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PHL3_ARATH
ID   PHL3_ARATH              Reviewed;         292 AA.
AC   Q8LAJ7; F4JTR5; Q8RXE4; Q9SVP8;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Protein PHR1-LIKE 3 {ECO:0000303|PubMed:26586833};
DE   AltName: Full=Myb family transcription factor PHL3 {ECO:0000303|PubMed:26586833};
DE   AltName: Full=Protein UNFERTILIZED EMBRYO SAC 16 {ECO:0000303|PubMed:15634699};
GN   Name=PHL3 {ECO:0000303|PubMed:26586833};
GN   Synonyms=UNE16 {ECO:0000303|PubMed:15634699};
GN   OrderedLocusNames=At4g13640 {ECO:0000312|Araport:AT4G13640};
GN   ORFNames=F18A5.30 {ECO:0000312|EMBL:CAB36828.1};
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:AAM65307.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
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   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15634699; DOI=10.1242/dev.01595;
RA   Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA   Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT   "Genetic and molecular identification of genes required for female
RT   gametophyte development and function in Arabidopsis.";
RL   Development 132:603-614(2005).
RN   [8]
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   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PHL2, SUBUNIT, INDUCTION
RP   BY PHOSPHATE, AND DISRUPTION PHENOTYPE.
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). Probable
CC       component of the central regulatory system controlling transcriptional
CC       responses to Pi starvation (PubMed:26586833). Binds in a sequence-
CC       specific manner to phosphate starvation-regulated promoters
CC       (PubMed:26586833). Required for female gametophyte development and
CC       function (PubMed:15634699). {ECO:0000269|PubMed:15634699,
CC       ECO:0000269|PubMed:26586833}.
CC   -!- SUBUNIT: Homo- and heterodimers (PubMed:26586833). Interacts with PHL2,
CC       but not with PHR1 (PubMed:26586833). {ECO:0000269|PubMed:26586833}.
CC   -!- INTERACTION:
CC       Q8LAJ7; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-4443730, EBI-2000137;
CC       Q8LAJ7; P93830: IAA17; NbExp=3; IntAct=EBI-4443730, EBI-632243;
CC       Q8LAJ7; Q9FNZ4: NIMIN-3; NbExp=3; IntAct=EBI-4443730, EBI-541115;
CC       Q8LAJ7; Q9FL03: SCL4; NbExp=3; IntAct=EBI-4443730, EBI-1238466;
CC       Q8LAJ7; O81316: SCL6; NbExp=3; IntAct=EBI-4443730, EBI-4428591;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26586833}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8LAJ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8LAJ7-2; Sequence=VSP_058430;
CC   -!- INDUCTION: Up-regulated in roots by low Pi.
CC       {ECO:0000269|PubMed:26586833}.
CC   -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000269|PubMed:15634699,
CC       ECO:0000269|PubMed:26586833}.
CC   -!- SIMILARITY: Belongs to the MYB-CC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL91199.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=CAB36828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78406.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035528; CAB36828.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161537; CAB78406.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83307.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83308.1; -; Genomic_DNA.
DR   EMBL; AY081310; AAL91199.1; ALT_SEQ; mRNA.
DR   EMBL; AY114630; AAM47949.1; -; mRNA.
DR   EMBL; AK226443; BAE98586.1; -; mRNA.
DR   EMBL; AY087771; AAM65307.1; -; mRNA.
DR   PIR; T05233; T05233.
DR   RefSeq; NP_001031626.1; NM_001036549.2. [Q8LAJ7-2]
DR   RefSeq; NP_567408.1; NM_117438.4. [Q8LAJ7-1]
DR   AlphaFoldDB; Q8LAJ7; -.
DR   SMR; Q8LAJ7; -.
DR   IntAct; Q8LAJ7; 13.
DR   STRING; 3702.AT4G13640.2; -.
DR   PRIDE; Q8LAJ7; -.
DR   ProteomicsDB; 236314; -. [Q8LAJ7-1]
DR   EnsemblPlants; AT4G13640.1; AT4G13640.1; AT4G13640. [Q8LAJ7-1]
DR   EnsemblPlants; AT4G13640.2; AT4G13640.2; AT4G13640. [Q8LAJ7-2]
DR   GeneID; 826998; -.
DR   Gramene; AT4G13640.1; AT4G13640.1; AT4G13640. [Q8LAJ7-1]
DR   Gramene; AT4G13640.2; AT4G13640.2; AT4G13640. [Q8LAJ7-2]
DR   KEGG; ath:AT4G13640; -.
DR   Araport; AT4G13640; -.
DR   TAIR; locus:2119425; AT4G13640.
DR   eggNOG; ENOG502QVJ9; Eukaryota.
DR   HOGENOM; CLU_053944_2_2_1; -.
DR   OMA; NLPVDAC; -.
DR   OrthoDB; 1021540at2759; -.
DR   PhylomeDB; Q8LAJ7; -.
DR   PRO; PR:Q8LAJ7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8LAJ7; 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:0009567; P:double fertilization forming a zygote and endosperm; IMP:TAIR.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA: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..292
FT                   /note="Protein PHR1-LIKE 3"
FT                   /id="PRO_0000436860"
FT   DOMAIN          34..94
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        65..90
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   COILED          137..157
FT                   /evidence="ECO:0000255"
FT   MOTIF           150..155
FT                   /note="LHEQLE"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         155
FT                   /note="E -> EYTQ (in isoform 2)"
FT                   /id="VSP_058430"
SQ   SEQUENCE   292 AA;  31723 MW;  AD1045B06E7079B9 CRC64;
     MYSAIRSSLP LDGSLGDYSD GTNLPIDACL VLTTDPKPRL RWTSELHERF VDAVTQLGGP
     DKATPKTIMR TMGVKGLTLY HLKSHLQKFR LGRQSCKESI DNSKDVSCVA ESQDTGSSST
     SSLRLAAQEQ NESYQVTEAL RAQMEVQRRL HEQLEVQRRL QLRIEAQGKY LQSILEKACK
     AIEEQAVAFA GLEAAREELS ELAIKASITN GCQGTTSTFD TTKMMIPSLS ELAVAIEHKN
     NCSAESSLTS STVGSPVSAA LMKKRQRGVF GNGDSVVVGH DAGWVMPSSS IG
 
 
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