WEX_ARATH
ID WEX_ARATH Reviewed; 288 AA.
AC Q84LH3; Q6QPM3; Q9FT68; Q9SVM6;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=3'-5' exonuclease {ECO:0000303|PubMed:12937173};
DE EC=3.1.-.- {ECO:0000269|PubMed:12937173};
DE AltName: Full=Werner Syndrome-like exonuclease;
GN Name=WEX; Synonyms=WRNEXO; OrderedLocusNames=At4g13870; ORFNames=F18A5.260;
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 [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INTERACTION
RP WITH RECQL2.
RX PubMed=11058127; DOI=10.1093/nar/28.21.4275;
RA Hartung F., Plchova H., Puchta H.;
RT "Molecular characterisation of RecQ homologues in Arabidopsis thaliana.";
RL Nucleic Acids Res. 28:4275-4282(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISRUPTION PHENOTYPE.
RX PubMed=12887585; DOI=10.1046/j.1365-313x.2003.01810.x;
RA Glazov E., Phillips K., Budziszewski G.J., Schob H., Meins F. Jr.,
RA Levin J.Z.;
RT "A gene encoding an RNase D exonuclease-like protein is required for post-
RT transcriptional silencing in Arabidopsis.";
RL Plant J. 35:342-349(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-287.
RC STRAIN=cv. Cit-0, cv. Columbia, cv. Ct-1, cv. Gd-1, cv. Gr-1, cv. Ita-0,
RC and cv. Kr-0;
RX PubMed=14871304; DOI=10.1111/j.0960-7412.2003.01999.x;
RA Comai L., Young K., Till B.J., Reynolds S.H., Greene E.A., Codomo C.A.,
RA Enns L.C., Johnson J.E., Burtner C., Odden A.R., Henikoff S.;
RT "Efficient discovery of DNA polymorphisms in natural populations by
RT Ecotilling.";
RL Plant J. 37:778-786(2004).
RN [7]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF GLU-135.
RX PubMed=12937173; DOI=10.1074/jbc.m303891200;
RA Plchova H., Hartung F., Puchta H.;
RT "Biochemical characterization of an exonuclease from Arabidopsis thaliana
RT reveals similarities to the DNA exonuclease of the human Werner syndrome
RT protein.";
RL J. Biol. Chem. 278:44128-44138(2003).
RN [8]
RP INTERACTION WITH KU70 AND KU80, AND ACTIVITY REGULATION.
RX PubMed=16396834; DOI=10.1093/nar/gki984;
RA Li B., Conway N., Navarro S., Comai L., Comai L.;
RT "A conserved and species-specific functional interaction between the Werner
RT syndrome-like exonuclease atWEX and the Ku heterodimer in Arabidopsis.";
RL Nucleic Acids Res. 33:6861-6867(2005).
CC -!- FUNCTION: Exonuclease that digests recessed strands of DNA duplexes in
CC the 3' to 5' direction but hardly single-stranded DNA or blunt-ended
CC duplexes. Also able to digest 3'-protruding strands and 3'-recessed
CC strand termini of duplexes containing mismatched bases.
CC {ECO:0000269|PubMed:12937173}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12937173};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12937173};
CC -!- ACTIVITY REGULATION: Activated upon interaction with the KU
CC heterodimer. Not stimulated by ATP. {ECO:0000269|PubMed:16396834}.
CC -!- SUBUNIT: Interacts with KU70 and KU80. Interacts with RECQL2.
CC {ECO:0000269|PubMed:11058127, ECO:0000269|PubMed:16396834}.
CC -!- INTERACTION:
CC Q84LH3; Q9FQ08: KU70; NbExp=2; IntAct=EBI-926580, EBI-476083;
CC Q84LH3; Q9FQ09: KU80; NbExp=2; IntAct=EBI-926580, EBI-926593;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84LH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84LH3-2; Sequence=VSP_039138;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:11058127}.
CC -!- DISRUPTION PHENOTYPE: Early flowering. Loss of post-transcriptional
CC gene silencing (PTGS), but not of transcriptional gene silencing (TGS).
CC {ECO:0000269|PubMed:12887585}.
CC -!- MISCELLANEOUS: Helix-distorting lesions (apurinic sites and cholesterol
CC adducts) and oxidative DNA damage (such as 8-oxoadenine and 8-
CC oxoguanine) block the exonuclease activity, while other DNA
CC modifications such as uracil, hypoxanthine or ethenoadenine have no
CC effects.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36851.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78429.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ404476; CAC14871.1; -; mRNA.
DR EMBL; AF531179; AAO33765.1; -; mRNA.
DR EMBL; AL035528; CAB36851.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161537; CAB78429.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83338.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83339.1; -; Genomic_DNA.
DR EMBL; BT010908; AAR24686.1; -; mRNA.
DR EMBL; AY530745; AAS45430.1; -; Genomic_DNA.
DR PIR; T05256; T05256.
DR RefSeq; NP_193123.2; NM_117461.2. [Q84LH3-2]
DR RefSeq; NP_974543.1; NM_202814.2. [Q84LH3-1]
DR AlphaFoldDB; Q84LH3; -.
DR SMR; Q84LH3; -.
DR BioGRID; 12318; 1.
DR IntAct; Q84LH3; 3.
DR STRING; 3702.AT4G13870.2; -.
DR PaxDb; Q84LH3; -.
DR PRIDE; Q84LH3; -.
DR EnsemblPlants; AT4G13870.1; AT4G13870.1; AT4G13870. [Q84LH3-2]
DR EnsemblPlants; AT4G13870.2; AT4G13870.2; AT4G13870. [Q84LH3-1]
DR GeneID; 827021; -.
DR Gramene; AT4G13870.1; AT4G13870.1; AT4G13870. [Q84LH3-2]
DR Gramene; AT4G13870.2; AT4G13870.2; AT4G13870. [Q84LH3-1]
DR KEGG; ath:AT4G13870; -.
DR Araport; AT4G13870; -.
DR TAIR; locus:2119525; AT4G13870.
DR eggNOG; KOG4373; Eukaryota.
DR InParanoid; Q84LH3; -.
DR OMA; CCYVYQL; -.
DR OrthoDB; 1295758at2759; -.
DR PhylomeDB; Q84LH3; -.
DR PRO; PR:Q84LH3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84LH3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Exonuclease; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..288
FT /note="3'-5' exonuclease"
FT /id="PRO_0000394132"
FT DOMAIN 129..279
FT /note="3'-5' exonuclease"
FT REGION 30..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 276..278
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11058127"
FT /id="VSP_039138"
FT MUTAGEN 135
FT /note="E->A: Loss of exonucleolytic activity."
FT /evidence="ECO:0000269|PubMed:12937173"
SQ SEQUENCE 288 AA; 32090 MW; C9B07E30377486CF CRC64;
MSSSNWIDDA FTEEELLAID AIEASYNFSR SSSSSSSAAP TVQATTSVHG HEEDPNQIPN
NIRRQLPRSI TSSTSYKRFP LSRCRARNFP AMRFGGRILY SKTATEVDKR AMQLIKVLDT
KRDESGIAFV GLDIEWRPSF RKGVLPGKVA TVQICVDSNY CDVMHIFHSG IPQSLQHLIE
DSTLVKVGIG IDGDSVKLFH DYGVSIKDVE DLSDLANQKI GGDKKWGLAS LTETLVCKEL
LKPNRIRLGN WEFYPLSKQQ LQYAATDAYA SWHLYKVLKD LPDAVSGS
