FHL_ARATH
ID FHL_ARATH Reviewed; 201 AA.
AC A8MR65; D5MAD5; Q9LZL2;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein FAR-RED-ELONGATED HYPOCOTYL 1-LIKE {ECO:0000303|PubMed:21097709};
GN Name=FHL {ECO:0000303|PubMed:21097709};
GN OrderedLocusNames=At5g02200 {ECO:0000312|Araport:AT5G02200};
GN ORFNames=T7H20.250 {ECO:0000312|EMBL:CAB82993.1};
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] (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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, MUTAGENESIS OF 32-LYS--LYS-35 AND 43-LEU--LEU-46, DISRUPTION
RP PHENOTYPE, NUCLEAR LOCALIZATION AND NUCLEAR EXPORT MOTIFS, REPRESSION BY
RP LIGHT, INTERACTION WITH FHY1, 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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION BY PHYA, AND INTERACTION WITH PHYA.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP 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 [9]
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 [10]
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 [11]
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 [12]
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).
CC -!- FUNCTION: Can activate transcription (By similarity). Essential for
CC light-regulated PHYA nuclear accumulation and subsequent PHYA
CC phototropic signaling processes (PubMed:21969386, PubMed:22374392,
CC PubMed:17566111). PHYA-specific signal transducer in response to
CC continuous FR lights. Mediates the association of PHYA with HFR1 and
CC LAF1 in the nucleus in response to FR conditions (PubMed:19482971,
CC PubMed:16045472). Contributes to inhibition of hypocotyl elongation in
CC continuous blue light (B) (PubMed:16045472).
CC {ECO:0000250|UniProtKB:Q8S4Q6, ECO:0000269|PubMed:16045472,
CC ECO:0000269|PubMed:17566111, ECO:0000269|PubMed:19482971,
CC ECO:0000269|PubMed:21969386, ECO:0000269|PubMed:22374392}.
CC -!- SUBUNIT: Homodimer and heterodimer with FHY1 (PubMed:16045472).
CC Interacts with PHYA, especially upon far-red (FR) light illumination
CC (PubMed:21969386, PubMed:21884939, PubMed:19482971, PubMed:19208901).
CC Binds to LAF1 and HFR1 (PubMed:19482971). {ECO:0000269|PubMed:16045472,
CC ECO:0000269|PubMed:19208901, ECO:0000269|PubMed:19482971,
CC ECO:0000269|PubMed:21884939, ECO:0000269|PubMed:21969386}.
CC -!- INTERACTION:
CC A8MR65; P14712: PHYA; NbExp=3; IntAct=EBI-1163353, EBI-624446;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21884939}. Cytoplasm
CC {ECO:0000269|PubMed:21884939}. Note=Shuttles from cytoplasm to nuclear
CC bodies in FR but stay in the cytoplasm in other light conditions.
CC {ECO:0000269|PubMed:21884939}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=FHL-3 {ECO:0000303|PubMed:21097709};
CC IsoId=A8MR65-1; Sequence=Displayed;
CC Name=2; Synonyms=FHL-1 {ECO:0000303|PubMed:21097709};
CC IsoId=A8MR65-2; Sequence=VSP_058418;
CC Name=3; Synonyms=FHL-2 {ECO:0000303|PubMed:21097709};
CC IsoId=A8MR65-3; Sequence=VSP_058419, VSP_058420;
CC -!- INDUCTION: Activated by FHY3/FAR1 under far-red light (FR); HY5
CC prevents this activation (PubMed:21097709, PubMed:18033885,
CC PubMed:16045472). Down-regulated by FR, red (R) and blue (B) lights
CC (PubMed:18033885, PubMed:16045472). {ECO:0000269|PubMed:16045472,
CC ECO:0000269|PubMed:18033885, ECO:0000269|PubMed:21097709}.
CC -!- PTM: Inactivated by rapid reversible PHYA-mediated phosphorylation.
CC {ECO:0000305|PubMed:19208901}.
