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Double-stranded RNA-binding protein 1 (Protein HYPONASTIC LEAVES 1) (dsRNA-binding protein 1) (AtDRB1)

 DRB1_ARATH              Reviewed;         419 AA.
O04492; C0Z3F9;
08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
30-AUG-2017, entry version 127.
RecName: Full=Double-stranded RNA-binding protein 1;
AltName: Full=Protein HYPONASTIC LEAVES 1;
AltName: Full=dsRNA-binding protein 1;
Short=AtDRB1;
Name=DRB1; Synonyms=HYL1; OrderedLocusNames=At1g09700;
ORFNames=F21M12.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. No-0;
PubMed=11148283; DOI=10.1105/tpc.12.12.2351;
Lu C., Fedoroff N.;
"A mutation in the Arabidopsis HYL1 gene encoding a dsRNA binding
protein affects responses to abscisic acid, auxin, and cytokinin.";
Plant Cell 12:2351-2366(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14972688; DOI=10.1016/j.cub.2004.01.035;
Vazquez F., Gasciolli V., Crete P., Vaucheret H.;
"The nuclear dsRNA binding protein HYL1 is required for microRNA
accumulation and plant development, but not posttranscriptional
transgene silencing.";
Curr. Biol. 14:346-351(2004).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14722360; DOI=10.1073/pnas.0307969100;
Han M.H., Goud S., Song L., Fedoroff N.;
"The Arabidopsis double-stranded RNA-binding protein HYL1 plays a role
in microRNA-mediated gene regulation.";
Proc. Natl. Acad. Sci. U.S.A. 101:1093-1098(2004).
[8]
FUNCTION, SUBUNIT, AND INTERACTION WITH DCL1; DRB2; DRB4 AND DRB5.
PubMed=15821876; DOI=10.1007/s11103-004-6853-5;
Hiraguri A., Itoh R., Kondo N., Nomura Y., Aizawa D., Murai Y.,
Koiwa H., Seki M., Shinozaki K., Fukuhara T.;
"Specific interactions between Dicer-like proteins and HYL1/DRB-family
dsRNA-binding proteins in Arabidopsis thaliana.";
Plant Mol. Biol. 57:173-188(2005).
[9]
FUNCTION, INTERACTION WITH SE, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=16889646; DOI=10.1111/j.1365-313X.2006.02835.x;
Yang L., Liu Z., Lu F., Dong A., Huang H.;
"SERRATE is a novel nuclear regulator in primary microRNA processing
in Arabidopsis.";
Plant J. 47:841-850(2006).
[10]
FUNCTION, AND INTERACTION WITH DCL1.
PubMed=16428603; DOI=10.1261/rna.2146906;
Kurihara Y., Takashi Y., Watanabe Y.;
"The interaction between DCL1 and HYL1 is important for efficient and
precise processing of pri-miRNA in plant microRNA biogenesis.";
RNA 12:206-212(2006).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN DSRNA-BINDING.
PubMed=17337628; DOI=10.1105/tpc.106.048637;
Wu F., Yu L., Cao W., Mao Y., Liu Z., He Y.;
"The N-terminal double-stranded RNA binding domains of Arabidopsis
HYPONASTIC LEAVES1 are sufficient for pre-microRNA processing.";
Plant Cell 19:914-925(2007).
[12]
SUBCELLULAR LOCATION.
PubMed=17442570; DOI=10.1016/j.cub.2007.04.005;
Fang Y., Spector D.L.;
"Identification of nuclear dicing bodies containing proteins for
microRNA biogenesis in living Arabidopsis plants.";
Curr. Biol. 17:818-823(2007).
[13]
FUNCTION.
PubMed=18632569; DOI=10.1073/pnas.0803356105;
Dong Z., Han M.-H., Fedoroff N.;
"The RNA-binding proteins HYL1 and SE promote accurate in vitro
processing of pri-miRNA by DCL1.";
Proc. Natl. Acad. Sci. U.S.A. 105:9970-9975(2008).
[14]
FUNCTION.
