PHL9_ARATH
ID PHL9_ARATH Reviewed; 394 AA.
AC Q9SQQ9; B3H651; E3VS07; Q8VXV5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Myb-related protein 2 {ECO:0000303|PubMed:21255164};
DE AltName: Full=Myb family transcription factor PHL9 {ECO:0000305};
DE AltName: Full=Protein NITROGEN STARVATION RESPONSE 1 {ECO:0000303|PubMed:15592750};
DE Short=AtNSR1 {ECO:0000303|PubMed:15592750};
DE AltName: Full=Protein PHR1-LIKE 9 {ECO:0000305};
GN Name=MYR2 {ECO:0000303|PubMed:21255164};
GN Synonyms=NSR1 {ECO:0000303|PubMed:15592750}, PHL9 {ECO:0000305};
GN OrderedLocusNames=At3g04030 {ECO:0000312|Araport:AT3G04030};
GN ORFNames=T11I18.14 {ECO:0000312|EMBL:AAF05867.1};
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 4), FUNCTION, AND DISRUPTION PHENOTYPE.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 2).
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 INDUCTION BY NITROGEN, AND FUNCTION.
RX PubMed=15592750; DOI=10.1007/s00425-004-1305-7;
RA Todd C.D., Zeng P., Huete A.M., Hoyos M.E., Polacco J.C.;
RT "Transcripts of MYB-like genes respond to phosphorous and nitrogen
RT deprivation in Arabidopsis.";
RL Planta 219:1003-1009(2004).
RN [7]
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 [8]
RP ALTERNATIVE SPLICING, SUBUNIT (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION
RP (ISOFORMS 1 AND 3), AND MUTAGENESIS OF LYS-70; THR-72; LYS-74 AND LYS-78.
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: Transcriptional activator that may activate the transcription
CC of specific genes involved in nitrogen uptake or assimilation
CC (PubMed:15592750). Acts redundantly with MYR1 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:15592750}.
CC -!- SUBUNIT: Isoform 1: Homodimer. Isoform 3: Does not form homodimer.
CC {ECO:0000269|PubMed:24309816}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:24309816}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:24309816}. Note=In 21% of the cells, localized to
CC one or more spots within the nucleus due to protein aggregation.
CC {ECO:0000305|PubMed:24309816}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9SQQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SQQ9-2; Sequence=VSP_058436;
CC Name=3;
CC IsoId=Q9SQQ9-3; Sequence=VSP_058435;
CC Name=4;
CC IsoId=Q9SQQ9-4; Sequence=VSP_058437;
CC -!- TISSUE SPECIFICITY: Expressed in phloem and/or cambium.
CC {ECO:0000269|PubMed:15923329}.
CC -!- INDUCTION: Up-regulated by nitrogen deficiency.
CC {ECO:0000269|PubMed:15592750}.
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}.
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DR EMBL; HQ222089; ADO32622.1; -; mRNA.
DR EMBL; AC011698; AAF05867.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74027.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74028.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74029.1; -; Genomic_DNA.
DR EMBL; AY074563; AAL67103.1; -; mRNA.
DR EMBL; AY143915; AAN28854.1; -; mRNA.
DR RefSeq; NP_001118567.1; NM_001125095.2. [Q9SQQ9-1]
DR RefSeq; NP_187053.2; NM_111274.4. [Q9SQQ9-2]
DR RefSeq; NP_974216.1; NM_202487.1. [Q9SQQ9-3]
DR AlphaFoldDB; Q9SQQ9; -.
DR SMR; Q9SQQ9; -.
DR STRING; 3702.AT3G04030.3; -.
DR PaxDb; Q9SQQ9; -.
DR PRIDE; Q9SQQ9; -.
DR ProteomicsDB; 236749; -. [Q9SQQ9-1]
DR EnsemblPlants; AT3G04030.1; AT3G04030.1; AT3G04030. [Q9SQQ9-2]
DR EnsemblPlants; AT3G04030.2; AT3G04030.2; AT3G04030. [Q9SQQ9-3]
DR EnsemblPlants; AT3G04030.3; AT3G04030.3; AT3G04030. [Q9SQQ9-1]
DR GeneID; 819558; -.
