ENDO5_ARATH
ID ENDO5_ARATH Reviewed; 296 AA.
AC F4JJL3; O65425; Q8LA68;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Endonuclease 5 {ECO:0000303|PubMed:17651368};
DE Short=AtENDO5 {ECO:0000303|PubMed:17651368};
DE EC=3.1.30.1 {ECO:0000269|PubMed:17651368, ECO:0000269|PubMed:23620482};
DE AltName: Full=Deoxyribonuclease ENDO5 {ECO:0000303|PubMed:17651368};
DE AltName: Full=Single-stranded-nucleate endonuclease ENDO5 {ECO:0000303|PubMed:17651368};
DE Flags: Precursor;
GN Name=ENDO5 {ECO:0000303|PubMed:17651368};
GN OrderedLocusNames=At4g21600 {ECO:0000312|Araport:AT4G21600};
GN ORFNames=F17L22.60 {ECO:0000312|EMBL:CAB36804.1},
GN F18E5.220 {ECO:0000312|EMBL:CAA18724.1};
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=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 [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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17651368; DOI=10.1111/j.1365-313x.2007.03201.x;
RA Triques K., Sturbois B., Gallais S., Dalmais M., Chauvin S., Clepet C.,
RA Aubourg S., Rameau C., Caboche M., Bendahmane A.;
RT "Characterization of Arabidopsis thaliana mismatch specific endonucleases:
RT application to mutation discovery by TILLING in pea.";
RL Plant J. 51:1116-1125(2007).
RN [5]
RP FUNCTION, MUTAGENESIS OF 281-ALA--LEU-296, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, COFACTOR, PROTEOLYTIC CLEAVAGE, AND GENE FAMILY.
RX PubMed=23620482; DOI=10.1093/pcp/pct061;
RA Lesniewicz K., Karlowski W.M., Pienkowska J.R., Krzywkowski P., Poreba E.;
RT "The plant s1-like nuclease family has evolved a highly diverse range of
RT catalytic capabilities.";
RL Plant Cell Physiol. 54:1064-1078(2013).
CC -!- FUNCTION: Hydrolyzes, with low efficiency, only single-stranded DNA and
CC RNA without apparent specificity for bases (PubMed:17651368,
CC PubMed:23620482). Endonuclease that recognizes and cleaves some
CC mismatches with high efficiency, including heteroduplex double-stranded
CC DNA; mostly efficient on T/G, A/G and G/G mismatches, less efficient
CC for T/T and poorly efficient for C/C, A/A, T/C and A/C
CC (PubMed:17651368). {ECO:0000269|PubMed:17651368,
CC ECO:0000269|PubMed:23620482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-
CC phosphooligonucleotide end-products.; EC=3.1.30.1;
CC Evidence={ECO:0000269|PubMed:17651368, ECO:0000269|PubMed:23620482};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23620482};
CC Note=Binds 3 divalent metal cations. {ECO:0000269|PubMed:23620482};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8 with RNA and ssDNA as substrates.
CC {ECO:0000269|PubMed:23620482};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclease type I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18724.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB36804.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81267.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022603; CAA18724.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL035527; CAB36804.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161555; CAB81267.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84479.1; -; Genomic_DNA.
DR EMBL; AY087996; AAM65542.1; -; mRNA.
DR PIR; T05168; T05168.
DR RefSeq; NP_567631.1; NM_118280.2.
DR AlphaFoldDB; F4JJL3; -.
DR SMR; F4JJL3; -.
DR BioGRID; 13535; 1.
DR STRING; 3702.AT4G21600.1; -.
DR PaxDb; F4JJL3; -.
DR PRIDE; F4JJL3; -.
DR ProteomicsDB; 222694; -.
DR EnsemblPlants; AT4G21600.1; AT4G21600.1; AT4G21600.
DR GeneID; 828246; -.
DR Gramene; AT4G21600.1; AT4G21600.1; AT4G21600.
DR KEGG; ath:AT4G21600; -.
DR Araport; AT4G21600; -.
DR TAIR; locus:2119612; AT4G21600.
DR eggNOG; ENOG502QRXU; Eukaryota.
DR HOGENOM; CLU_044365_3_0_1; -.
DR InParanoid; F4JJL3; -.
DR OMA; ITDEWST; -.
DR OrthoDB; 1114699at2759; -.
DR BRENDA; 3.1.30.2; 399.
DR PRO; PR:F4JJL3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JJL3; baseline and differential.
DR Genevisible; F4JJL3; AT.
DR GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0043765; F:T/G mismatch-specific endonuclease activity; IDA:TAIR.
DR GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:UniProtKB.
DR CDD; cd11010; S1-P1_nuclease; 1.
DR Gene3D; 1.10.575.10; -; 1.
DR InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR InterPro; IPR003154; S1/P1nuclease.
DR PANTHER; PTHR33146; PTHR33146; 1.
DR Pfam; PF02265; S1-P1_nuclease; 1.
DR SUPFAM; SSF48537; SSF48537; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Metal-binding;
KW Nuclease; Reference proteome; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..280
FT /note="Endonuclease 5"
FT /id="PRO_0000417623"
FT PROPEP 281..296
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:23620482"
FT /id="PRO_0000445544"
FT REGION 144..193
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 21..26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 21
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 26
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 66..72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 66
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 81..84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 81
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 91..96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 148
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 148
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 178
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 182
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT SITE 66
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P24021"
FT SITE 69
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 30..62
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT DISULFID 90..243
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT DISULFID 98..108
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT DISULFID 223..230
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT MUTAGEN 281..296
FT /note="Missing: Loss of activity."
FT /evidence="ECO:0000269|PubMed:23620482"
FT CONFLICT 105
FT /note="K -> R (in Ref. 3; AAM65542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 33610 MW; 048B564AB53BE180 CRC64;
MRLWIVSVLV LTHLVHGALC WGKDGHYTVC KLAEGFFEDD TIAAVKKLLP ESVDGGGLAD
FCSWPDEIKK LSQWQWTSTL HYVNTPEYRC NYEYCRDCHD THKHKDWCVT GAIFNYTNQL
MSASENSQNI VHYNLTEALL FLSHYMGDVH QPLHTGFLGD LGGNTIIVNW YHNKSNLHHV
WDNMIIDSAL ETYYNSSLPH MIQALQAKLK NGWSNDVPSW KSCHFHQKAC PNLYASESID
LACKYAYRNA TPGTTLGDEY FLSRLPVVEK RLAQGGIRLA ATLNRIFSAK PKLAGL
