FHY1_ARATH
ID FHY1_ARATH Reviewed; 202 AA.
AC Q8S4Q6; D5MAD1; D5MAD2; O80936; Q7Y200; Q8W565;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein FAR-RED ELONGATED HYPOCOTYL 1 {ECO:0000303|PubMed:11711433};
DE AltName: Full=Protein PHYTOCHROME A SIGNAL TRANSDUCTION 3 {ECO:0000303|PubMed:11726703};
GN Name=FHY1 {ECO:0000303|PubMed:11711433};
GN Synonyms=PAT3 {ECO:0000303|PubMed:11726703};
GN OrderedLocusNames=At2g37678 {ECO:0000312|Araport:AT2G37678};
GN ORFNames=F13M22 {ECO:0000305};
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 [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION,
RP DISRUPTION PHENOTYPE, INDUCTION BY FHY3 AND DARKNESS, TISSUE SPECIFICITY,
RP AND NUCLEAR LOCALIZATION AND NUCLEAR EXPORT MOTIFS.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11711433; DOI=10.1101/gad.205401;
RA Desnos T., Puente P., Whitelam G.C., Harberd N.P.;
RT "FHY1: a phytochrome A-specific signal transducer.";
RL Genes Dev. 15:2980-2990(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP INDUCTION BY LIGHT, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11726703; DOI=10.1093/pcp/pce177;
RA Zeidler M., Bolle C., Chua N.H.;
RT "The phytochrome A specific signaling component PAT3 is a positive
RT regulator of Arabidopsis photomorphogenesis.";
RL Plant Cell Physiol. 42:1193-1200(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND INDUCTION BY FAR-RED
RP LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=21097709; DOI=10.1105/tpc.110.075788;
RA Li J., Li G., Gao S., Martinez C., He G., Zhou Z., Huang X., Lee J.-H.,
RA Zhang H., Shen Y., Wang H., Deng X.W.;
RT "Arabidopsis transcription factor ELONGATED HYPOCOTYL5 plays a role in the
RT feedback regulation of phytochrome A signaling.";
RL Plant Cell 22:3634-3649(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8364355; DOI=10.2307/3869613;
RA Whitelam G.C., Johnson E., Peng J., Carol P., Anderson M.L., Cowl J.S.,
RA Harberd N.P.;
RT "Phytochrome A null mutants of Arabidopsis display a wild-type phenotype in
RT white light.";
RL Plant Cell 5:757-768(1993).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, NUCLEAR LOCALIZATION AND NUCLEAR EXPORT
RP MOTIFS, AND REGULATION BY FAR RED.
RC STRAIN=cv. Columbia;
RX PubMed=15469493; DOI=10.1111/j.1365-313x.2004.02212.x;
RA Zeidler M., Zhou Q., Sarda X., Yau C.-P., Chua N.-H.;
RT "The nuclear localization signal and the C-terminal region of FHY1 are
RT required for transmission of phytochrome A signals.";
RL Plant J. 40:355-365(2004).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, REPRESSION BY LIGHT, INTERACTION WITH FHL,
RP HOMODIMERIZATION, AND INDUCTION BY FHY3.
RX PubMed=16045472; DOI=10.1111/j.1365-313x.2005.02453.x;
RA Zhou Q., Hare P.D., Yang S.W., Zeidler M., Huang L.-F., Chua N.-H.;
RT "FHL is required for full phytochrome A signaling and shares overlapping
RT functions with FHY1.";
RL Plant J. 43:356-370(2005).
RN [11]
RP DEVELOPMENTAL STAGE, AND REGULATION BY LIGHT.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=16244150; DOI=10.1104/pp.105.067645;
RA Shen Y., Feng S., Ma L., Lin R., Qu L.-J., Chen Z., Wang H., Deng X.W.;
RT "Arabidopsis FHY1 protein stability is regulated by light via phytochrome A
RT and 26S proteasome.";
RL Plant Physiol. 139:1234-1243(2005).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17566111; DOI=10.1073/pnas.0703855104;
RA Roesler J., Klein I., Zeidler M.;
RT "Arabidopsis fhl/fhy1 double mutant reveals a distinct cytoplasmic action
RT of phytochrome A.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10737-10742(2007).
