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Protein BTR1 (Binding to ToMV RNA 1)

 BTR1_ARATH              Reviewed;         313 AA.
Q9LZ82; B9DH67; F4JW99;
27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 125.
RecName: Full=Protein BTR1 {ECO:0000303|PubMed:18762309};
AltName: Full=Binding to ToMV RNA 1 {ECO:0000303|PubMed:18762309};
Name=BTR1 {ECO:0000303|PubMed:18762309};
OrderedLocusNames=At5g04430 {ECO:0000312|Araport:AT5G04430};
ORFNames=T32M21_30 {ECO:0000312|EMBL:CAB85549.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BTR1S).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BTR1S).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-313 (ISOFORM BTR1L).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16807317; DOI=10.1093/nar/gkl429;
de la Fuente van Bentem S., Anrather D., Roitinger E., Djamei A.,
Hufnagl T., Barta A., Csaszar E., Dohnal I., Lecourieux D., Hirt H.;
"Phosphoproteomics reveals extensive in vivo phosphorylation of
Arabidopsis proteins involved in RNA metabolism.";
Nucleic Acids Res. 34:3267-3278(2006).
[7]
FUNCTION, ALTERNATIVE SPLICING, IDENTIFICATION BY MASS SPECTROMETRY
(ISOFORM BTR1S), SUBCELLULAR LOCATION, INDUCTION BY TOMV INFECTION,
AND DISRUPTION PHENOTYPE.
PubMed=18762309; DOI=10.1016/j.virol.2008.07.033;
Fujisaki K., Ishikawa M.;
"Identification of an Arabidopsis thaliana protein that binds to
tomato mosaic virus genomic RNA and inhibits its multiplication.";
Virology 380:402-411(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Negative regulator of tomato mosaic virus (ToMV)
multiplication, but has no effect on the multiplication of
cucumber mosaic virus (CMV). Limits the spreading of the virus
(PubMed:18762309). Isoform BTR1S: binds preferentially and
directly to the 5'terminal region of ToMV genomic RNA, and affects
the efficiency of translation rather than mRNA stability
(PubMed:18762309). {ECO:0000269|PubMed:18762309}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18762309}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=BTR1S {ECO:0000303|PubMed:18762309};
IsoId=Q9LZ82-1; Sequence=Displayed;
Name=BTR1L {ECO:0000303|PubMed:18762309};
IsoId=Q9LZ82-2; Sequence=VSP_057661;
-!- TISSUE SPECIFICITY: Expressed in leaves, stems and siliques.
{ECO:0000305|PubMed:18762309}.
-!- INDUCTION: Not induced by ToMV infection.
{ECO:0000269|PubMed:18762309}.
-!- DISRUPTION PHENOTYPE: Higher accumulation of ToMV in infected
leaves. {ECO:0000269|PubMed:18762309}.
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EMBL; AL162875; CAB85549.1; -; Genomic_DNA.
EMBL; CP002688; AED90743.1; -; Genomic_DNA.
EMBL; CP002688; AED90744.1; -; Genomic_DNA.
EMBL; AF375411; AAK52995.1; -; mRNA.
EMBL; AY086553; AAM63617.1; -; mRNA.
EMBL; BT000854; AAN38691.1; -; mRNA.
EMBL; AK317416; BAH20084.1; -; mRNA.
PIR; T48439; T48439.
RefSeq; NP_196063.1; NM_120525.4. [Q9LZ82-1]
RefSeq; NP_850764.1; NM_180433.3. [Q9LZ82-2]
UniGene; At.4918; -.
ProteinModelPortal; Q9LZ82; -.
SMR; Q9LZ82; -.
IntAct; Q9LZ82; 2.
iPTMnet; Q9LZ82; -.
PRIDE; Q9LZ82; -.
EnsemblPlants; AT5G04430.1; AT5G04430.1; AT5G04430. [Q9LZ82-1]
EnsemblPlants; AT5G04430.2; AT5G04430.2; AT5G04430. [Q9LZ82-2]
GeneID; 830322; -.
Gramene; AT5G04430.1; AT5G04430.1; AT5G04430. [Q9LZ82-1]
Gramene; AT5G04430.2; AT5G04430.2; AT5G04430. [Q9LZ82-2]
KEGG; ath:AT5G04430; -.
Araport; AT5G04430; -.
TAIR; locus:2184362; AT5G04430.
eggNOG; KOG2191; Eukaryota.
eggNOG; ENOG410XRZD; LUCA.
HOGENOM; HOG000264316; -.
InParanoid; F4JW99; -.
KO; K14944; -.
OMA; MVASKDM; -.
OrthoDB; EOG09360G25; -.
PhylomeDB; Q9LZ82; -.
Reactome; R-ATH-72163; mRNA Splicing - Major Pathway.
PRO; PR:Q9LZ82; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9LZ82; baseline and differential.
Genevisible; Q9LZ82; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003729; F:mRNA binding; IDA:TAIR.
GO; GO:0046719; P:regulation by virus of viral protein levels in host cell; IMP:TAIR.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0008380; P:RNA splicing; NAS:TAIR.
Gene3D; 3.30.1370.10; -; 3.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
Pfam; PF00013; KH_1; 3.
SMART; SM00322; KH; 3.
SUPFAM; SSF54791; SSF54791; 3.
PROSITE; PS50084; KH_TYPE_1; 3.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Phosphoprotein; Reference proteome; Repeat; RNA-binding.
CHAIN 1 313 Protein BTR1.
/FTId=PRO_0000433025.
DOMAIN 34 102 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 120 188 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 233 300 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:16807317,
ECO:0000244|PubMed:19376835}.
VAR_SEQ 208 208 A -> AGLFYSGFHGPPYAYALPSVAT (in isoform
BTR1L).
/FTId=VSP_057661.
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


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