLocusNames=At5g29000; ORFNames=F3F24.100;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] (ISOFORM 1).
RA Yamada K., Chan M.M., Chang C.H., Dale J.M., Hsuan V.W., Lee J.M.,
RA Onodera C.S., Quach H.L., Tang C.C., Toriumi M., Wong C., Wu H.C., Yu G.,
RA Yuan S., Chen H., Cheuk R., Jones T., Kim C.J., Nguyen M., Palm C.J.,
RA Shinn P., Southwick A., Tripp M.G., Wu T., Davis R.W., Ecker J.R.,
RA Theologis A.;
RT "Arabidopsis open reading frame (ORF) clones.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=20838596; DOI=10.1371/journal.pgen.1001102;
RA Bustos R., Castrillo G., Linhares F., Puga M.I., Rubio V., Perez-Perez J.,
RA Solano R., Leyva A., Paz-Ares J.;
RT "A central regulatory system largely controls transcriptional activation
RT and repression responses to phosphate starvation in Arabidopsis.";
RL PLoS Genet. 6:E1001102-E1001102(2010).
RN [7]
RP INTERACTION WITH MED25.
RX PubMed=21343311; DOI=10.1093/mp/ssr002;
RA Ou B., Yin K.Q., Liu S.N., Yang Y., Gu T., Wing Hui J.M., Zhang L.,
RA Miao J., Kondou Y., Matsui M., Gu H.Y., Qu L.J.;
RT "A high-throughput screening system for Arabidopsis transcription factors
RT and its application to Med25-dependent transcriptional regulation.";
RL Mol. Plant 4:546-555(2011).
RN [8]
RP INTERACTION WITH MED25.
RX PubMed=21536906; DOI=10.1073/pnas.1002981108;
RA Elfving N., Davoine C., Benlloch R., Blomberg J., Braennstroem K.,
RA Mueller D., Nilsson A., Ulfstedt M., Ronne H., Wingsle G., Nilsson O.,
RA Bjoerklund S.;
RT "The Arabidopsis thaliana Med25 mediator subunit integrates environmental
RT cues to control plant development.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8245-8250(2011).
RN [9]
RP FUNCTION.
RX PubMed=23788639; DOI=10.1074/jbc.m113.482281;
RA Bournier M., Tissot N., Mari S., Boucherez J., Lacombe E., Briat J.F.,
RA Gaymard F.;
RT "Arabidopsis ferritin 1 (AtFer1) gene regulation by the phosphate
RT starvation response 1 (AtPHR1) transcription factor reveals a direct
RT molecular link between iron and phosphate homeostasis.";
RL J. Biol. Chem. 288:22670-22680(2013).
RN [10]
RP LACK OF INTERACTION WITH PHL2 OR PHL3, AND LACK OF 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: Transcription factor acting as central integrator of
CC phosphate starvation responses (PubMed:20838596). Regulates FER1
CC expression upon phosphate starvation, linking iron and phosphate
CC homeostasis (PubMed:23788639). {ECO:0000269|PubMed:20838596,
CC ECO:0000269|PubMed:23788639}.
CC -!- SUBUNIT: Homodimers and heterodimers (PubMed:20838596). Interacts with
CC MED25 (PubMed:21343311, PubMed:21536906). Does not interact with PHL2
CC or PHL3 (PubMed:26586833). {ECO:0000269|PubMed:20838596,
CC ECO:0000269|PubMed:21343311, ECO:0000269|PubMed:21536906,
CC ECO:0000269|PubMed:26586833}.
CC -!- INTERACTION:
CC Q8GUN5-2; Q7XYY2-1: MED25; NbExp=2; IntAct=EBI-15924466, EBI-15924435;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8GUN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GUN5-2; Sequence=VSP_043994;
CC Name=3;
CC IsoId=Q8GUN5-3; Sequence=VSP_043995, VSP_043996;
CC -!- TISSUE SPECIFICITY: Expressed in shoots and roots.
CC {ECO:0000269|PubMed:20838596}.
CC -!- INDUCTION: Not up-regulated by Pi starvation.
CC {ECO:0000269|PubMed:26586833}.
CC -!- DISRUPTION PHENOTYPE: No effect on phosphate starvation responsiveness,
CC due to the redundancy with PHR1. {ECO:0000269|PubMed:20838596}.
CC -!- SIMILARITY: Belongs to the MYB-CC family. {ECO:0000305}.
