LAF1_ARATH
ID LAF1_ARATH Reviewed; 283 AA.
AC Q9M0K4; Q9SUI1; Q9ZTF0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Transcription factor LAF1 {ECO:0000303|PubMed:11581165};
DE AltName: Full=Myb-related protein 18 {ECO:0000303|PubMed:9839469};
DE Short=AtMYB18 {ECO:0000303|PubMed:9839469};
DE AltName: Full=Protein LONG AFTER FAR-RED LIGHT 1 {ECO:0000303|PubMed:11581165};
GN Name=LAF1 {ECO:0000303|PubMed:11581165};
GN Synonyms=MYB18 {ECO:0000303|PubMed:9839469};
GN OrderedLocusNames=At4g25560 {ECO:0000312|Araport:AT4G25560};
GN ORFNames=M7J2.70 {ECO:0000312|EMBL:CAA18170.1};
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF LYS-258.
RX PubMed=11581165; DOI=10.1101/gad.915001;
RA Ballesteros M.L., Bolle C., Lois L.M., Moore J.M., Vielle-Calzada J.-P.,
RA Grossniklaus U., Chua N.-H.;
RT "LAF1, a MYB transcription activator for phytochrome A signaling.";
RL Genes Dev. 15:2613-2625(2001).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=15208423; DOI=10.1104/pp.104.042176;
RA Gong W., Shen Y.-P., Ma L.-G., Pan Y., Du Y.-L., Wang D.-H., Yang J.-Y.,
RA Hu L.-D., Liu X.-F., Dong C.-X., Ma L., Chen Y.-H., Yang X.-Y., Gao Y.,
RA Zhu D., Tan X., Mu J.-Y., Zhang D.-B., Liu Y.-L., Dinesh-Kumar S.P., Li Y.,
RA Wang X.-P., Gu H.-Y., Qu L.-J., Bai S.-N., Lu Y.-T., Li J.-Y., Zhao J.-D.,
RA Zuo J., Huang H., Deng X.-W., Zhu Y.-X.;
RT "Genome-wide ORFeome cloning and analysis of Arabidopsis transcription
RT factor genes.";
RL Plant Physiol. 135:773-782(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-283, INDUCTION, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=9839469; DOI=10.1046/j.1365-313x.1998.00278.x;
RA Kranz H.D., Denekamp M., Greco R., Jin H.-L., Leyva A., Meissner R.C.,
RA Petroni K., Urzainqui A., Bevan M., Martin C., Smeekens S., Tonelli C.,
RA Paz-Ares J., Weisshaar B.;
RT "Towards functional characterisation of the members of the R2R3-MYB gene
RT family from Arabidopsis thaliana.";
RL Plant J. 16:263-276(1998).
RN [6]
RP UBIQUITINATION BY COP1.
RX PubMed=12827204; DOI=10.1038/nature01696;
RA Seo H.S., Yang J.-Y., Ishikawa M., Bolle C., Ballesteros M.L., Chua N.-H.;
RT "LAF1 ubiquitination by COP1 controls photomorphogenesis and is stimulated
RT by SPA1.";
RL Nature 423:995-999(2003).
RN [7]
RP GENE FAMILY.
RX PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
RA Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y., Wang X.,
RA Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W., Chen Z., Gu H.,
RA Qu L.-J.;
RT "The MYB transcription factor superfamily of Arabidopsis: expression
RT analysis and phylogenetic comparison with the rice MYB family.";
RL Plant Mol. Biol. 60:107-124(2006).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP FHY1 AND FHL.
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).
CC -!- FUNCTION: Transcription factor that promotes photomorphogenesis in the
CC light by participating in the transmission of phytochrome A (phyA)
CC signals to downstream responses (PubMed:11581165, PubMed:19482971).
CC Probably acts by activating expression of light-induced genes. In
CC darkness, its degradation prevents the activation of light-induced
CC genes (PubMed:11581165). {ECO:0000269|PubMed:11581165,
CC ECO:0000269|PubMed:19482971}.
CC -!- SUBUNIT: Binds to FHY1 and FHL (PubMed:19482971). Interacts with COP1.
CC {ECO:0000269|PubMed:19482971}.
