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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
 
 
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