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DR EMBL; AC018632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93856.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93857.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93858.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93859.1; -; Genomic_DNA.
DR EMBL; BT002344; AAN86177.1; -; mRNA.
DR EMBL; AY085154; AAM61707.1; -; mRNA.
DR RefSeq; NP_001078629.1; NM_001085160.2. [Q8GUN5-2]
DR RefSeq; NP_001119299.1; NM_001125827.1. [Q8GUN5-3]
DR RefSeq; NP_568512.3; NM_122784.5. [Q8GUN5-1]
DR RefSeq; NP_851090.1; NM_180759.4. [Q8GUN5-2]
DR AlphaFoldDB; Q8GUN5; -.
DR SMR; Q8GUN5; -.
DR BioGRID; 18298; 8.
DR DIP; DIP-60341N; -.
DR IntAct; Q8GUN5; 1.
DR STRING; 3702.AT5G29000.2; -.
DR PaxDb; Q8GUN5; -.
DR PRIDE; Q8GUN5; -.
DR ProteomicsDB; 236144; -. [Q8GUN5-1]
DR EnsemblPlants; AT5G29000.1; AT5G29000.1; AT5G29000. [Q8GUN5-2]
DR EnsemblPlants; AT5G29000.2; AT5G29000.2; AT5G29000. [Q8GUN5-1]
DR EnsemblPlants; AT5G29000.3; AT5G29000.3; AT5G29000. [Q8GUN5-2]
DR EnsemblPlants; AT5G29000.4; AT5G29000.4; AT5G29000. [Q8GUN5-3]
DR GeneID; 833026; -.
DR Gramene; AT5G29000.1; AT5G29000.1; AT5G29000. [Q8GUN5-2]
DR Gramene; AT5G29000.2; AT5G29000.2; AT5G29000. [Q8GUN5-1]
DR Gramene; AT5G29000.3; AT5G29000.3; AT5G29000. [Q8GUN5-2]
DR Gramene; AT5G29000.4; AT5G29000.4; AT5G29000. [Q8GUN5-3]
DR KEGG; ath:AT5G29000; -.
DR Araport; AT5G29000; -.
DR TAIR; locus:2148720; AT5G29000.
DR eggNOG; ENOG502RQ9X; Eukaryota.
DR InParanoid; Q8GUN5; -.
DR OMA; HNEPASA; -.
DR PhylomeDB; Q8GUN5; -.
DR PRO; PR:Q8GUN5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GUN5; baseline and differential.
DR Genevisible; Q8GUN5; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; PTHR31314; PTHR31314; 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; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..413
FT /note="Protein PHR1-LIKE 1"
FT /id="PRO_0000418125"
FT DOMAIN 228..288
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 259..284
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 171..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..342
FT /note="Coiled coil"
FT /evidence="ECO:0000305"
FT REGION 363..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 335..340
FT /note="LHEQLE"
FT /evidence="ECO:0000305"
FT COMPBIAS 176..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_043994"
FT VAR_SEQ 298..311
FT /note="EPQEKKMTSIEDIK -> KELKYFNIILLHFF (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_043995"
FT VAR_SEQ 312..413
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_043996"
FT CONFLICT 26
FT /note="D -> H (in Ref. 4; AAM61707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46221 MW; 739BAB69CD76C047 CRC64;
MTLANDFGYS TAMSSSYSAL HTSVEDRYHK LPNSFWVSSG QELMNNPVPC QSVSGGNSGG
YLFPSSSGYC NVSAVLPHGR NLQNQPPVST VPRDRLAMQD CPLIAQSSLI NHHPQEFIDP
LHEFFDFSDH VPVQNLQAES SGVRVDSSVE LHKKSEWQDW ADQLISVDDG SEPNWSELLG
DSSSHNPNSE IPTPFLDVPR LDITANQQQQ MVSSEDQLSG RNSSSSVATS KQRMRWTPEL
HEAFVEAVNQ LGGSERATPK AVLKLLNNPG LTIYHVKSHL QKYRTARYKP ETSEVTGEPQ
EKKMTSIEDI KSLDMKTSVE ITQALRLQME VQKRLHEQLE IQRSLQLQIE KQGRYLQMMF
EKQQKIQDNK SSSSEASPKQ CNGSFAEVEV GLETLTGDQN ESASASRKRV RED
