FHY3_ARATH
ID FHY3_ARATH Reviewed; 839 AA.
AC Q9LIE5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein FAR-RED ELONGATED HYPOCOTYL 3;
GN Name=FHY3; OrderedLocusNames=At3g22170; ORFNames=MKA23.12;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 IDENTIFICATION, MUTANTS FHY3-9 AND FHY3-10, FUNCTION, INDUCTION,
RP INTERACTION WITH FAR1, AND SUBCELLULAR LOCATION.
RX PubMed=11889039; DOI=10.1093/emboj/21.6.1339;
RA Wang H., Deng X.W.;
RT "Arabidopsis FHY3 defines a key phytochrome A signaling component directly
RT interacting with its homologous partner FAR1.";
RL EMBO J. 21:1339-1349(2002).
RN [4]
RP FUNCTION.
RX PubMed=12753585; DOI=10.1046/j.1365-313x.2003.01741.x;
RA Hudson M.E., Lisch D.R., Quail P.H.;
RT "The FHY3 and FAR1 genes encode transposase-related proteins involved in
RT regulation of gene expression by the phytochrome A-signaling pathway.";
RL Plant J. 34:453-471(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15591448; DOI=10.1104/pp.104.052191;
RA Lin R., Wang H.;
RT "Arabidopsis FHY3/FAR1 gene family and distinct roles of its members in
RT light control of Arabidopsis development.";
RL Plant Physiol. 136:4010-4022(2004).
RN [6]
RP FUNCTION.
RX PubMed=17012604; DOI=10.1105/tpc.105.037358;
RA Allen T., Koustenis A., Theodorou G., Somers D.E., Kay S.A., Whitelam G.C.,
RA Devlin P.F.;
RT "Arabidopsis FHY3 specifically gates phytochrome signaling to the circadian
RT clock.";
RL Plant Cell 18:2506-2516(2006).
RN [7]
RP FUNCTION, CHARACTERIZATION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18033885; DOI=10.1126/science.1146281;
RA Lin R., Ding L., Casola C., Ripoll D.R., Feschotte C., Wang H.;
RT "Transposase-derived transcription factors regulate light signaling in
RT Arabidopsis.";
RL Science 318:1302-1305(2007).
RN [8]
RP INTERACTION WITH PHYA, AND SUBCELLULAR LOCATION.
RX PubMed=18722184; DOI=10.1016/j.molcel.2008.08.003;
RA Saijo Y., Zhu D., Li J., Rubio V., Zhou Z., Shen Y., Hoecker U., Wang H.,
RA Deng X.W.;
RT "Arabidopsis COP1/SPA1 complex and FHY1/FHY3 associate with distinct
RT phosphorylated forms of phytochrome A in balancing light signaling.";
RL Mol. Cell 31:607-613(2008).
RN [9]
RP FUNCTION, MUTAGENESIS OF CYS-118; CYS-157; HIS-180; HIS-182; ASP-288;
RP GLU-323; CYS-579 AND HIS-591, AND SUBCELLULAR LOCATION.
RX PubMed=18715961; DOI=10.1104/pp.108.120436;
RA Lin R., Teng Y., Park H.-J., Ding L., Black C., Fang P., Wang H.;
RT "Discrete and essential roles of the multiple domains of Arabidopsis FHY3
RT in mediating phytochrome A signal transduction.";
RL Plant Physiol. 148:981-992(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP FUNCTION, INTERACTION WITH PIF1, DISRUPTION PHENOTYPE, AND INDUCTION BY
RP LIGHT.
RX PubMed=22634759; DOI=10.1105/tpc.112.097022;
RA Tang W., Wang W., Chen D., Ji Q., Jing Y., Wang H., Lin R.;
RT "Transposase-derived proteins FHY3/FAR1 interact with PHYTOCHROME-
RT INTERACTING FACTOR1 to regulate chlorophyll biosynthesis by modulating
RT HEMB1 during deetiolation in Arabidopsis.";
RL Plant Cell 24:1984-2000(2012).
