ID   DRB2_ARATH              Reviewed;         434 AA.
AC   Q9SKN2;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Double-stranded RNA-binding protein 2;
DE   AltName: Full=dsRNA-binding protein 2;
DE            Short=AtDRB2;
GN   Name=DRB2; OrderedLocusNames=At2g28380; ORFNames=T1B3.10;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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].
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   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH DCL1; DCL5;
RP   DRB1 AND DRB5.
RX   PubMed=15821876; DOI=10.1007/s11103-004-6853-5;
RA   Hiraguri A., Itoh R., Kondo N., Nomura Y., Aizawa D., Murai Y., Koiwa H.,
RA   Seki M., Shinozaki K., Fukuhara T.;
RT   "Specific interactions between Dicer-like proteins and HYL1/DRB-family
RT   dsRNA-binding proteins in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 57:173-188(2005).
RN   [5]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=18625233; DOI=10.1016/j.febslet.2008.07.004;
RA   Curtin S.J., Watson J.M., Smith N.A., Eamens A.L., Blanchard C.L.,
RA   Waterhouse P.M.;
RT   "The roles of plant dsRNA-binding proteins in RNAi-like pathways.";
RL   FEBS Lett. 582:2753-2760(2008).
CC   -!- FUNCTION: Binds double-stranded RNA. May be involved in RNA-mediated
CC       silencing. {ECO:0000269|PubMed:15821876}.
CC   -!- SUBUNIT: Heterodimer with DRB1 or DRB5. Interacts with DCL1 and DCL5.
CC       {ECO:0000269|PubMed:15821876}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15821876}.
CC   -!- DISRUPTION PHENOTYPE: Flat, serrated, blue-green and ovoid leaves.
CC       {ECO:0000269|PubMed:18625233}.
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DR   EMBL; AC006283; AAD20688.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08114.1; -; Genomic_DNA.
DR   EMBL; AY034976; AAK59481.1; -; mRNA.
DR   EMBL; AY062965; AAL33811.1; -; mRNA.
DR   PIR; B84684; B84684.
DR   RefSeq; NP_565672.1; NM_128398.4.
DR   AlphaFoldDB; Q9SKN2; -.
DR   SMR; Q9SKN2; -.
DR   BioGRID; 2736; 11.
DR   IntAct; Q9SKN2; 8.
DR   STRING; 3702.AT2G28380.1; -.
DR   PaxDb; Q9SKN2; -.
DR   PRIDE; Q9SKN2; -.
DR   ProteomicsDB; 241258; -.
DR   EnsemblPlants; AT2G28380.1; AT2G28380.1; AT2G28380.
DR   GeneID; 817386; -.
DR   Gramene; AT2G28380.1; AT2G28380.1; AT2G28380.
DR   KEGG; ath:AT2G28380; -.
DR   Araport; AT2G28380; -.
DR   TAIR; locus:2057491; AT2G28380.
DR   eggNOG; ENOG502QTBA; Eukaryota.
DR   HOGENOM; CLU_038996_1_1_1; -.
DR   InParanoid; Q9SKN2; -.
DR   OMA; SMPEPEN; -.
DR   OrthoDB; 752697at2759; -.
DR   PhylomeDB; Q9SKN2; -.
DR   PRO; PR:Q9SKN2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SKN2; baseline and differential.
DR   Genevisible; Q9SKN2; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:TAIR.
DR   GO; GO:0035196; P:miRNA processing; IMP:TAIR.
DR   CDD; cd19907; DSRM_AtDRB-like_rpt1; 1.
DR   CDD; cd19908; DSRM_AtDRB-like_rpt2; 1.
DR   InterPro; IPR044450; AtDRB-like_DSRM_1.
DR   InterPro; IPR044451; AtDRB-like_DSRM_2.
DR   InterPro; IPR014720; dsRBD_dom.
DR   Pfam; PF00035; dsrm; 2.
DR   SMART; SM00358; DSRM; 2.
DR   PROSITE; PS50137; DS_RBD; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Repeat; RNA-binding;
KW   RNA-mediated gene silencing.
FT   CHAIN           1..434
FT                   /note="Double-stranded RNA-binding protein 2"
FT                   /id="PRO_0000404653"
FT   DOMAIN          1..70
FT                   /note="DRBM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   DOMAIN          87..155
FT                   /note="DRBM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   REGION          402..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  47440 MW;  72DE2AC3C567C16C CRC64;
     MYKNQLQELA QRSCFNLPSY TCIREGPDHA PRFKATVNFN GEIFESPQYC STLRQAEHSA
     AEVALNALSN RGPSHSLAAR ILDETGVYKN LLQEIAQRVG APLPRYTTFR SGLGHQPVFT
     GTVELAGITF TGDPAKNKKQ AEKNAAMAAW SSLKQLAKET SSSMPEPENI DELEQVIIAR
     ALINYRIKEN IGTGSSSSAP VPFAKKFFMQ NLRPTSPQPS PATTSRILPF ICPKQPSRSS
     RSSLAATSGI DRIMAAALES RSYQRPQQRF ANPPYVPMRQ FRSQCHGMAP PVTIRTAVPV
     FSAPPMPPPP CTNNTQLPSS VYVPSLMRTA PPVRIAPPVT IRTAVPVFAS APPVRIRTAV
     KPTVEAGETR ISSVQEKESI PVLPDSLEIG VEGSTITITD CEKTASKETE RAEFKDSSKG
     EPETARERLE NLKI