FAR1_ARATH
ID FAR1_ARATH Reviewed; 827 AA.
AC Q9SWG3; O23363;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Protein FAR-RED IMPAIRED RESPONSE 1;
GN Name=FAR1; OrderedLocusNames=At4g15090; ORFNames=dl3590w, FCAALL.134;
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], SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. No-0;
RX PubMed=10444599; DOI=10.1101/gad.13.15.2017;
RA Hudson M., Ringli C., Boylan M.T., Quail P.H.;
RT "The FAR1 locus encodes a novel nuclear protein specific to phytochrome A
RT signaling.";
RL Genes Dev. 13:2017-2027(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH FHY3.
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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. Positive regulator of chlorophyll
CC biosynthesis via the activation of HEMB1 gene expression.
CC {ECO:0000269|PubMed:11889039, ECO:0000269|PubMed:12753585,
CC ECO:0000269|PubMed:18033885, ECO:0000269|PubMed:22634759}.
CC -!- SUBUNIT: Homodimer and heterodimer with FHY3.
CC -!- INTERACTION:
CC Q9SWG3; Q5UBY2: FRS1; NbExp=3; IntAct=EBI-625464, EBI-625440;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10444599,
CC ECO:0000269|PubMed:18033885}.
CC -!- INDUCTION: Down-regulated after exposure to far-red light. Subject to a
CC negative feedback regulation by PHYA signaling.
CC {ECO:0000269|PubMed:18033885}.
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: Elongated hypocotyls and reduced expansion of
CC cotyledons under continuous far-red light. Reduced protochlorophyllide
CC levels in darkness and less photobleaching in the light.
CC {ECO:0000269|PubMed:10444599, ECO:0000269|PubMed:22634759}.
CC -!- SIMILARITY: Belongs to the FHY3/FAR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10288.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g03900 has been split into 2 genes: At4g15090 and At4g15093.; Evidence={ECO:0000305};
CC Sequence=CAB78551.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g03900 has been split into 2 genes: At4g15090 and At4g15093.; Evidence={ECO:0000305};
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DR EMBL; AF159587; AAD51282.1; -; mRNA.
DR EMBL; Z97337; CAB10288.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78551.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83553.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67625.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67626.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67627.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67628.1; -; Genomic_DNA.
DR PIR; F71414; F71414.
DR PIR; T02124; T02124.
DR RefSeq; NP_001329443.1; NM_001340994.1.
DR RefSeq; NP_001329444.1; NM_001340995.1.
DR RefSeq; NP_001329445.1; NM_001340992.1.
DR RefSeq; NP_001329446.1; NM_001340993.1.
DR RefSeq; NP_567455.4; NM_117596.6.
DR AlphaFoldDB; Q9SWG3; -.
DR BioGRID; 12470; 14.
DR IntAct; Q9SWG3; 12.
DR STRING; 3702.AT4G15090.1; -.
DR PaxDb; Q9SWG3; -.
DR PRIDE; Q9SWG3; -.
DR ProteomicsDB; 222444; -.
DR EnsemblPlants; AT4G15090.1; AT4G15090.1; AT4G15090.
DR EnsemblPlants; AT4G15090.2; AT4G15090.2; AT4G15090.
DR EnsemblPlants; AT4G15090.3; AT4G15090.3; AT4G15090.
DR EnsemblPlants; AT4G15090.4; AT4G15090.4; AT4G15090.
DR EnsemblPlants; AT4G15090.5; AT4G15090.5; AT4G15090.
DR GeneID; 827173; -.
DR Gramene; AT4G15090.1; AT4G15090.1; AT4G15090.
DR Gramene; AT4G15090.2; AT4G15090.2; AT4G15090.
DR Gramene; AT4G15090.3; AT4G15090.3; AT4G15090.
DR Gramene; AT4G15090.4; AT4G15090.4; AT4G15090.
DR Gramene; AT4G15090.5; AT4G15090.5; AT4G15090.
DR KEGG; ath:AT4G15090; -.
DR Araport; AT4G15090; -.
DR TAIR; locus:2129665; AT4G15090.
DR eggNOG; ENOG502QS58; Eukaryota.
DR HOGENOM; CLU_008459_7_1_1; -.
DR InParanoid; Q9SWG3; -.
DR OMA; NTRHCFA; -.
DR OrthoDB; 197084at2759; -.
DR PhylomeDB; Q9SWG3; -.
DR PRO; PR:Q9SWG3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SWG3; baseline and differential.
DR Genevisible; Q9SWG3; AT.
DR GO; GO:0005634; C:nucleus; 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:0010018; P:far-red light signaling pathway; 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:0010218; P:response to far red light; IMP:TAIR.
DR GO; GO:0009639; P:response to red or far red light; IMP:TAIR.
DR InterPro; IPR004330; FAR1_DNA_bnd_dom.
DR InterPro; IPR031052; FHY3/FAR1.
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 Pfam; PF04434; SWIM; 1.
DR SMART; SM00575; ZnF_PMZ; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..827
FT /note="Protein FAR-RED IMPAIRED RESPONSE 1"
FT /id="PRO_0000363478"
FT DOMAIN 65..154
FT /note="FAR1"
FT DOMAIN 275..371
FT /note="MULE"
FT ZN_FING 555..591
FT /note="SWIM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT REGION 103..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 95449 MW; 34737270F5BB81CD CRC64;
MDLQENLVSD AGDDHMVDIV VEPHSNRDIG IVDEFNIGGD VGFSGDLDLE PRNGIDFDTH
EAAYIFYQEY AKSMGFTTSI KNSRRSKKTK DFIDAKFACS RYGVTPESES SGSSSRRSTV
KKTDCKASMH VKRRPDGKWI IHEFVKDHNH ELLPALAYHF RIQRNVKLAE KNNIDILHAV
SERTKKMYVE MSRQSGGYKN IGSLLQTDVS SQVDKGRYLA LEEGDSQVLL EYFKRIKKEN
PKFFYAIDLN EDQRLRNLFW ADAKSRDDYL SFNDVVSFDT TYVKFNDKLP LALFIGVNHH
SQPMLLGCAL VADESMETFV WLIKTWLRAM GGRAPKVILT DQDKFLMSAV SELLPNTRHC
FALWHVLEKI PEYFSHVMKR HENFLLKFNK CIFRSWTDDE FDMRWWKMVS QFGLENDEWL
LWLHEHRQKW VPTFMSDVFL AGMSTSQRSE SVNSFFDKYI HKKITLKEFL RQYGVILQNR
YEEESVADFD TCHKQPALKS PSPWEKQMAT TYTHTIFKKF QVEVLGVVAC HPRKEKEDEN
MATFRVQDCE KDDDFLVTWS KTKSELCCFC RMFEYKGFLC RHALMILQMC GFASIPPQYI
LKRWTKDAKS GVLAGEGADQ IQTRVQRYND LCSRATELSE EGCVSEENYN IALRTLVETL
KNCVDMNNAR NNITESNSQL NNGTHEEENQ VMAGVKATKK KTVYRKRKGQ QEASQMLESQ
QSLQPMETIS SEAMDMNGYY GPQQNVQGLL NLMEPPHEGY YVDQRTIQGL GQLNSIAPAQ
DSFFTNQQAM SGMVGQIDFR PPPNFTYTLQ EEHLSSAQLP GSSSRQL