PubMed=19304749; DOI=10.1093/nar/gkp189;
Szarzynska B., Sobkowiak L., Pant B.D., Balazadeh S., Scheible W.R.,
Mueller-Roeber B., Jarmolowski A., Szweykowska-Kulinska Z.;
"Gene structures and processing of Arabidopsis thaliana HYL1-dependent
pri-miRNAs.";
Nucleic Acids Res. 37:3083-3093(2009).
[15]
FUNCTION.
PubMed=19861421; DOI=10.1261/rna.1646909;
Eamens A.L., Smith N.A., Curtin S.J., Wang M.B., Waterhouse P.M.;
"The Arabidopsis thaliana double-stranded RNA binding protein DRB1
directs guide strand selection from microRNA duplexes.";
RNA 15:2219-2235(2009).
[16]
INTERACTION WITH RCF3; RS40 AND RS41, AND SUBCELLULAR LOCATION.
PubMed=26227967; DOI=10.1093/nar/gkv751;
Chen T., Cui P., Xiong L.;
"The RNA-binding protein HOS5 and serine/arginine-rich proteins RS40
and RS41 participate in miRNA biogenesis in Arabidopsis.";
Nucleic Acids Res. 43:8283-8298(2015).
[17]
STRUCTURE BY NMR OF 1-170, FUNCTION, AND DOMAIN DSRNA-BINDING.
PubMed=20735118; DOI=10.1021/bi100672x;
Rasia R.M., Mateos J., Bologna N.G., Burdisso P., Imbert L.,
Palatnik J.F., Boisbouvier J.;
"Structure and RNA interactions of the plant MicroRNA processing-
associated protein HYL1.";
Biochemistry 49:8237-8239(2010).
[18]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 15-172 IN COMPLEX WITH
DSRNA, FUNCTION, SUBUNIT, AND DOMAIN DSRNA-BINDING.
PubMed=20462493; DOI=10.1016/j.str.2010.02.006;
Yang S.W., Chen H.Y., Yang J., Machida S., Chua N.H., Yuan Y.A.;
"Structure of Arabidopsis HYPONASTIC LEAVES1 and its molecular
implications for miRNA processing.";
Structure 18:594-605(2010).
-!- FUNCTION: Double-stranded RNA-binding protein involved in RNA-
mediated post-transcriptional gene silencing (PTGS). Functions in
the microRNAs (miRNAs) biogenesis by assisting DICER-LIKE 1 (DCL1)
in the accurate processing from primary miRNAs (pri-miRNAs) to
miRNAs in the nucleus. Forms a complex with SERRATE (SE) and DCL1
to promote accurate processing of pri-miRNAs by DCL1. Binds and
assist DCL1 for accurate processing of precursor miRNAs (pre-
miRNA). Indirectly involved in the production of trans-acting
small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or
TAS3 endogenous transcripts by participating in the production of
their initiating miRNAs. Involved with argonaute 1 (AGO1) in the
guide strand selection from miRNA duplexes, presumably by
directional loading of the miRNA duplex (guide stand and passenger
strand) onto the RNA-induced silencing complex (RISC) for
passenger strand degradation. Does not participate in sense
transgene-induced post-transcriptional gene silencing (S-PTGS).
Involved in several plant development aspects and response to
hormones through its role in miRNAs processing.
{ECO:0000269|PubMed:11148283, ECO:0000269|PubMed:14722360,
ECO:0000269|PubMed:14972688, ECO:0000269|PubMed:15821876,
ECO:0000269|PubMed:16428603, ECO:0000269|PubMed:16889646,
ECO:0000269|PubMed:17337628, ECO:0000269|PubMed:18632569,
ECO:0000269|PubMed:19304749, ECO:0000269|PubMed:19861421,
ECO:0000269|PubMed:20462493, ECO:0000269|PubMed:20735118}.
-!- SUBUNIT: Homodimer. Heterodimer with DRB2, DRB4 or DRB5. Interacts
with SE and DCL1 (PubMed:15821876, PubMed:16428603,
PubMed:16889646, PubMed:20462493). Interacts with RCF3, RS40 and
RS41 (PubMed:26227967). {ECO:0000269|PubMed:15821876,
ECO:0000269|PubMed:16428603, ECO:0000269|PubMed:16889646,
ECO:0000269|PubMed:20462493, ECO:0000269|PubMed:26227967}.