RN [13]
RP REGULATION BY FAR-RED LIGHT.
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 [14]
RP INTERACTION WITH PHYA.
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 [15]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION MOTIF.
RX PubMed=18670649; DOI=10.1371/journal.pgen.1000143;
RA Genoud T., Schweizer F., Tscheuschler A., Debrieux D., Casal J.J.,
RA Schaefer E., Hiltbrunner A., Fankhauser C.;
RT "FHY1 mediates nuclear import of the light-activated phytochrome A
RT photoreceptor.";
RL PLoS Genet. 4:E1000143-E1000143(2008).
RN [16]
RP PHOSPHORYLATION BY PHYA, INTERACTION WITH PHYA, AND REGULATION BY RED
RP LIGHT.
RX PubMed=19208901; DOI=10.1105/tpc.108.061259;
RA Shen Y., Zhou Z., Feng S., Li J., Tan-Wilson A., Qu L.J., Wang H.,
RA Deng X.W.;
RT "Phytochrome A mediates rapid red light-induced phosphorylation of
RT Arabidopsis FAR-RED ELONGATED HYPOCOTYL1 in a low fluence response.";
RL Plant Cell 21:494-506(2009).
RN [17]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP PHYA; LAF1 AND HFR1.
RC STRAIN=cv. Columbia;
RX PubMed=19482971; DOI=10.1105/tpc.109.067215;
RA Yang S.W., Jang I.-C., Henriques R., Chua N.-H.;
RT "FAR-RED ELONGATED HYPOCOTYL1 and FHY1-LIKE associate with the Arabidopsis
RT transcription factors LAF1 and HFR1 to transmit phytochrome A signals for
RT inhibition of hypocotyl elongation.";
RL Plant Cell 21:1341-1359(2009).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=18980642; DOI=10.1111/j.1365-313x.2008.03721.x;
RA Pfeiffer A., Kunkel T., Hiltbrunner A., Neuhaus G., Wolf I., Speth V.,
RA Adam E., Nagy F., Schaefer E.;
RT "A cell-free system for light-dependent nuclear import of phytochrome.";
RL Plant J. 57:680-689(2009).
RN [19]
RP REVIEW.
RX PubMed=22303272; DOI=10.1199/tab.0148;
RA Li J., Li G., Wang H., Deng X.W.;
RT "Phytochrome signaling mechanisms.";
RL Arabidopsis Book 9:E0148-E0148(2011).
RN [20]
RP INTERACTION WITH PHYA, AND SUBCELLULAR LOCATION.
RX PubMed=21884939; DOI=10.1016/j.cell.2011.07.023;
RA Rausenberger J., Tscheuschler A., Nordmeier W., Wuest F., Timmer J.,
RA Schaefer E., Fleck C., Hiltbrunner A.;
RT "Photoconversion and nuclear trafficking cycles determine phytochrome A's
RT response profile to far-red light.";
RL Cell 146:813-825(2011).
RN [21]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=22374392; DOI=10.1105/tpc.111.095083;
RA Kami C., Hersch M., Trevisan M., Genoud T., Hiltbrunner A., Bergmann S.,
RA Fankhauser C.;
RT "Nuclear phytochrome A signaling promotes phototropism in Arabidopsis.";
RL Plant Cell 24:566-576(2012).
RN [22]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-14; SER-39; SER-49 AND
RP THR-61, PHOSPHORYLATION AT SER-39 AND THR-61, INDUCTION BY PHYA, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22582101; DOI=10.1105/tpc.112.097733;
RA Chen F., Shi X., Chen L., Dai M., Zhou Z., Shen Y., Li J., Li G., Wei N.,
RA Deng X.W.;
RT "Phosphorylation of FAR-RED ELONGATED HYPOCOTYL1 is a key mechanism
RT defining signaling dynamics of phytochrome A under red and far-red light in
RT Arabidopsis.";
RL Plant Cell 24:1907-1920(2012).
