ENDO1_ARATH
ID ENDO1_ARATH Reviewed; 305 AA.
AC Q9SXA6; Q9ZR89;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Endonuclease 1 {ECO:0000303|PubMed:17651368};
DE Short=AtENDO1 {ECO:0000303|PubMed:17651368};
DE EC=3.1.30.1 {ECO:0000269|PubMed:23620482};
DE AltName: Full=Bifunctional nuclease I {ECO:0000303|PubMed:10631260};
DE Short=AtBFN1 {ECO:0000303|PubMed:10631260};
DE AltName: Full=Deoxyribonuclease ENDO1 {ECO:0000303|PubMed:17651368};
DE AltName: Full=Single-stranded-nucleate endonuclease ENDO1 {ECO:0000303|PubMed:17651368};
DE Flags: Precursor;
GN Name=ENDO1 {ECO:0000303|PubMed:17651368};
GN Synonyms=BFN1 {ECO:0000303|PubMed:10631260};
GN OrderedLocusNames=At1g11190 {ECO:0000312|Araport:AT1G11190};
GN ORFNames=T28P6.14 {ECO:0000312|EMBL:AAD49996.1};
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10631260; DOI=10.1104/pp.122.1.169;
RA Perez-Amador M.A., Abler M.L., De Rocher E.J., Thompson D.M., van Hoof A.,
RA LeBrasseur N.D., Lers A., Green P.J.;
RT "Identification of BFN1, a bifunctional nuclease induced during leaf and
RT stem senescence in Arabidopsis.";
RL Plant Physiol. 122:169-179(2000).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, BIOTECHNOLOGY, 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 [7]
RP BIOTECHNOLOGY.
RX PubMed=18433472; DOI=10.1186/1471-2199-9-42;
RA Triques K., Piednoir E., Dalmais M., Schmidt J., Le Signor C., Sharkey M.,
RA Caboche M., Sturbois B., Bendahmane A.;
RT "Mutation detection using ENDO1: application to disease diagnostics in
RT humans and TILLING and Eco-TILLING in plants.";
RL BMC Mol. Biol. 9:42-42(2008).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=18603613; DOI=10.1093/jxb/ern176;
RA Farage-Barhom S., Burd S., Sonego L., Perl-Treves R., Lers A.;
RT "Expression analysis of the BFN1 nuclease gene promoter during senescence,
RT abscission, and programmed cell death-related processes.";
RL J. Exp. Bot. 59:3247-3258(2008).
RN [9]
RP INDUCTION BY NAC92/ORE1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=23340744; DOI=10.1093/mp/sst012;
RA Matallana-Ramirez L.P., Rauf M., Farage-Barhom S., Dortay H., Xue G.-P.,
RA Droege-Laser W., Lers A., Balazadeh S., Mueller-Roeber B.;
RT "NAC transcription factor ORE1 and senescence-induced BIFUNCTIONAL
RT NUCLEASE1 (BFN1) constitute a regulatory cascade in Arabidopsis.";
RL Mol. Plant 6:1438-1452(2013).
RN [10]
RP FUNCTION, MUTAGENESIS OF 287-MET--THR-305, 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: Endonuclease that can use RNA, single-stranded and double-
CC stranded DNA as substrates (PubMed:23620482). Hydrolyzes single-
CC stranded DNA and RNA without apparent specificity for bases during
CC senescence. Endonuclease that recognizes and cleaves all types of
CC mismatches with high efficiency, including heteroduplex double-stranded
CC DNA. Maybe involved in programmed cell death (PCD) and senescence.
CC {ECO:0000269|PubMed:10631260, ECO:0000269|PubMed:17651368,
CC ECO:0000269|PubMed:18603613, 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:23620482};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23620482};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:23620482};
CC Note=Binds 3 divalent metal cations (PubMed:23620482). Uses Ca(2+) ions
CC with ssDNA as substrate (PubMed:23620482). Can also use Mn(2+) with
CC lower efficiency with ssDNA and dsDNA as substrates (PubMed:23620482).
CC {ECO:0000269|PubMed:23620482};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8 with RNA, ssDNA and dsDNA as substrates.
CC {ECO:0000269|PubMed:23620482};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers and during leaf and
CC stem senescence, and, to a lower extent, detectable at low levels in
CC roots, leaves, and stems. Particularly expressed in senescing tissues
CC in a NAC92/ORE1-dependent manner. {ECO:0000269|PubMed:10631260,
CC ECO:0000269|PubMed:18603613, ECO:0000269|PubMed:23340744}.
