GENL1_ORYSJ
ID GENL1_ORYSJ Reviewed; 629 AA.
AC Q64MA3; B7E8Q8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Flap endonuclease GEN-like 1 {ECO:0000303|PubMed:15792960};
DE Short=OsGEN-L {ECO:0000303|PubMed:15792960};
DE Short=Protein OsGEN-like {ECO:0000303|PubMed:15792960};
DE EC=3.1.-.-;
DE AltName: Full=OsRAD {ECO:0000303|PubMed:15792960};
GN Name=RAD {ECO:0000303|PubMed:15792960};
GN Synonyms=GEN1 {ECO:0000303|PubMed:15792960};
GN OrderedLocusNames=Os09g0521900 {ECO:0000305}, LOC_Os09g35000 {ECO:0000305};
GN ORFNames=OsJ_016655 {ECO:0000312|EMBL:EAZ33172.1},
GN OsJ_17430 {ECO:0000312|EMBL:EEE62627.1},
GN OSJNOa273B05.7 {ECO:0000312|EMBL:BAD46702.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Toride; TISSUE=Root;
RX PubMed=15792960; DOI=10.1093/pcp/pci090;
RA Moritoh S., Miki D., Akiyama M., Kawahara M., Izawa T., Maki H.,
RA Shimamoto K.;
RT "RNAi-mediated silencing of OsGEN-L (OsGEN-like), a new member of the
RT RAD2/XPG nuclease family, causes male sterility by defect of microspore
RT development in rice.";
RL Plant Cell Physiol. 46:699-715(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH PCNA.
RX PubMed=22247560; DOI=10.1093/jb/mvr145;
RA Yang Y., Ishino S., Yamagami T., Kumamaru T., Satoh H., Ishino Y.;
RT "The OsGEN-L protein from Oryza sativa possesses Holliday junction
RT resolvase activity as well as 5'-flap endonuclease activity.";
RL J. Biochem. 151:317-327(2012).
CC -!- FUNCTION: Endonuclease which cleaves flap structures at the junction
CC between single-stranded DNA and double-stranded DNA. Possesses both
CC single-stranded and double-stranded DNA-binding activities. Involved in
CC early microspore development, but does not alter meiosis or tapetal
CC cells development (PubMed:15792960, PubMed:22247560). Possesses
CC Holliday junction (HJ) resolvase activity in vitro. Cleaves HJ at
CC symmetrically related sites of the branch point (PubMed:22247560).
CC {ECO:0000269|PubMed:15792960, ECO:0000269|PubMed:22247560}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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};
CC -!- SUBUNIT: Monomer. Interacts with PCNA. PCNA stimulates the nuclease
CC activity without altering cleavage specificity.
CC {ECO:0000269|PubMed:22247560}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15792960}.
CC -!- TISSUE SPECIFICITY: Highly expressed in anthers. Expressed in roots and
CC leaves. {ECO:0000269|PubMed:15792960}.
CC -!- DISRUPTION PHENOTYPE: Plants develop abnormal anthers with degraded
CC microspores, causing male sterility. {ECO:0000269|PubMed:15792960}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. GEN subfamily.
CC {ECO:0000305}.
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DR EMBL; AB158320; BAD93194.1; -; mRNA.
DR EMBL; AB194139; BAD93331.1; -; Genomic_DNA.
DR EMBL; AP006859; BAD46702.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT09023.1; -; Genomic_DNA.
DR EMBL; CM000142; EAZ33172.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE62627.1; -; Genomic_DNA.
DR EMBL; AK063534; BAG88755.1; -; mRNA.
DR RefSeq; XP_015610616.1; XM_015755130.1.
DR AlphaFoldDB; Q64MA3; -.
DR SMR; Q64MA3; -.
DR STRING; 4530.OS09T0521900-01; -.
DR PaxDb; Q64MA3; -.
DR PRIDE; Q64MA3; -.
DR EnsemblPlants; Os09t0521900-01; Os09t0521900-01; Os09g0521900.
DR GeneID; 4347617; -.
DR Gramene; Os09t0521900-01; Os09t0521900-01; Os09g0521900.
DR KEGG; osa:4347617; -.
DR eggNOG; KOG2519; Eukaryota.
DR HOGENOM; CLU_013777_1_0_1; -.
DR InParanoid; Q64MA3; -.
DR OMA; MCAYLNE; -.
DR OrthoDB; 1094524at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q64MA3; OS.
DR GO; GO:0005634; C:nucleus; IDA:Gramene.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:Gramene.
DR GO; GO:0048256; F:flap endonuclease activity; IDA:Gramene.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:Gramene.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IMP:Gramene.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
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; 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 DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..629
FT /note="Flap endonuclease GEN-like 1"
FT /id="PRO_0000315623"
FT REGION 1..87
FT /note="N-domain"
FT REGION 2..98
FT /note="XPG-N domain"
FT /evidence="ECO:0000250|UniProtKB:Q17RS7"
FT REGION 136..225
FT /note="I-domain"
FT /evidence="ECO:0000250|UniProtKB:Q9LPD2"
FT REGION 136..221
FT /note="XPG-I domain"
FT /evidence="ECO:0000250|UniProtKB:Q17RS7"
FT REGION 221..421
FT /note="5'-3' exonuclease domain"
FT /evidence="ECO:0000250|UniProtKB:Q17RS7"
FT REGION 594..617
FT /note="Disordered"
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 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17RS7"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58839"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58839"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ84"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ84"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58839"
SQ SEQUENCE 629 AA; 70757 MW; C4EF1A47536FEF62 CRC64;
MGVGGSFWDL LKPYARHEGA GYLRGRRVAV DLSFWVVSHS AAIRARSPHA RLPHLRTLFF
RTLSLFSKMG AFPVFVVDGQ PSPLKSQVRA ARFFRGSGMD LAALPSTEAE ASADALVQPR
NAKFTRYVED CVELLEYLGM PVLRAKGEGE ALCAQLNNQG HVDACITSDS DAFLFGAKTV
IKVLRSNCKE PFECYNMADI ESGLGLKRKQ MVAMALLVGS DHDLHGVPGF GPETALRFVQ
LFDEDNVLAK LYEIGKGVYP FIGVSAPNID DLPSPSTKSL PRARSPHCSH CGHPGNKKNH
IKDGCNFCLV DSLENCVEKP AGFICECPSC DKARDLKVQR RNENWQIKVC KRIAAETNFP
NEEIINLYLN DDNLDNENGV PLLTWNKPDM EILVDFLSFK QNWEPAYIRQ RMLPMLSTIY
LREMASSQSK SFLLYDQYKF HSIQRIKIRY GHPYYLVKWK RVTRSMISND PPSKQTELEG
KNDKVEVLDG DDEVVDEEEE EPTMISETTE LLDEPDVPQV LDDDKDCFLL TDEDIELVNA
AFPDEAQRFQ EEQRLKEAKS IARKSKLNVA GFETPKGPRP SGVQLSIKEF YRSKKGLSGD
SGKDGSRKSS DVDLSKNLPK SVRRRLLFD