DR Gramene; AT3G04030.1; AT3G04030.1; AT3G04030. [Q9SQQ9-2]
DR Gramene; AT3G04030.2; AT3G04030.2; AT3G04030. [Q9SQQ9-3]
DR Gramene; AT3G04030.3; AT3G04030.3; AT3G04030. [Q9SQQ9-1]
DR KEGG; ath:AT3G04030; -.
DR Araport; AT3G04030; -.
DR TAIR; locus:2095933; AT3G04030.
DR eggNOG; ENOG502QT7M; Eukaryota.
DR HOGENOM; CLU_053944_3_0_1; -.
DR InParanoid; Q9SQQ9; -.
DR OMA; MEKICES; -.
DR OrthoDB; 828397at2759; -.
DR PhylomeDB; Q9SQQ9; -.
DR BioCyc; ARA:AT1G11680-MON; -.
DR PRO; PR:Q9SQQ9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SQQ9; 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..394
FT /note="Myb-related protein 2"
FT /id="PRO_0000436866"
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 148..168
FT /note="Coiled coil"
FT /evidence="ECO:0000305"
FT REGION 338..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..166
FT /note="LHEQLE"
FT /evidence="ECO:0000305"
FT COMPBIAS 345..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 70..71
FT /note="KA -> T (in isoform 3)"
FT /id="VSP_058435"
FT VAR_SEQ 167..172
FT /note="Missing (in isoform 2)"
FT /id="VSP_058436"
FT VAR_SEQ 167..168
FT /note="Missing (in isoform 4)"
FT /id="VSP_058437"
FT MUTAGEN 70
FT /note="K->A: Partly directed to one or more nuclear spots.
FT Partly located to extra-nuclear aggregates; when associated
FT with A-74 or A-78. Complete loss of nuclear localization;
FT when associated with A-74 and A-78."
FT /evidence="ECO:0000269|PubMed:24309816"
FT MUTAGEN 70
FT /note="K->R: No effect on nuclear localization. No effect
FT nuclear localization; when associated with R-74 and R-78."
FT /evidence="ECO:0000269|PubMed:24309816"
FT MUTAGEN 72
FT /note="T->A: In isoform 1 and isoform 3; no effect on
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:24309816"
FT MUTAGEN 72
FT /note="T->E: In isoform 1; partial localization to one or
FT more nuclear spots. In isoform 3; increased localization to
FT nuclear spots."
FT /evidence="ECO:0000269|PubMed:24309816"
FT MUTAGEN 74
FT /note="K->A: Partly directed to one or more nuclear spots.
FT Partly located to extra-nuclear aggregates; when associated
FT with A-70 or A-78. Complete loss of nuclear localization;
FT when associated with A-74 and A-78."
FT /evidence="ECO:0000269|PubMed:24309816"
FT MUTAGEN 74
FT /note="K->R: No effect on nuclear localization. No effect
FT nuclear localization; when associated with R-70 and R-78."
FT /evidence="ECO:0000269|PubMed:24309816"
FT MUTAGEN 78
FT /note="K->A: Partly located to extra-nuclear aggregates;
FT when associated with A-70 or A-74. Complete loss of nuclear
FT localization; when associated with A-70 and A-74."
FT /evidence="ECO:0000269|PubMed:24309816"
FT MUTAGEN 78
FT /note="K->R: No effect on nuclear localization. No effect
FT nuclear localization; when associated with R-70 and R-74."
FT /evidence="ECO:0000269|PubMed:24309816"
SQ SEQUENCE 394 AA; 44612 MW; 435D9D06FF7D9724 CRC64;
MYYQNQHQGK NILSSSRMHI TSERHPFLRG NSPGDSGLIL STDAKPRLKW TPDLHERFIE
AVNQLGGADK ATPKTIMKVM GIPGLTLYHL KSHLQKYRLS KNLNGQANNS FNKIGIMTMM
EEKTPDADEI QSENLSIGPQ PNKNSPIGEA LQMQIEVQRR LHEQLEVQRH LQLRIEAQGK
YLQSVLEKAQ ETLGRQNLGA AGIEAAKVQL SELVSKVSAE YPNSSFLEPK ELQNLCSQQM
QTNYPPDCSL ESCLTSSEGT QKNSKMLENN RLGLRTYIGD STSEQKEIME EPLFQRMELT
WTEGLRGNPY LSTMVSEAEQ RISYSERSPG RLSIGVGLHG HKSQHQQGNN EDHKLETRNR
KGMDSTTELD LNTHVENYCT TRTKQFDLNG FSWN