GENL1_ARATH
ID GENL1_ARATH Reviewed; 599 AA.
AC Q9LPD2; F4HU72;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Flap endonuclease GEN-like 1 {ECO:0000303|PubMed:25037209};
DE Short=AtGEN1 {ECO:0000303|PubMed:25037209};
DE Short=XPG-like endonuclease 1 {ECO:0000303|PubMed:25037209};
DE EC=3.1.-.-;
GN Name=GEN1 {ECO:0000303|PubMed:25037209};
GN OrderedLocusNames=At1g01880 {ECO:0000312|Araport:AT1G01880};
GN ORFNames=F22M8.2 {ECO:0000312|EMBL:AAF76467.1};
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=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 FUNCTION, AND MUTAGENESIS OF ASP-75.
RC STRAIN=cv. Columbia;
RX PubMed=25037209; DOI=10.1104/pp.114.237834;
RA Bauknecht M., Kobbe D.;
RT "AtGEN1 and AtSEND1, two paralogs in Arabidopsis, possess holliday junction
RT resolvase activity.";
RL Plant Physiol. 166:202-216(2014).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26704385; DOI=10.1105/tpc.15.00898;
RA Olivier M., Da Ines O., Amiard S., Serra H., Goubely C., White C.I.,
RA Gallego M.E.;
RT "The structure-specific endonucleases MUS81 and SEND1 are essential for
RT telomere stability in Arabidopsis.";
RL Plant Cell 28:74-86(2016).
CC -!- FUNCTION: Endonuclease which cleaves flap structures at the junction
CC between single-stranded DNA and double-stranded DNA with a specific
CC cleavage site in the 5' overhang strand exactly one nucleotide 3' of
CC the branch point (PubMed:25037209). Structure- and sequence-specific
CC nuclease that resolves holliday junctions (HJs) by symmetrically
CC oriented incisions in two opposing strands near the junction point,
CC thus leading to ligatable products; HJs are physical links between
CC homologous DNA molecules that arise as central intermediary structures
CC during homologous recombination and repair in meiotic and somatic cells
CC (PubMed:25037209). Structure-specific nuclease with 5'-flap
CC endonuclease activity, preferentially cleaving static flaps 5' overhang
CC strand exactly one nucleotide in the 3' direction of the branch point
CC (PubMed:25037209). Also able to cleave double-stranded flap strand 1
CC exactly at the branch point (PubMed:25037209).
CC {ECO:0000269|PubMed:25037209}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q17RS7};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000250|UniProtKB:Q17RS7};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q17RS7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LPD2-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Normal sensitivity to DNA damaging agents
CC (PubMed:26704385). Mild UV sensitivity in the gen1 send1 double mutant
CC (PubMed:26704385). {ECO:0000269|PubMed:26704385}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. GEN subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76467.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC020622; AAF76467.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27345.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58562.1; -; Genomic_DNA.
DR PIR; F86150; F86150.
DR RefSeq; NP_001320987.1; NM_001331312.1. [Q9LPD2-1]
DR RefSeq; NP_171691.2; NM_100069.3. [Q9LPD2-1]
DR AlphaFoldDB; Q9LPD2; -.
DR SMR; Q9LPD2; -.
DR BioGRID; 22614; 3.
DR IntAct; Q9LPD2; 3.
DR STRING; 3702.AT1G01880.1; -.
DR PaxDb; Q9LPD2; -.
DR PRIDE; Q9LPD2; -.
DR EnsemblPlants; AT1G01880.1; AT1G01880.1; AT1G01880. [Q9LPD2-1]
DR EnsemblPlants; AT1G01880.3; AT1G01880.3; AT1G01880. [Q9LPD2-1]
DR GeneID; 837373; -.
DR Gramene; AT1G01880.1; AT1G01880.1; AT1G01880. [Q9LPD2-1]
DR Gramene; AT1G01880.3; AT1G01880.3; AT1G01880. [Q9LPD2-1]
DR KEGG; ath:AT1G01880; -.
DR Araport; AT1G01880; -.
DR TAIR; locus:2025447; AT1G01880.
DR eggNOG; KOG2519; Eukaryota.
DR HOGENOM; CLU_013777_1_0_1; -.
DR InParanoid; Q9LPD2; -.
DR OMA; MCAYLNE; -.
DR PRO; PR:Q9LPD2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPD2; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IDA:UniProtKB.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IBA:GO_Central.
DR GO; GO:0009650; P:UV protection; IGI:UniProtKB.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081; PTHR11081; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA repair; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..599
FT /note="Flap endonuclease GEN-like 1"
FT /id="PRO_0000315622"
FT REGION 1..96
FT /note="N-domain"
FT REGION 2..95
FT /note="XPG-N domain"
FT /evidence="ECO:0000250|UniProtKB:Q17RS7"
FT REGION 128..217
FT /note="I-domain"
FT REGION 128..213
FT /note="XPG-I domain"
FT /evidence="ECO:0000250|UniProtKB:Q17RS7"
FT REGION 213..407
FT /note="5'-3' exonuclease domain"
FT /evidence="ECO:0000250|UniProtKB:Q17RS7"
FT REGION 522..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39748"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17RS7"
FT BINDING 140
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17RS7"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58839"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ84"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ84"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58839"
FT MUTAGEN 75
FT /note="D->A: Impaired nuclease activity."
FT /evidence="ECO:0000269|PubMed:25037209"
SQ SEQUENCE 599 AA; 67193 MW; 69086D368EED30A7 CRC64;
MGVGGNFWDL LRPYAQQQGF DFLRNKRVAV DLSFWIVQHE TAVKGFVLKP HLRLTFFRTI
NLFSKFGAYP VFVVDGTPSP LKSQARISRF FRSSGIDTCN LPVIKDGVSV ERNKLFSEWV
RECVELLELL GIPVLKANGE AEALCAQLNS QGFVDACITP DSDAFLFGAM CVIKDIKPNS
REPFECYHMS HIESGLGLKR KHLIAISLLV GNDYDSGGVL GIGVDKALRI VREFSEDQVL
ERLQDIGNGL QPAVPGGIKS GDDGEEFRSE MKKRSPHCSR CGHLGSKRTH FKSSCEHCGC
DSGCIKKPLG FRCECSFCSK DRDLREQKKT NDWWIKVCDK IALAPEFPNR KIIELYLSDG
LMTGDGSSMS WGTPDTGMLV DLMVFKLHWD PSYVRKMLLP MLSTIYLREK ARNNTGYALL
CDQYEFHSIK CIKTRYGHQS FVIRWRKPKS TSGYSHSHSE PEESIVVLEE EEESVDPLDG
LNEPQVQNDN GDCFLLTDEC IGLVQSAFPD ETEHFLHEKK LRESKKKNVS EEETATPRAT
TMGVQRSITD FYRSAKKAAA GQSIETGGSS KASAEKKRQA TSTSSSNLTK SVRRRLLFG