CC -!- INTERACTION:
CC Q9M0K4; P43254: COP1; NbExp=3; IntAct=EBI-1543309, EBI-301649;
CC Q9M0K4; Q9FE22: HFR1; NbExp=6; IntAct=EBI-1543309, EBI-626001;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000255|PROSITE-
CC ProRule:PRU00625, ECO:0000269|PubMed:11581165,
CC ECO:0000269|PubMed:19482971}.
CC -!- TISSUE SPECIFICITY: Expressed at very low level. Expressed in cauline
CC leaves. {ECO:0000269|PubMed:11581165}.
CC -!- INDUCTION: By hormones or elicitors treatment. By exposure to abiotic
CC stress. {ECO:0000269|PubMed:9839469}.
CC -!- PTM: Ubiquitinated by COP1. Ubiquitination takes place in darkness and
CC leads to its subsequent degradation, thereby preventing to activate
CC photomorphogenesis signals. Ubiquitination is stimulated by SPA1.
CC {ECO:0000269|PubMed:12827204}.
CC -!- DISRUPTION PHENOTYPE: Partially blind to far-red (FR). Impaired
CC inhibition of hypocotyl elongation and cotyledons expansion under
CC continuous FR light conditions. {ECO:0000269|PubMed:19482971}.
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DR EMBL; AL022197; CAA18170.1; -; Genomic_DNA.
DR EMBL; AL161563; CAB81366.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85077.1; -; Genomic_DNA.
DR EMBL; AY519609; AAS10079.1; -; mRNA.
DR EMBL; AF062867; AAC83589.1; -; mRNA.
DR PIR; D85295; D85295.
DR PIR; T05791; T05791.
DR PIR; T51639; T51639.
DR RefSeq; NP_194286.1; NM_118688.3.
DR AlphaFoldDB; Q9M0K4; -.
DR SMR; Q9M0K4; -.
DR BioGRID; 13948; 11.
DR IntAct; Q9M0K4; 2.
DR STRING; 3702.AT4G25560.1; -.
DR PaxDb; Q9M0K4; -.
DR PRIDE; Q9M0K4; -.
DR EnsemblPlants; AT4G25560.1; AT4G25560.1; AT4G25560.
DR GeneID; 828661; -.
DR Gramene; AT4G25560.1; AT4G25560.1; AT4G25560.
DR KEGG; ath:AT4G25560; -.
DR Araport; AT4G25560; -.
DR TAIR; locus:2131844; AT4G25560.
DR eggNOG; KOG0048; Eukaryota.
DR HOGENOM; CLU_028567_6_5_1; -.
DR InParanoid; Q9M0K4; -.
DR OMA; TEMMINN; -.
DR OrthoDB; 1499244at2759; -.
DR PhylomeDB; Q9M0K4; -.
DR PRO; PR:Q9M0K4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0K4; baseline and differential.
DR Genevisible; Q9M0K4; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0010018; P:far-red light signaling pathway; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0009639; P:response to red or far red light; IMP:TAIR.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Phytochrome signaling pathway;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..283
FT /note="Transcription factor LAF1"
FT /id="PRO_0000197074"
FT DOMAIN 7..59
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 60..114
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 35..59
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 87..110
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT MUTAGEN 258
FT /note="K->R: Abolishes the speckles localization in the
FT nucleus possibly due to the absence of sumoylation at this
FT residue."
FT /evidence="ECO:0000269|PubMed:11581165"
FT CONFLICT 82
FT /note="S -> P (in Ref. 5; AAC83589)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="K -> E (in Ref. 5; AAC83589)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="F -> L (in Ref. 5; AAC83589)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="S -> P (in Ref. 5; AAC83589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 32433 MW; A04054C846CF2411 CRC64;
MAKTKYGERH RKGLWSPEED EKLRSFILSY GHSCWTTVPI KAGLQRNGKS CRLRWINYLR
PGLKRDMISA EEEETILTFH SSLGNKWSQI AKFLPGRTDN EIKNYWHSHL KKKWLKSQSL
QDAKSISPPS SSSSSLVACG KRNPETLISN HVFSFQRLLE NKSSSPSQES NGNNSHQCSS
APEIPRLFFS EWLSSSYPHT DYSSEFTDSK HSQAPNVEET LSAYEEMGDV DQFHYNEMMI
NNSNWTLNDI VFGSKCKKQE HHIYREASDC NSSAEFFSPS TTT