RN [23]
RP INTERACTION WITH PHYA.
RX PubMed=21969386; DOI=10.1104/pp.111.186288;
RA Sokolova V., Bindics J., Kircher S., Adam E., Schaefer E., Nagy F.,
RA Viczian A.;
RT "Missense mutation in the amino terminus of phytochrome A disrupts the
RT nuclear import of the photoreceptor.";
RL Plant Physiol. 158:107-118(2012).
RN [24]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=25071219; DOI=10.1073/pnas.1412528111;
RA Chen F., Li B., Demone J., Charron J.-B., Shi X., Deng X.W.;
RT "Photoreceptor partner FHY1 has an independent role in gene modulation and
RT plant development under far-red light.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11888-11893(2014).
CC -!- FUNCTION: Key regulator of far red / red (FR/R) spectrum-specific
CC responses essential for the adaption to changing light conditions (e.g.
CC de-etiolation), essentially by regulating PHYA shuttling from the
CC cytoplasm to the nucleus and by directly regulating the expression of
CC some target genes, depending on light conditions and phosphorylation
CC status (PubMed:22582101). Binds chromatin at target genes promoters,
CC especially in FR light conditions (PubMed:25071219). Can activate
CC transcription of different genes, some being in a phytochrome A (PHYA)-
CC dependent and other in a PHYA-independent manners (PubMed:15469493,
CC PubMed:11726703, PubMed:25071219). Controls specific aspects of plant
CC development, such as the inhibition of seed germination under FR during
CC salt stress (PubMed:25071219). Essential for light-regulated PHYA
CC nuclear accumulation and subsequent PHYA phototropic signaling
CC processes involved in photomorphogenesis (PubMed:17566111,
CC PubMed:21969386, PubMed:25071219, PubMed:22374392, PubMed:19482971).
CC Mediates the association of PHYA with HFR1 and LAF1 in the nucleus in
CC response to FR conditions (PubMed:19482971). PHYA-specific signal
CC transducer in response to continuous FR lights (PubMed:15469493,
CC PubMed:16045472, PubMed:19482971, PubMed:11711433, PubMed:11726703,
CC PubMed:8364355). Contributes to inhibition of hypocotyl elongation in
CC continuous blue light (B) (PubMed:16045472).
CC {ECO:0000269|PubMed:11711433, ECO:0000269|PubMed:11726703,
CC ECO:0000269|PubMed:15469493, ECO:0000269|PubMed:16045472,
CC ECO:0000269|PubMed:17566111, ECO:0000269|PubMed:19482971,
CC ECO:0000269|PubMed:21969386, ECO:0000269|PubMed:22374392,
CC ECO:0000269|PubMed:22582101, ECO:0000269|PubMed:25071219,
CC ECO:0000269|PubMed:8364355}.
CC -!- SUBUNIT: Homodimer and heterodimer with FHL (PubMed:16045472).
CC Interacts with underphosphorylated PHYA, especially upon far-red (FR)
CC light illumination (PubMed:19208901, PubMed:18722184, PubMed:21884939,
CC PubMed:19482971). Binds to LAF1 and HFR1. Forms PHYA/FHY1/HFR1 complex
CC in darkness but dissociates from PHYA and HFR1 in response to
CC continuous FR light (FRc) (PubMed:19482971).
CC {ECO:0000269|PubMed:16045472, ECO:0000269|PubMed:18722184,
CC ECO:0000269|PubMed:19208901, ECO:0000269|PubMed:19482971,
CC ECO:0000269|PubMed:21884939}.
