ID   DI32L_ARATH             Reviewed;        1055 AA.
AC   Q0WPN0; Q56WY4; Q9CA26;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Inactive exonuclease DIS3L2;
DE   AltName: Full=DIS3-like exonuclease 2;
DE   AltName: Full=Protein SUPPRESSOR OF VARICOSE {ECO:0000303|PubMed:20798041};
DE   AltName: Full=RRP44 homolog B {ECO:0000305};
DE   AltName: Full=Ribosomal RNA-processing protein 44 homolog B {ECO:0000305};
DE            Short=AtRRP44B {ECO:0000303|PubMed:24244451};
GN   Name=SOV {ECO:0000303|PubMed:20798041}; Synonyms=DIS3L2;
GN   OrderedLocusNames=At1g77680; ORFNames=T32E8.1, T5M16;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   LACK OF FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20798041; DOI=10.1073/pnas.1007060107;
RA   Zhang W., Murphy C., Sieburth L.E.;
RT   "Conserved RNaseII domain protein functions in cytoplasmic mRNA decay and
RT   suppresses Arabidopsis decapping mutant phenotypes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:15981-15985(2010).
RN   [5]
RP   FUNCTION.
RX   PubMed=24244451; DOI=10.1371/journal.pone.0079219;
RA   Kumakura N., Otsuki H., Tsuzuki M., Takeda A., Watanabe Y.;
RT   "Arabidopsis AtRRP44A is the functional homolog of Rrp44/Dis3, an exosome
RT   component, is essential for viability and is required for RNA processing
RT   and degradation.";
RL   PLoS ONE 8:E79219-E79219(2013).
CC   -!- FUNCTION: Probable inactive 3'-5'-exoribonuclease. Is unable to
CC       complement the growth defect of a yeast mutant lacking RRP44
CC       exonuclease (PubMed:24244451). {ECO:0000269|PubMed:20798041,
CC       ECO:0000269|PubMed:24244451}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11130712}.
CC       Note=Localizes to cytoplasmic foci. {ECO:0000269|PubMed:11130712}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: The protein in cv. Landsberg erecta (AC P0DM58) and cv.
CC       Columbia only differ by one residue in position 705 (a Pro and Arg
CC       residue, respectively); this variation leading to inactivate the
CC       protein in cv. Columbia. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD94251.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC010704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC012193; AAG51632.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36008.1; -; Genomic_DNA.
DR   EMBL; AK221895; BAD94251.1; ALT_INIT; mRNA.
DR   EMBL; AK229034; BAF00919.1; -; mRNA.
DR   PIR; E96806; E96806.
DR   RefSeq; NP_177891.1; NM_106417.3.
DR   AlphaFoldDB; Q0WPN0; -.
DR   SMR; Q0WPN0; -.
DR   STRING; 3702.AT1G77680.1; -.
DR   iPTMnet; Q0WPN0; -.
DR   PaxDb; Q0WPN0; -.
DR   PRIDE; Q0WPN0; -.
DR   ProteomicsDB; 224277; -.
DR   EnsemblPlants; AT1G77680.1; AT1G77680.1; AT1G77680.
DR   GeneID; 844104; -.
DR   Gramene; AT1G77680.1; AT1G77680.1; AT1G77680.
DR   KEGG; ath:AT1G77680; -.
DR   Araport; AT1G77680; -.
DR   TAIR; locus:2203231; AT1G77680.
DR   eggNOG; KOG2102; Eukaryota.
DR   HOGENOM; CLU_002333_5_2_1; -.
DR   OMA; WTRMKGP; -.
DR   OrthoDB; 1104619at2759; -.
DR   PhylomeDB; Q0WPN0; -.
DR   PRO; PR:Q0WPN0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q0WPN0; baseline and differential.
DR   Genevisible; Q0WPN0; AT.
DR   GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IEA:InterPro.
DR   GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03045; DIS3L2; 1.
DR   InterPro; IPR041505; Dis3_CSD2.
DR   InterPro; IPR028591; DIS3L2.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   Pfam; PF17849; OB_Dis3; 1.
DR   Pfam; PF00773; RNB; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; SSF50249; 3.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Magnesium; Metal-binding; Reference proteome; RNA-binding.
FT   CHAIN           1..1055
FT                   /note="Inactive exonuclease DIS3L2"
FT                   /id="PRO_0000423297"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         488
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT   CONFLICT        903
FT                   /note="Y -> F (in Ref. 3; BAD94251)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1055 AA;  116843 MW;  FD95800ECE781B31 CRC64;
     MKSASSEQSV ERIENGHKKK RNRPQKQNRR SKQSSVPIED AHVEESLDGR DSSRSKAKDS
     TSSSKQQRPN TDELEAMRAS NVAFNSMPPM RAESGYPRRS ASPLLSSPEV SKQLLSKSCP
     DPRACEQSPG MNGELFQQIE GSSQRKIFSS HWSLDAVTEA LEKGEAFKAL FRVNAHNRNE
     AYCKIDGVPT DILINGNVCQ SRAVEGDTVV IKLDPLSLWP KMKGFVTESA AKPEGTNSPP
     EKDDKKARQK NGIDVVEGFE DGFSKNKSSV IGKGAKNGVT PSSPPSLDSC LGSFCEQKGN
     CSAVDKLCGI LSSFPHKRPT GQVVAVVEKS LVRDSIVGLL DVKGWIHYKE SDPKRCKSPL
     SLSDDEYVQL MPADPRFPKL IVPFHVLPGS IRARLENLDP NLEAELVAAQ IVDWGEGSPF
     PVAQITHLFG RGSELEPQIN AILYQNSVCD SDFSPGSLTS LPRVPWEVPE EEVQRRKDLR
     DLCVLTIDPS TATDLDDALS VQSLPGGFFR VGVHIADVSY FVLPETALDT EARFRSTSVY
     LMQRKISMLP PLLSENVGSL SPGADRLAFS ILWDLNREGD VIDRWIGRTI IRSCCKLSYD
     HAQDIIDGKS DVAENGWPAL HGSFKWCDVT RSVKQLSEIS TTLRQKRFRN GALQLENSKP
     VFLFDEHGVP YDFVTCSRKG SNFLVEEFML LANMTAAEVI SQAYRASSLL RRHPEPNTRK
     LKEFEGFCSK HGMDLDISSS GQLQDSLEKI TGNLKDDSVF VDILNNYAIK PMQLASYFCT
     GNLKDSVAEW GHYALAVPLY THFTSPLRRY PDIVVHRALA AALEAEELYS KQKQTAIDEG
     RSCFTGIHFN KDAAESIEGK EALSVAALKH GVPSTEILSD VAAYCNERKL AARKVRDACD
     KLYTWFVLKQ KEIFPCEARV MNLGSRFMTV YISKLGIERR IYYDQIEGLC ADWLEATSTL
     IVDKLYSKRG GRGFFKPMKE AVYLVSPCEV CVAKCSALSV HDTESPEAVS IDEVAPAVFP
     LTIQLFSTIP VVLHAVGGDD GPLDIGARLY MSSYY