RTL2_ARATH
ID RTL2_ARATH Reviewed; 391 AA.
AC Q9LTQ0; Q94B67;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ribonuclease 3-like protein 2;
DE EC=3.1.26.-;
DE AltName: Full=Ribonuclease III-like protein 2;
DE Short=RNase III-like protein 2;
DE AltName: Full=Ribonuclease three-like protein 2;
GN Name=RTL2; OrderedLocusNames=At3g20420; ORFNames=MQC12.21;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=18158302; DOI=10.1093/nar/gkm1130;
RA Comella P., Pontvianne F., Lahmy S., Vignols F., Barbezier N., Debures A.,
RA Jobet E., Brugidou E., Echeverria M., Saez-Vasquez J.;
RT "Characterization of a ribonuclease III-like protein required for cleavage
RT of the pre-rRNA in the 3'ETS in Arabidopsis.";
RL Nucleic Acids Res. 36:1163-1175(2008).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ASP-100.
RX PubMed=20978817; DOI=10.1007/s10265-010-0382-x;
RA Kiyota E., Okada R., Kondo N., Hiraguri A., Moriyama H., Fukuhara T.;
RT "An Arabidopsis RNase III-like protein, AtRTL2, cleaves double-stranded RNA
RT in vitro.";
RL J. Plant Res. 124:405-414(2011).
CC -!- FUNCTION: Ribonuclease that cleaves double-stranded RNA (dsRNA).
CC Required for 3'-external transcribed spacer (ETS) cleavage of the pre-
CC rRNA precursors. May promote the production of 21 nucleotide small
CC interfering RNA (siRNA) during post-transcriptional gene silencing
CC (PTGS). {ECO:0000269|PubMed:18158302, ECO:0000269|PubMed:20978817}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds Mg(2+) or Mn(2+). {ECO:0000250};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305|PubMed:18158302}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18158302}. Cytoplasm
CC {ECO:0000269|PubMed:18158302}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds, leaves and flower buds.
CC {ECO:0000269|PubMed:18158302}.
CC -!- DEVELOPMENTAL STAGE: Expressed in siliques from 0 to 10 days after
CC fertilization (DAF). Levels decrease at 13 DAF and disappear at 16 DAF.
CC Expressed early in seed germination from 6 hours to 48 hours after seed
CC imbibition. {ECO:0000269|PubMed:18158302}.
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DR EMBL; AB024036; BAB02825.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76376.1; -; Genomic_DNA.
DR EMBL; AY042815; AAK68755.2; -; mRNA.
DR EMBL; AY081681; AAM10243.1; -; mRNA.
DR RefSeq; NP_566661.1; NM_112933.3.
DR AlphaFoldDB; Q9LTQ0; -.
DR SMR; Q9LTQ0; -.
DR BioGRID; 6919; 8.
DR IntAct; Q9LTQ0; 7.
DR STRING; 3702.AT3G20420.1; -.
DR PaxDb; Q9LTQ0; -.
DR PRIDE; Q9LTQ0; -.
DR ProteomicsDB; 228048; -.
DR EnsemblPlants; AT3G20420.1; AT3G20420.1; AT3G20420.
DR GeneID; 821587; -.
DR Gramene; AT3G20420.1; AT3G20420.1; AT3G20420.
DR KEGG; ath:AT3G20420; -.
DR Araport; AT3G20420; -.
DR TAIR; locus:2092409; AT3G20420.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_5_0_1; -.
DR InParanoid; Q9LTQ0; -.
DR OMA; DIKHWKN; -.
DR OrthoDB; 935825at2759; -.
DR PhylomeDB; Q9LTQ0; -.
DR PRO; PR:Q9LTQ0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LTQ0; baseline and differential.
DR Genevisible; Q9LTQ0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IMP:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 1.10.1520.10; -; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Endonuclease; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nuclease; Nucleus; Reference proteome; Repeat; RNA-binding;
KW rRNA processing.
FT CHAIN 1..391
FT /note="Ribonuclease 3-like protein 2"
FT /id="PRO_0000404663"
FT DOMAIN 60..203
FT /note="RNase III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 218..294
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 313..387
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT MOTIF 7..26
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT MOTIF 371..387
FT /note="Bipartite nuclear localization"
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 185
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT DISULFID 240..322
FT /evidence="ECO:0000255"
FT MUTAGEN 100
FT /note="D->A: Unable to cleave dsRNA."
FT /evidence="ECO:0000269|PubMed:20978817"
FT CONFLICT 81
FT /note="I -> V (in Ref. 3; AAK68755/AAM10243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 44109 MW; 3200AC9E81B37CAB CRC64;
MDHSISPEYN FPAITRCSLS NSLPHRPPSP LPSSADIHRF YNSLSPSAPS VPVSSEMESM
EAVEKILNYK FSNKSLLKEA ITHTSCTDFP SYERLEFIGD SAIGLAISNY LYLTYPSLEP
HDLSLLRAAN VSTEKLARVS LNHGLYSFLR RNAPSLDEKV KEFSEAVGKE DDLSVSYGGL
VKAPKVLADL FESLAGAVYV DVNFDLQRLW VIFRGLLEPI VTLDDLQKQP QPVSMLFKLC
HKHKKRIDIK NWKDGNVSIA VIYLDDELLA SGRAENKDIA RLIAAKEALR KLSEVFPVEM
VIDEDSVEIQ LTHAKTKLNE ICLKKKWPKP IYSVEEDRSS VQGKRFVCSA KIKITEEKTL
YMKGDEQSKI KKAESSSAYH MIRALRKSHY L
