BTR1_ARATH
ID BTR1_ARATH Reviewed; 313 AA.
AC Q9LZ82; B9DH67; F4JW99;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Protein BTR1 {ECO:0000303|PubMed:18762309};
DE AltName: Full=Binding to ToMV RNA 1 {ECO:0000303|PubMed:18762309};
GN Name=BTR1 {ECO:0000303|PubMed:18762309};
GN OrderedLocusNames=At5g04430 {ECO:0000312|Araport:AT5G04430};
GN ORFNames=T32M21_30 {ECO:0000312|EMBL:CAB85549.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BTR1S).
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 BTR1S).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-313 (ISOFORM BTR1L).
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16807317; DOI=10.1093/nar/gkl429;
RA de la Fuente van Bentem S., Anrather D., Roitinger E., Djamei A.,
RA Hufnagl T., Barta A., Csaszar E., Dohnal I., Lecourieux D., Hirt H.;
RT "Phosphoproteomics reveals extensive in vivo phosphorylation of Arabidopsis
RT proteins involved in RNA metabolism.";
RL Nucleic Acids Res. 34:3267-3278(2006).
RN [7]
RP FUNCTION, ALTERNATIVE SPLICING, IDENTIFICATION BY MASS SPECTROMETRY
RP (ISOFORM BTR1S), SUBCELLULAR LOCATION, INDUCTION BY TOMV INFECTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18762309; DOI=10.1016/j.virol.2008.07.033;
RA Fujisaki K., Ishikawa M.;
RT "Identification of an Arabidopsis thaliana protein that binds to tomato
RT mosaic virus genomic RNA and inhibits its multiplication.";
RL Virology 380:402-411(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Negative regulator of tomato mosaic virus (ToMV)
CC multiplication, but has no effect on the multiplication of cucumber
CC mosaic virus (CMV). Limits the spreading of the virus
CC (PubMed:18762309). Isoform BTR1S: binds preferentially and directly to
CC the 5'terminal region of ToMV genomic RNA, and affects the efficiency
CC of translation rather than mRNA stability (PubMed:18762309).
CC {ECO:0000269|PubMed:18762309}.
CC -!- INTERACTION:
CC Q9LZ82; Q9ASW4: At3g21215; NbExp=4; IntAct=EBI-4449845, EBI-4435127;
CC Q9LZ82; A0A1P8BC43: MCL19.25; NbExp=3; IntAct=EBI-4449845, EBI-25519435;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18762309}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=BTR1S {ECO:0000303|PubMed:18762309};
CC IsoId=Q9LZ82-1; Sequence=Displayed;
CC Name=BTR1L {ECO:0000303|PubMed:18762309};
CC IsoId=Q9LZ82-2; Sequence=VSP_057661;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and siliques.
CC {ECO:0000305|PubMed:18762309}.
CC -!- INDUCTION: Not induced by ToMV infection.
CC {ECO:0000269|PubMed:18762309}.
CC -!- DISRUPTION PHENOTYPE: Higher accumulation of ToMV in infected leaves.
CC {ECO:0000269|PubMed:18762309}.
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DR EMBL; AL162875; CAB85549.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90743.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90744.1; -; Genomic_DNA.
DR EMBL; AF375411; AAK52995.1; -; mRNA.
DR EMBL; AY086553; AAM63617.1; -; mRNA.
DR EMBL; BT000854; AAN38691.1; -; mRNA.
DR EMBL; AK317416; BAH20084.1; -; mRNA.
DR PIR; T48439; T48439.
DR RefSeq; NP_196063.1; NM_120525.4. [Q9LZ82-1]
DR RefSeq; NP_850764.1; NM_180433.3. [Q9LZ82-2]
DR AlphaFoldDB; Q9LZ82; -.
DR SMR; Q9LZ82; -.
DR IntAct; Q9LZ82; 3.
DR STRING; 3702.AT5G04430.2; -.
DR iPTMnet; Q9LZ82; -.
DR MetOSite; Q9LZ82; -.
DR PRIDE; Q9LZ82; -.
DR ProteomicsDB; 240368; -. [Q9LZ82-1]
DR EnsemblPlants; AT5G04430.1; AT5G04430.1; AT5G04430. [Q9LZ82-1]
DR EnsemblPlants; AT5G04430.2; AT5G04430.2; AT5G04430. [Q9LZ82-2]
DR GeneID; 830322; -.
DR Gramene; AT5G04430.1; AT5G04430.1; AT5G04430. [Q9LZ82-1]
DR Gramene; AT5G04430.2; AT5G04430.2; AT5G04430. [Q9LZ82-2]
DR KEGG; ath:AT5G04430; -.
DR Araport; AT5G04430; -.
DR TAIR; locus:2184362; AT5G04430.
DR eggNOG; KOG2191; Eukaryota.
DR HOGENOM; CLU_022670_1_0_1; -.
DR OMA; SIAKEPH; -.
DR OrthoDB; 1167935at2759; -.
DR PhylomeDB; Q9LZ82; -.
DR PRO; PR:Q9LZ82; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZ82; baseline and differential.
DR Genevisible; Q9LZ82; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:TAIR.
DR GO; GO:0046719; P:regulation by virus of viral protein levels in host cell; IMP:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; NAS:TAIR.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..313
FT /note="Protein BTR1"
FT /id="PRO_0000433025"
FT DOMAIN 34..102
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 120..188
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 233..300
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 208
FT /note="A -> AGLFYSGFHGPPYAYALPSVAT (in isoform BTR1L)"
FT /id="VSP_057661"
SQ SEQUENCE 313 AA; 33821 MW; 407A9FD44A52408F CRC64;
MESTESYAAG SPEELAKRSP EPHDSSEADS AEKPTHIRFL VSNAAAGSVI GKGGSTITEF
QAKSGARIQL SRNQEFFPGT TDRIIMISGS IKEVVNGLEL ILDKLHSELH AEDGNEVEPR
RRIRLVVPNS SCGGIIGKGG ATIKSFIEES KAGIKISPLD NTFYGLSDRL VTLSGTFEEQ
MRAIDLILAK LTEDDHYSQN VHSPYSYAAG YNSVNYAPNG SGGKYQNHKE EASTTVTIGV
ADEHIGLVLG RGGRNIMEIT QMTGARIKIS DRGDFMSGTT DRKVSITGPQ RAIQQAETMI
KQKVDSATER TTD
