BRN1L_ARATH
ID BRN1L_ARATH Reviewed; 441 AA.
AC Q8LFS6; Q8VZ45; Q9ZNS7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=RNA-binding protein BRN1 {ECO:0000305};
DE AltName: Full=Protein BRUNO-LIKE 1 {ECO:0000303|PubMed:23437850};
DE Short=AtBRN1 {ECO:0000303|PubMed:23437850};
DE AltName: Full=Protein RNA-BINDING PROTEIN-DEFENSE RELATED 1 {ECO:0000303|PubMed:20636102};
DE Short=AtRBP-DR1 {ECO:0000303|PubMed:20636102};
GN Name=BRN1 {ECO:0000303|PubMed:23437850};
GN Synonyms=RBP-DR1 {ECO:0000303|PubMed:20636102};
GN OrderedLocusNames=At4g03110 {ECO:0000312|Araport:AT4G03110};
GN ORFNames=F4C21.3 {ECO:0000312|EMBL:AAD14439.1},
GN T4I9.1 {ECO:0000312|EMBL:AAC79095.1};
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 [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 [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY ABSCISIC ACID.
RX PubMed=12432076; DOI=10.1242/jcs.00175;
RA Hoth S., Morgante M., Sanchez J.-P., Hanafey M.K., Tingey S.V., Chua N.-H.;
RT "Genome-wide gene expression profiling in Arabidopsis thaliana reveals new
RT targets of abscisic acid and largely impaired gene regulation in the abi1-1
RT mutant.";
RL J. Cell Sci. 115:4891-4900(2002).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20636102; DOI=10.1094/mpmi-05-10-0106;
RA Qi Y., Tsuda K., Joe A., Sato M., Nguyen L.V., Glazebrook J., Alfano J.R.,
RA Cohen J.D., Katagiri F.;
RT "A putative RNA-binding protein positively regulates salicylic acid-
RT mediated immunity in Arabidopsis.";
RL Mol. Plant Microbe Interact. 23:1573-1583(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23437850; DOI=10.1111/nph.12181;
RA Kim H.S., Abbasi N., Choi S.B.;
RT "Bruno-like proteins modulate flowering time via 3' UTR-dependent decay of
RT SOC1 mRNA.";
RL New Phytol. 198:747-756(2013).
CC -!- FUNCTION: RNA-binding protein involved in the regulation of flowering
CC time. Acts as repressor of the activity of SOC1, a transcriptional
CC activator of flowering time. Binds to the 3'-UTR of SOC1 mRNA in the
CC cytoplasm and participates in SOC1 mRNA decay, mediated by the distal
CC region of the SOC1 3'-UTR (PubMed:23437850). Acts as positive regulator
CC of salicylic acid (SA)-mediated immunity. May act on SA signaling-
CC related genes at a post-transcriptional level (PubMed:20636102).
CC {ECO:0000269|PubMed:20636102, ECO:0000269|PubMed:23437850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20636102,
CC ECO:0000269|PubMed:23437850}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LFS6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LFS6-2; Sequence=VSP_057470;
CC -!- TISSUE SPECIFICITY: Highly expressed in stems and cauline leaves, and
CC at lower levels in siliques, flowers, roots and rosette leaves.
CC {ECO:0000269|PubMed:23437850}.
CC -!- INDUCTION: By abscisic acid (ABA). {ECO:0000269|PubMed:12432076}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show enhanced susceptibility to the
CC pathogen Pseudomonas syringae pv. tomato DC3000.
CC {ECO:0000269|PubMed:20636102}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79095.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD14439.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005275; AAD14439.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF069442; AAC79095.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161496; CAB77796.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82272.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82273.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67473.1; -; Genomic_DNA.
DR EMBL; AY065261; AAL38737.1; -; mRNA.
DR EMBL; AK316961; BAH19660.1; -; mRNA.
DR EMBL; AY084669; AAM61231.1; -; mRNA.
DR PIR; T01382; T01382.
DR RefSeq; NP_001329301.1; NM_001340422.1. [Q8LFS6-2]
DR RefSeq; NP_567249.1; NM_116545.4. [Q8LFS6-1]
DR RefSeq; NP_849294.1; NM_178963.3.
DR AlphaFoldDB; Q8LFS6; -.
DR STRING; 3702.AT4G03110.1; -.
DR PaxDb; Q8LFS6; -.
DR PRIDE; Q8LFS6; -.
DR ProteomicsDB; 222819; -. [Q8LFS6-1]
DR EnsemblPlants; AT4G03110.1; AT4G03110.1; AT4G03110. [Q8LFS6-1]
DR EnsemblPlants; AT4G03110.3; AT4G03110.3; AT4G03110. [Q8LFS6-2]
DR GeneID; 828090; -.
DR Gramene; AT4G03110.1; AT4G03110.1; AT4G03110. [Q8LFS6-1]
DR Gramene; AT4G03110.3; AT4G03110.3; AT4G03110. [Q8LFS6-2]
DR KEGG; ath:AT4G03110; -.
DR Araport; AT4G03110; -.
DR TAIR; locus:2139340; AT4G03110.
DR eggNOG; KOG0144; Eukaryota.
DR HOGENOM; CLU_015367_5_1_1; -.
DR InParanoid; Q8LFS6; -.
DR OMA; PMGNGMN; -.
DR OrthoDB; 1209165at2759; -.
DR PhylomeDB; Q8LFS6; -.
DR PRO; PR:Q8LFS6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LFS6; baseline and differential.
DR Genevisible; Q8LFS6; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0080151; P:positive regulation of salicylic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR002343; Hud_Sxl_RNA.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Flowering; Plant defense;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
FT CHAIN 1..441
FT /note="RNA-binding protein BRN1"
FT /id="PRO_0000431960"
FT DOMAIN 18..99
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 106..186
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 349..427
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 258..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 394..441
FT /note="FVSYDSQAAAQNAIDMMNGRHLGGKKLKVQLKRDSNNGQPSSNPSLIS ->
FT KLSFDLVFPLLKLVHCEGRKKAFFCCCCWLQVLLAMTHKPRRRTLLT (in isoform
FT 2)"
FT /id="VSP_057470"
FT CONFLICT 234
FT /note="Missing (in Ref. 3; AAL38737 and 2; AEE82273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 48199 MW; 66A028EE84D7E010 CRC64;
MAEAKEENRE KNEEEESVKL FVGQIPKHMS ESQLLTLFQE FAVVDEVNII KDKITRASRG
CCFLLCPSRE EADKLVNACH NKKTLPGANS LLQVKYADGE LERLEHKLFV GMLPKNVSEA
EVQSLFSKYG TIKDLQILRG AQQTSKGCAF LKYETKEQAV SAMESINGKH KMEGSTVPLV
VKWADTERER HTRRLQKAQS HIARLGNGDP TNPSLFGALP MGYVPPYNGY GYHQPPGTYG
YMLPPIQNQA AFSNMIAQPN QGNNNALQGT SPDSVPPRLA RRNFPMPPGN YMGSGYPAMR
GHPFPFAYPR GIVSPRPLSS SPGSISPGMS TPLGIGLSSV VQTEGPEGAN LFIYNIPREF
GDQELAAAFQ SFGIVLSAKV FVDKATGVSK CFGFVSYDSQ AAAQNAIDMM NGRHLGGKKL
KVQLKRDSNN GQPSSNPSLI S