CC -!- DEVELOPMENTAL STAGE: Present in the margins and tips of the oldest
CC leaves, senescent leaves, differentiating xylem and at the abscission
CC zone of flowers. In flowers, expressed in developing anthers and seeds.
CC Accumulates in stigma, mature anthers, sepals, and petals of
CC older/fully opened flowers. Also present in floral organs after
CC fertilization. In mature siliques, observed in abscission zones and in
CC the distal portion of the valve margins. {ECO:0000269|PubMed:18603613,
CC ECO:0000269|PubMed:23340744}.
CC -!- INDUCTION: Directly induced by NAC92 during senescence onset.
CC {ECO:0000269|PubMed:23340744}.
CC -!- BIOTECHNOLOGY: ENDO1 is used to detect mutations generated by ethyl
CC methan sulfonate (EMS) to produce a TILLING (targeting-induced local
CC lesions in genomes) platform (PubMed:17651368, PubMed:18433472).
CC {ECO:0000269|PubMed:17651368, ECO:0000269|PubMed:18433472}.
CC -!- SIMILARITY: Belongs to the nuclease type I family. {ECO:0000305}.
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DR EMBL; U90264; AAD00693.1; -; Genomic_DNA.
DR EMBL; AC007259; AAD49996.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28697.1; -; Genomic_DNA.
DR EMBL; AY040016; AAK64173.1; -; mRNA.
DR EMBL; AY079368; AAL85099.1; -; mRNA.
DR EMBL; AY088393; AAM65931.1; -; mRNA.
DR PIR; H86245; H86245.
DR RefSeq; NP_172585.1; NM_100991.2.
DR AlphaFoldDB; Q9SXA6; -.
DR SMR; Q9SXA6; -.
DR STRING; 3702.AT1G11190.1; -.
DR PaxDb; Q9SXA6; -.
DR PRIDE; Q9SXA6; -.
DR ProteomicsDB; 222714; -.
DR EnsemblPlants; AT1G11190.1; AT1G11190.1; AT1G11190.
DR GeneID; 837660; -.
DR Gramene; AT1G11190.1; AT1G11190.1; AT1G11190.
DR KEGG; ath:AT1G11190; -.
DR Araport; AT1G11190; -.
DR TAIR; locus:2202114; AT1G11190.
DR eggNOG; ENOG502QTPJ; Eukaryota.
DR HOGENOM; CLU_044365_3_0_1; -.
DR InParanoid; Q9SXA6; -.
DR OMA; DCHDTHG; -.
DR OrthoDB; 1114699at2759; -.
DR PhylomeDB; Q9SXA6; -.
DR BRENDA; 3.1.30.2; 399.
DR PRO; PR:Q9SXA6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SXA6; baseline and differential.
DR Genevisible; Q9SXA6; AT.
DR GO; GO:0008309; F:double-stranded DNA exodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IDA:TAIR.
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:0080187; P:floral organ senescence; IEP:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IEP:UniProtKB.
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 Calcium; Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Manganese;
KW Metal-binding; Nuclease; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..286
FT /note="Endonuclease 1"
FT /id="PRO_0000417619"
FT PROPEP 287..305
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:23620482"
FT /id="PRO_0000445540"
FT REGION 150..199
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 29..34
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 29
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 73..79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 73
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 88..91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 88
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 98..103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 160
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 184
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT BINDING 188
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT SITE 73
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P24021"
FT SITE 76
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P24289"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 38..69
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT DISULFID 97..249
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT DISULFID 105..115
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT DISULFID 230..236
FT /evidence="ECO:0000250|UniProtKB:Q9C9G4"
FT MUTAGEN 287..305
FT /note="Missing: Loss of activity."
FT /evidence="ECO:0000269|PubMed:23620482"
FT CONFLICT 292
FT /note="V -> D (in Ref. 1; AAD00693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 34885 MW; CE6542070A86CDA5 CRC64;
MASAFRSSTR LILVLGILIL CSVSSVRSWS KEGHILTCRI AQNLLEAGPA HVVENLLPDY
VKGDLSALCV WPDQIRHWYK YRWTSHLHYI DTPDQACSYE YSRDCHDQHG LKDMCVDGAI
QNFTSQLQHY GEGTSDRRYN MTEALLFLSH FMGDIHQPMH VGFTSDEGGN TIDLRWYKHK
SNLHHVWDRE IILTALKENY DKNLDLLQED LEKNITNGLW HDDLSSWTEC NDLIACPHKY
ASESIKLACK WGYKGVKSGE TLSEEYFNTR LPIVMKRIVQ GGVRLAMILN RVFSDDHAIA
GVAAT