CC -!- INTERACTION:
CC Q8S4Q6; P14712: PHYA; NbExp=4; IntAct=EBI-1163379, EBI-624446;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11711433,
CC ECO:0000269|PubMed:11726703, ECO:0000269|PubMed:18670649,
CC ECO:0000269|PubMed:18980642, ECO:0000269|PubMed:21884939,
CC ECO:0000269|PubMed:22582101}. Cytoplasm {ECO:0000269|PubMed:11711433,
CC ECO:0000269|PubMed:11726703, ECO:0000269|PubMed:18980642,
CC ECO:0000269|PubMed:21884939, ECO:0000269|PubMed:22582101}. Note=In
CC hypocotyls, mostly present in nucleus of dark (cD) grown plants, but
CC also detected at low levels in cytoplasm of cD and continuous far red
CC (cFR) grown plants. Disappearance of the nuclear pool after exposition
CC of etiolated plants to the light is faster in red (R), blue (B) and
CC white light (WL) than in FR (PubMed:11711433). Shuttles reversibly from
CC cytoplasm to nuclear bodies when dephosphorylated in FR but stay in the
CC cytoplasm when phosphorylated by PHYA in other light conditions
CC (PubMed:18980642, PubMed:22582101, PubMed:21884939).
CC {ECO:0000269|PubMed:11711433, ECO:0000269|PubMed:18980642,
CC ECO:0000269|PubMed:21884939, ECO:0000269|PubMed:22582101}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=FHY1-3 {ECO:0000303|PubMed:21097709};
CC IsoId=Q8S4Q6-1; Sequence=Displayed;
CC Name=2; Synonyms=FHY1-1 {ECO:0000303|PubMed:21097709};
CC IsoId=Q8S4Q6-2; Sequence=VSP_058415;
CC Name=3; Synonyms=FHY1-2 {ECO:0000303|PubMed:21097709};
CC IsoId=Q8S4Q6-3; Sequence=VSP_058416, VSP_058417;
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyl cells of etiolated plants.
CC {ECO:0000269|PubMed:11711433, ECO:0000269|PubMed:11726703}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in young seedlings with a peak three
CC days after seed germination (PubMed:11726703). Mostly abundant in young
CC seedlings grown in darkness, but quickly down-regulated during further
CC seedling development and by light exposure (at protein level)
CC (PubMed:16244150). {ECO:0000269|PubMed:11726703,
CC ECO:0000269|PubMed:16244150}.
CC -!- INDUCTION: Activated by FHY3 and FAR1 under far-red light (FR); HY5
CC prevents this activation (PubMed:16045472, PubMed:21097709,
CC PubMed:18033885). Down-regulated by FR, red (R) and blue (B) lights
CC (PubMed:18033885, PubMed:16045472). Accumulates in dark (D)-grown but
CC not in R and FR-grown hypocotyl cells. Repressed in etiolated plants
CC transferred to FR conditions in a FHY3-dependent manner
CC (PubMed:15469493, PubMed:11711433). Inhibited by light
CC (PubMed:11726703). Repressed by PHYA-mediated phosphorylation in R
CC illumination; the phosphorylated form is a substrate for
CC ubiquitin/proteasome-mediated degradation (PubMed:22582101,
CC PubMed:19208901). PHYA-dependent down-regulation by light is largely at
CC post-transcriptional level, primarily mediated through the 26S
CC proteasome-dependent protein degradation (PubMed:16244150).
CC {ECO:0000269|PubMed:11711433, ECO:0000269|PubMed:11726703,
CC ECO:0000269|PubMed:15469493, ECO:0000269|PubMed:16045472,
CC ECO:0000269|PubMed:16244150, ECO:0000269|PubMed:18033885,
CC ECO:0000269|PubMed:19208901, ECO:0000269|PubMed:21097709,
CC ECO:0000269|PubMed:22582101}.
CC -!- PTM: Inactivated by rapid reversible PHYA-mediated phosphorylation at
CC Ser-39 and Thr-61 in red light (R), thus inhibiting PHYA signaling in a
CC negative feedback loop; this ensures the seedling deetiolation process
CC in response to a R-enriched light condition (PubMed:19208901,
CC PubMed:22582101). Subsequent exposure to far-red light (FR) after the R
CC conditions leads to dephosphorylation (PubMed:19208901). The
CC phosphorylated form is cytoplasmic only and unable to bind to chromatin
CC at direct target genes whereas the unphosphorylated form can shuttle
CC from cytoplasm to nucleus (PubMed:22582101).
