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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
 
 
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