DI3L2_ARATH
ID DI3L2_ARATH Reviewed; 1055 AA.
AC P0DM58;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=DIS3-like exonuclease 2 {ECO:0000255|HAMAP-Rule:MF_03045};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_03045};
DE AltName: Full=Protein SUPPRESSOR OF VARICOSE;
GN Name=SOV; Synonyms=DIS3L2;
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP PRO-705.
RC STRAIN=cv. Landsberg erecta;
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).
CC -!- FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs
CC polyuridylated at their 3' end and mediates their degradation.
CC Component of an exosome-independent RNA degradation pathway that
CC mediates degradation of cytoplasmic mRNAs that have been deadenylated
CC and subsequently uridylated at their 3' (Probable).
CC {ECO:0000305|PubMed:20798041}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03045};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03045,
CC ECO:0000269|PubMed:20798041}. Cytoplasm, P-body
CC {ECO:0000305|PubMed:20798041}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20798041}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03045}.
CC -!- CAUTION: The protein in cv. Landsberg erecta and cv. Columbia (AC
CC Q0WPN0) 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 (AC Q0WPN0). {ECO:0000305}.
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DR AlphaFoldDB; P0DM58; -.
DR SMR; P0DM58; -.
DR ExpressionAtlas; P0DM58; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; TAS:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Exonuclease; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nuclease; RNA-binding.
FT CHAIN 1..1055
FT /note="DIS3-like exonuclease 2"
FT /id="PRO_0000423298"
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 SITE 496
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT MUTAGEN 705
FT /note="P->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20798041"
SQ SEQUENCE 1055 AA; 116784 MW; 5BBCE243BED444F8 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 SQAYPASSLL 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