CC {ECO:0000269|PubMed:19208901, ECO:0000269|PubMed:22582101}.
CC -!- DISRUPTION PHENOTYPE: Partially blind to far-red (FR) (PubMed:15469493,
CC PubMed:11711433, PubMed:11726703, PubMed:19482971, PubMed:16045472).
CC Impaired inhibition of hypocotyl elongation and cotyledons expansion
CC under continuous FR light conditions (PubMed:11711433, PubMed:11726703,
CC PubMed:8364355, PubMed:22582101, PubMed:19482971, PubMed:16045472).
CC Absence of FR-induced killing response (PubMed:11726703). Increased
CC seed germination rate in salt stress conditions (PubMed:25071219). In
CC plants lacking FHY1 and FHL, altered phototropism (e.g. phototropic
CC bending) associated with abnormal consitutive cytosolic localization of
CC PHYA (PubMed:22374392, PubMed:17566111). In the double mutant fhl fhy1
CC several PHYA-dependent phototropic responses are altered (e.g.
CC hypocotyl elongation and cotyledon opening under high-irradiance
CC conditions and seed germination under very-low-fluence conditions), but
CC not for some PHYA-dependent responses such as the abrogation of
CC negative gravitropism in blue light and red-enhanced phototropism
CC (PubMed:17566111). Hyposensitivity to blue light (B) (PubMed:16045472).
CC {ECO:0000269|PubMed:11711433, ECO:0000269|PubMed:11726703,
CC ECO:0000269|PubMed:15469493, ECO:0000269|PubMed:16045472,
CC ECO:0000269|PubMed:17566111, ECO:0000269|PubMed:19482971,
CC ECO:0000269|PubMed:22374392, ECO:0000269|PubMed:22582101,
CC ECO:0000269|PubMed:25071219, ECO:0000269|PubMed:8364355}.
CC -!- SIMILARITY: Belongs to the FHY1 protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23638.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAP40489.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF432142; AAL35819.1; -; Genomic_DNA.
DR EMBL; AF424739; AAL87850.1; -; mRNA.
DR EMBL; HM029240; ADE60260.1; -; mRNA.
DR EMBL; HM029241; ADE60261.1; -; mRNA.
DR EMBL; HM029242; ADE60262.1; -; mRNA.
DR EMBL; AC004684; AAC23638.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09433.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61436.1; -; Genomic_DNA.
DR EMBL; BT008682; AAP40489.1; ALT_INIT; mRNA.
DR EMBL; AK229717; BAF01555.1; -; mRNA.
DR PIR; T02534; T02534.
DR RefSeq; NP_001078018.1; NM_001084549.2. [Q8S4Q6-1]
DR RefSeq; NP_001323653.1; NM_001336669.1. [Q8S4Q6-3]
DR AlphaFoldDB; Q8S4Q6; -.
DR IntAct; Q8S4Q6; 2.
DR STRING; 3702.AT2G37678.1; -.
DR iPTMnet; Q8S4Q6; -.
DR PaxDb; Q8S4Q6; -.
DR PRIDE; Q8S4Q6; -.
DR ProteomicsDB; 230592; -. [Q8S4Q6-1]
DR EnsemblPlants; AT2G37678.1; AT2G37678.1; AT2G37678. [Q8S4Q6-1]
DR EnsemblPlants; AT2G37678.2; AT2G37678.2; AT2G37678. [Q8S4Q6-3]
DR GeneID; 5007942; -.
DR Gramene; AT2G37678.1; AT2G37678.1; AT2G37678. [Q8S4Q6-1]
DR Gramene; AT2G37678.2; AT2G37678.2; AT2G37678. [Q8S4Q6-3]
DR KEGG; ath:AT2G37678; -.
DR Araport; AT2G37678; -.
DR TAIR; locus:4010713689; AT2G37678.
DR eggNOG; KOG4635; Eukaryota.