CC -!- FUNCTION: Transcription activator that recognizes and binds to the DNA
CC consensus sequence 5'-CACGCGC-3'. Activates the expression of FHY1 and
CC FHL involved in light responses. When associated with PHYA, protects it
CC from being recognized and degraded by the COP1/SPA complex. Positive
CC regulator of chlorophyll biosynthesis via the activation of HEMB1 gene
CC expression. {ECO:0000269|PubMed:11889039, ECO:0000269|PubMed:12753585,
CC ECO:0000269|PubMed:17012604, ECO:0000269|PubMed:18033885,
CC ECO:0000269|PubMed:18715961, ECO:0000269|PubMed:22634759}.
CC -!- SUBUNIT: Homodimer and heterodimer with FAR1. Interacts (via N-
CC terminus) with PIF1 and with underphosphorylated PHYA.
CC {ECO:0000269|PubMed:11889039, ECO:0000269|PubMed:18722184,
CC ECO:0000269|PubMed:22634759}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11889039,
CC ECO:0000269|PubMed:18033885, ECO:0000269|PubMed:18715961,
CC ECO:0000269|PubMed:18722184}.
CC -!- INDUCTION: Down-regulated after exposure to far-red light. Subject to a
CC negative feedback regulation by PHYA signaling. Up-regulated by white
CC light. {ECO:0000269|PubMed:11889039, ECO:0000269|PubMed:18033885,
CC ECO:0000269|PubMed:22634759}.
CC -!- DOMAIN: The FAR1 domain is involved in direct DNA binding, the SWIM-
CC type zinc finger is essential for transcriptional activation activity
CC and both the MULE and SWIM domains are essential for dimerization.
CC -!- DISRUPTION PHENOTYPE: Reduced protochlorophyllide levels in darkness
CC and less photobleaching in the light. {ECO:0000269|PubMed:22634759}.
CC -!- SIMILARITY: Belongs to the FHY3/FAR1 family. {ECO:0000305}.
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DR EMBL; AP001306; BAB03065.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76596.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76597.1; -; Genomic_DNA.
DR RefSeq; NP_001118673.1; NM_001125201.2.
DR RefSeq; NP_188856.2; NM_113114.3.
DR AlphaFoldDB; Q9LIE5; -.
DR BioGRID; 7113; 7.
DR STRING; 3702.AT3G22170.2; -.
DR iPTMnet; Q9LIE5; -.
DR PaxDb; Q9LIE5; -.
DR PRIDE; Q9LIE5; -.
DR ProteomicsDB; 230576; -.
DR EnsemblPlants; AT3G22170.1; AT3G22170.1; AT3G22170.
DR EnsemblPlants; AT3G22170.2; AT3G22170.2; AT3G22170.
DR GeneID; 821781; -.
DR Gramene; AT3G22170.1; AT3G22170.1; AT3G22170.
DR Gramene; AT3G22170.2; AT3G22170.2; AT3G22170.
DR KEGG; ath:AT3G22170; -.
DR Araport; AT3G22170; -.
DR TAIR; locus:2090394; AT3G22170.
DR eggNOG; ENOG502QPXR; Eukaryota.
DR HOGENOM; CLU_008459_7_1_1; -.
DR InParanoid; Q9LIE5; -.
DR OMA; ENRDATC; -.
DR OrthoDB; 197084at2759; -.
DR PhylomeDB; Q9LIE5; -.
DR PRO; PR:Q9LIE5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIE5; baseline and differential.
DR Genevisible; Q9LIE5; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007623; P:circadian rhythm; IMP:TAIR.
DR GO; GO:1900056; P:negative regulation of leaf senescence; IMP:TAIR.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0010017; P:red or far-red light signaling pathway; IMP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IMP:TAIR.
DR GO; GO:0010218; P:response to far red light; IMP:TAIR.
DR InterPro; IPR004330; FAR1_DNA_bnd_dom.
DR InterPro; IPR031052; FHY3/FAR1.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR018289; MULE_transposase_dom.
DR InterPro; IPR006564; Znf_PMZ.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR31669; PTHR31669; 1.
DR Pfam; PF03101; FAR1; 1.
DR Pfam; PF10551; MULE; 1.