-!- INTERACTION:
Q3EBC8:At3g03300; NbExp=2; IntAct=EBI-632620, EBI-2464030;
Q9SP32:DCL1; NbExp=3; IntAct=EBI-632620, EBI-632627;
Q8GY79:DRB5; NbExp=4; IntAct=EBI-632620, EBI-632672;
Q9ZVD0:SE; NbExp=5; IntAct=EBI-632620, EBI-6553299;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14722360,
ECO:0000269|PubMed:17337628, ECO:0000269|PubMed:17442570}. Nucleus
speckle {ECO:0000269|PubMed:26227967}. Note=Localizes to nuclear
dicing body (also named D body), a nuclear body distributed
throughout the nucleoplasm and involved in miRNA processing.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O04492-1; Sequence=Displayed;
Name=2;
IsoId=O04492-2; Sequence=VSP_040613;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in rosette and cauline leaves,
stems, roots, flowers and siliques. {ECO:0000269|PubMed:11148283,
ECO:0000269|PubMed:16889646}.
-!- INDUCTION: By abscisic acid (ABA). {ECO:0000269|PubMed:11148283}.
-!- DOMAIN: The dsRNA binding domains (dsRBDs) 1 and 2 are sufficient
for the function in miRNA precursors processing and mature miRNA
generation. {ECO:0000269|PubMed:17337628,
ECO:0000269|PubMed:20462493, ECO:0000269|PubMed:20735118}.
-!- DISRUPTION PHENOTYPE: Short plant, delayed flowering, leaf
hyponasty, reduced fertility, decreased rate of root growth,
altered root gravitropic response, decreased sensitivity to auxin
and cytokinin and hypersensitivity to abscisic acid (ABA).
Reduction of several miRNA accumulation.
{ECO:0000269|PubMed:11148283, ECO:0000269|PubMed:14972688,
ECO:0000269|PubMed:16889646}.
-!- MISCELLANEOUS: Plants overexpressing HYL1 show decreased stability
of transcripts targeted by miRNAs.
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EMBL; AF276440; AAG49890.1; -; mRNA.
EMBL; AC000132; AAB60726.1; -; Genomic_DNA.
EMBL; CP002684; AEE28481.1; -; Genomic_DNA.
EMBL; AY054631; AAK96822.1; -; mRNA.
EMBL; AY081525; AAM10087.1; -; mRNA.
EMBL; AK319123; BAH57238.1; -; mRNA.
PIR; H86230; H86230.
RefSeq; NP_563850.1; NM_100842.4. [O04492-1]
UniGene; At.10223; -.
PDB; 2L2M; NMR; -; A=97-170.
PDB; 2L2N; NMR; -; A=1-100.
PDB; 3ADG; X-ray; 1.70 A; A=15-84.
PDB; 3ADI; X-ray; 3.20 A; A/B/C=15-84.
PDB; 3ADJ; X-ray; 3.00 A; A=100-172.
PDBsum; 2L2M; -.
PDBsum; 2L2N; -.
PDBsum; 3ADG; -.
PDBsum; 3ADI; -.
PDBsum; 3ADJ; -.
ProteinModelPortal; O04492; -.
SMR; O04492; -.
BioGrid; 22739; 19.
DIP; DIP-33453N; -.
IntAct; O04492; 6.
STRING; 3702.AT1G09700.1; -.
PaxDb; O04492; -.
EnsemblPlants; AT1G09700.1; AT1G09700.1; AT1G09700. [O04492-1]
GeneID; 837498; -.
Gramene; AT1G09700.1; AT1G09700.1; AT1G09700.
KEGG; ath:AT1G09700; -.
Araport; AT1G09700; -.
TAIR; locus:2024407; AT1G09700.
eggNOG; ENOG410IWVA; Eukaryota.
eggNOG; ENOG4111ZFG; LUCA.
InParanoid; O04492; -.
OMA; SCMNGLK; -.
OrthoDB; EOG093606OP; -.
EvolutionaryTrace; O04492; -.
PRO; PR:O04492; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; O04492; AT.