DR HOGENOM; CLU_1565045_0_0_1; -.
DR InParanoid; Q8S4Q6; -.
DR OMA; LDFIYGS; -.
DR OrthoDB; 1204859at2759; -.
DR PhylomeDB; Q8S4Q6; -.
DR PRO; PR:Q8S4Q6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S4Q6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0010018; P:far-red light signaling pathway; IMP:TAIR.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IDA:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1901000; P:regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IMP:UniProtKB.
DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0010218; P:response to far red light; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0010114; P:response to red light; IMP:UniProtKB.
DR GO; GO:0009639; P:response to red or far red light; IMP:TAIR.
DR InterPro; IPR037766; FHY1.
DR PANTHER; PTHR37723; PTHR37723; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Developmental protein; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..202
FT /note="Protein FAR-RED ELONGATED HYPOCOTYL 1"
FT /id="PRO_0000436754"
FT MOTIF 40..43
FT /note="Nuclear localization sequence (NLS)"
FT /evidence="ECO:0000269|PubMed:15469493,
FT ECO:0000269|PubMed:18670649, ECO:0000303|PubMed:11711433"
FT MOTIF 54..57
FT /note="Nuclear export sequence (NES)"
FT /evidence="ECO:0000269|PubMed:15469493"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22582101"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22582101"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /id="VSP_058415"
FT VAR_SEQ 177..184
FT /note="DDSTLHET -> GKENRILV (in isoform 3)"
FT /id="VSP_058416"
FT VAR_SEQ 185..202
FT /note="Missing (in isoform 3)"
FT /id="VSP_058417"
FT MUTAGEN 14
FT /note="S->A: Normal red light induced phosphorylation."
FT /evidence="ECO:0000269|PubMed:22582101"
FT MUTAGEN 39
FT /note="S->A: Reduced red light (R) induced phosphorylation.
FT Abnormal persistent nuclear localization after R and far
FT red illumination; when associated with A-61."
FT /evidence="ECO:0000269|PubMed:22582101"
FT MUTAGEN 39
FT /note="S->D: Phosphorylation mimic mutant unable to respond
FT to far red light (FR) and to fulfill associated FR
FT responses thus leading to very long hypocotyl, altered
FT anthocyanin accumulation and closed cotyledons, abnormal
FT constitutive subcellular localization in cytoplasm and
FT impaired chromatin binding at direct target genes; when
FT associated with D-61."
FT /evidence="ECO:0000269|PubMed:22582101"
FT MUTAGEN 49
FT /note="S->A: Normal red light induced phosphorylation."
FT /evidence="ECO:0000269|PubMed:22582101"
FT MUTAGEN 61
FT /note="T->A: Impaired red light induced phosphorylation.
FT Abnormal persistent nuclear localization after R and far
FT red illumination; when associated with A-39."
FT /evidence="ECO:0000269|PubMed:22582101"
FT MUTAGEN 61
FT /note="T->D: Phosphorylation mimic mutant unable to respond
FT to far red light (FR) and to fulfill associated FR
FT responses thus leading to very long hypocotyl, altered
FT anthocyanin accumulation and closed cotyledons, abnormal
FT constitutive subcellular localization in cytoplasm and
FT impaired chromatin binding at direct target genes; when
FT associated with S-39."
FT /evidence="ECO:0000269|PubMed:22582101"
FT CONFLICT 38
FT /note="V -> M (in Ref. 1; AAL35819)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="A -> V (in Ref. 1; AAL35819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 23013 MW; F0E3056D4CFCE0E3 CRC64;
MPEVEVDNNN EKPSEINSFH HMIISSSKNV LKMEEVEVSK KRKFQTDQSD ELSLLPLSKH
TCFANVACSE NTNGNSEIDT EYSMSSYVNS TTSMECNNDI EMKEESSGSC GEDKMISFES
HLDYIYGTQN LEDFSEKVIE NILYLDEQEE EEEDAKGCSS NAAKFVLSSG RWTVNQDDST
LHETKKPTID QEFEQYFSTL ML