DR SMART; SM00575; ZnF_PMZ; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Phytochrome signaling pathway; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..839
FT /note="Protein FAR-RED ELONGATED HYPOCOTYL 3"
FT /id="PRO_0000363477"
FT DOMAIN 84..186
FT /note="FAR1"
FT DOMAIN 284..380
FT /note="MULE"
FT ZN_FING 564..600
FT /note="SWIM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT REGION 128..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 118
FT /note="C->A: Loss of DNA binding. Loss of DNA binding; when
FT associated with A-157; A-180 and A-182."
FT /evidence="ECO:0000269|PubMed:18715961"
FT MUTAGEN 157
FT /note="C->A: Loss of DNA binding. Loss of DNA binding; when
FT associated with A-180 and A-182. Loss of DNA binding; when
FT associated with A-118; A-180 and A-182."
FT /evidence="ECO:0000269|PubMed:18715961"
FT MUTAGEN 180
FT /note="H->A: Loss of DNA binding; when associated with A-
FT 157 and A-182. Loss of DNA binding; when associated with A-
FT 118; A-157 and A-182."
FT /evidence="ECO:0000269|PubMed:18715961"
FT MUTAGEN 182
FT /note="H->A: Loss of DNA binding; when associated with A-
FT 157 and A-180. Loss of DNA binding; when associated with A-
FT 118; A-157 and A-180."
FT /evidence="ECO:0000269|PubMed:18715961"
FT MUTAGEN 283
FT /note="D->N: In fhy3-10; loss of dimerization and loss of
FT transcriptional activation activity."
FT MUTAGEN 288
FT /note="D->A: Loss of dimerization and partial loss of
FT transcriptional activation activity."
FT /evidence="ECO:0000269|PubMed:18715961"
FT MUTAGEN 305
FT /note="G->R: In fhy3-9; loss of dimerization and loss of
FT transcriptional activation activity."
FT MUTAGEN 323
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:18715961"
FT MUTAGEN 579
FT /note="C->A: Loss of dimerization and loss of
FT transcriptional activation activity."
FT /evidence="ECO:0000269|PubMed:18715961"
FT MUTAGEN 591
FT /note="H->A: Loss of dimerization and loss of
FT transcriptional activation activity."
FT /evidence="ECO:0000269|PubMed:18715961"
SQ SEQUENCE 839 AA; 95996 MW; CBBF60DF8B6797F8 CRC64;
MDIDLRLHSG DLCKGDDEDR GLDNVLHNEE DMDIGKIEDV SVEVNTDDSV GMGVPTGELV
EYTEGMNLEP LNGMEFESHG EAYSFYQEYS RAMGFNTAIQ NSRRSKTTRE FIDAKFACSR
YGTKREYDKS FNRPRARQSK QDPENMAGRR TCAKTDCKAS MHVKRRPDGK WVIHSFVREH
NHELLPAQAV SEQTRKIYAA MAKQFAEYKT VISLKSDSKS SFEKGRTLSV ETGDFKILLD
FLSRMQSLNS NFFYAVDLGD DQRVKNVFWV DAKSRHNYGS FCDVVSLDTT YVRNKYKMPL
AIFVGVNQHY QYMVLGCALI SDESAATYSW LMETWLRAIG GQAPKVLITE LDVVMNSIVP
EIFPNTRHCL FLWHVLMKVS ENLGQVVKQH DNFMPKFEKC IYKSGKDEDF ARKWYKNLAR
FGLKDDQWMI SLYEDRKKWA PTYMTDVLLA GMSTSQRADS INAFFDKYMH KKTSVQEFVK
VYDTVLQDRC EEEAKADSEM WNKQPAMKSP SPFEKSVSEV YTPAVFKKFQ IEVLGAIACS
PREENRDATC STFRVQDFEN NQDFMVTWNQ TKAEVSCICR LFEYKGYLCR HTLNVLQCCH
LSSIPSQYIL KRWTKDAKSR HFSGEPQQLQ TRLLRYNDLC ERALKLNEEA SLSQESYNIA
FLAIEGAIGN CAGINTSGRS LPDVVTSPTQ GLISVEEDNH SRSAGKTSKK KNPTKKRKVN
PEQDVMPVAA PESLQQMDKL SPRTVGIESY YGTQQSVQGM VQLNLMGPTR DNFYGNQQTM
QGLRQLNSIA PSYDSYYGPQ QGIHGQGVDF FRPANFSYDI RDDPNVRTTQ LHEDASRHS