CC -!- DISRUPTION PHENOTYPE: Partially blind to far-red (FR). Impaired
CC inhibition of hypocotyl elongation and cotyledons expansion under
CC continuous FR light conditions (PubMed:19482971, PubMed:16045472). 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:16045472, ECO:0000269|PubMed:17566111,
CC ECO:0000269|PubMed:19482971, ECO:0000269|PubMed:22374392}.
CC -!- SIMILARITY: Belongs to the FHY1 protein family. {ECO:0000305}.
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DR EMBL; HM029243; ADE60263.1; -; mRNA.
DR EMBL; HM029244; ADE60264.1; -; mRNA.
DR EMBL; HM029245; ADE60265.1; -; mRNA.
DR EMBL; AL162508; CAB82993.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90443.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90444.1; -; Genomic_DNA.
DR PIR; T48241; T48241.
DR RefSeq; NP_001078521.1; NM_001085052.2. [A8MR65-1]
DR RefSeq; NP_195840.1; NM_120298.3. [A8MR65-2]
DR AlphaFoldDB; A8MR65; -.
DR IntAct; A8MR65; 2.
DR STRING; 3702.AT5G02200.2; -.
DR iPTMnet; A8MR65; -.
DR PaxDb; A8MR65; -.
DR PRIDE; A8MR65; -.
DR DNASU; 830832; -.
DR EnsemblPlants; AT5G02200.1; AT5G02200.1; AT5G02200. [A8MR65-2]
DR EnsemblPlants; AT5G02200.2; AT5G02200.2; AT5G02200. [A8MR65-1]
DR GeneID; 830832; -.
DR Gramene; AT5G02200.1; AT5G02200.1; AT5G02200. [A8MR65-2]
DR Gramene; AT5G02200.2; AT5G02200.2; AT5G02200. [A8MR65-1]
DR KEGG; ath:AT5G02200; -.
DR Araport; AT5G02200; -.
DR TAIR; locus:2185188; AT5G02200.
DR eggNOG; ENOG502S4AF; Eukaryota.
DR InParanoid; A8MR65; -.
DR OMA; DMELFCP; -.
DR OrthoDB; 1204859at2759; -.
DR PhylomeDB; A8MR65; -.
DR PRO; PR:A8MR65; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; A8MR65; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; ISS:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0009637; P:response to blue light; IMP:TAIR.
DR GO; GO:0010218; P:response to far red light; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR InterPro; IPR037766; FHY1.
DR PANTHER; PTHR37723; PTHR37723; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..201
FT /note="Protein FAR-RED-ELONGATED HYPOCOTYL 1-LIKE"
FT /id="PRO_0000436755"
FT MOTIF 32..35
FT /note="Nuclear localization sequence (NLS)"
FT /evidence="ECO:0000269|PubMed:16045472"
FT MOTIF 43..46
FT /note="Nuclear export sequence (NES)"
FT /evidence="ECO:0000269|PubMed:16045472"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /id="VSP_058418"
FT VAR_SEQ 178..180
FT /note="DSK -> GNQ (in isoform 3)"
FT /id="VSP_058419"
FT VAR_SEQ 181..201
FT /note="Missing (in isoform 3)"
FT /id="VSP_058420"
FT MUTAGEN 32..35
FT /note="KKRK->AAAA: Impaired nuclear import."
FT /evidence="ECO:0000269|PubMed:16045472"
FT MUTAGEN 43..46
FT /note="LLPL->AAAA: Impaired nuclear export."
FT /evidence="ECO:0000269|PubMed:16045472"
SQ SEQUENCE 201 AA; 22376 MW; 842F8A47AD141007 CRC64;
MDDADKSCSP SLDHSDINDP MIVAVESLDT SKKRKLHAEE SDLLPLPKHF CSEHQASLVN
SSCPSSVIDY AECSYAMENT KTSDEASSSA SFTGPSLYMF KDSIYSTGSS SSGYAATSSI
EQCFSKVDHK TQEDTQDFTH MEFIYHDSEF AVEDLQEVLN PVESYILSSA RWSVSNQDSK
EATTKPTIDQ EFEQYFSTLM M