GO; GO:0010445; C:nuclear dicing body; IDA:TAIR.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003725; F:double-stranded RNA binding; IDA:TAIR.
GO; GO:0035198; F:miRNA binding; IDA:TAIR.
GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
GO; GO:0010589; P:leaf proximal/distal pattern formation; IMP:TAIR.
GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
GO; GO:0035279; P:mRNA cleavage involved in gene silencing by miRNA; IMP:TAIR.
GO; GO:0031054; P:pre-miRNA processing; IMP:UniProtKB.
GO; GO:0031053; P:primary miRNA processing; IBA:GO_Central.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:TAIR.
GO; GO:0010267; P:production of ta-siRNAs involved in RNA interference; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
GO; GO:0009733; P:response to auxin; IMP:TAIR.
GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
InterPro; IPR031147; DRB.
InterPro; IPR014720; dsRBD_dom.
PANTHER; PTHR11207:SF10; PTHR11207:SF10; 1.
Pfam; PF00035; dsrm; 2.
SMART; SM00358; DSRM; 2.
PROSITE; PS50137; DS_RBD; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Nucleus;
Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing.
CHAIN 1 419 Double-stranded RNA-binding protein 1.
/FTId=PRO_0000404652.
DOMAIN 15 84 DRBM 1. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 101 170 DRBM 2. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
REPEAT 247 274 1.
REPEAT 275 302 2.
REPEAT 303 330 3.
REPEAT 331 358 4.
REPEAT 359 386 5.
REPEAT 387 414 6.
REGION 247 414 6 X 28 AA repeats of E-K-I-E-T-T-P-N-L-E-
[PS]-[PS]-S-C-M-[NS]-G-L-K-E-A-A-F-G-S-V-
E-T.
MOTIF 207 222 Bipartite nuclear localization.
VAR_SEQ 72 87 Missing (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_040613.
HELIX 16 26 {ECO:0000244|PDB:3ADG}.
STRAND 33 41 {ECO:0000244|PDB:3ADG}.
STRAND 42 44 {ECO:0000244|PDB:2L2N}.
STRAND 46 53 {ECO:0000244|PDB:3ADG}.
STRAND 56 59 {ECO:0000244|PDB:3ADG}.
STRAND 64 66 {ECO:0000244|PDB:3ADG}.
HELIX 67 82 {ECO:0000244|PDB:3ADG}.
HELIX 100 111 {ECO:0000244|PDB:3ADJ}.
TURN 112 114 {ECO:0000244|PDB:3ADJ}.
STRAND 119 126 {ECO:0000244|PDB:3ADJ}.
STRAND 128 130 {ECO:0000244|PDB:3ADJ}.
STRAND 132 140 {ECO:0000244|PDB:3ADJ}.
STRAND 143 146 {ECO:0000244|PDB:3ADJ}.
STRAND 150 152 {ECO:0000244|PDB:3ADJ}.
HELIX 153 169 {ECO:0000244|PDB:3ADJ}.
SEQUENCE 419 AA; 45547 MW; FDBE165679537DFB CRC64;
MTSTDVSSGV SNCYVFKSRL QEYAQKYKLP TPVYEIVKEG PSHKSLFQST VILDGVRYNS
LPGFFNRKAA EQSAAEVALR ELAKSSELSQ CVSQPVHETG LCKNLLQEYA QKMNYAIPLY
QCQKVETLGR VTQFTCTVEI GGIKYTGAAT RTKKDAEISA GRTALLAIQS DTKNNLANYN
TQLTVLPCEK KTIQAAIPLK ETVKTLKARK AQFKKKAQKG KRTVAKNPED IIIPPQPTDH
CQNDQSEKIE TTPNLEPSSC MNGLKEAAFG SVETEKIETT PNLEPPSCMN GLKEAAFGSV
ETEKIETTPN LEPPSCMNGL KEAAFGSVET EKIETTPNLE PSSCMNGLKE AAFGSVETEK
IETTPNLEPP SCMNGLKEAA FGSVETEKIE TTPNLESSSC MSGLKEAAFG SVETEASHA


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Genprice Inc, Invoices and accounting
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