RRP1_DROME
ID RRP1_DROME Reviewed; 679 AA.
AC P27864; Q540Y1; Q9VQJ4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Recombination repair protein 1 {ECO:0000303|PubMed:1713691};
DE AltName: Full=DNA-(apurinic or apyrimidinic site) endonuclease {ECO:0000250|UniProtKB:P27695};
DE EC=3.1.11.2 {ECO:0000269|PubMed:16507570, ECO:0000269|PubMed:1713691, ECO:0000269|PubMed:8918793};
GN Name=Rrp1 {ECO:0000303|PubMed:1713691, ECO:0000312|FlyBase:FBgn0004584};
GN ORFNames=CG3178 {ECO:0000312|FlyBase:FBgn0004584};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Oregon-R;
RX PubMed=1713691; DOI=10.1073/pnas.88.15.6780;
RA Sander M., Lowenhaupt K., Rich A.;
RT "Drosophila Rrp1 protein: an apurinic endonuclease with homologous
RT recombination activities.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6780-6784(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=1653418; DOI=10.1093/nar/19.16.4523;
RA Sander M., Lowenhaupt K., Lane W.S., Rich A.;
RT "Cloning and characterization of Rrp1, the gene encoding Drosophila strand
RT transferase: carboxy-terminal homology to DNA repair endo/exonucleases.";
RL Nucleic Acids Res. 19:4523-4529(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RA Tsoi S.C.M., Huang S.M., Sander M.;
RT "Genomic organization of the Drosophila 23C genetic interval:
RT identification of 3 genes in the 10Kb region surrounding the RRP1 gene.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=8918793; DOI=10.1093/nar/24.20.3926;
RA Sander M., Benhaim D.;
RT "Drosophila Rrp1 3'-exonuclease: demonstration of DNA sequence dependence
RT and DNA strand specificity.";
RL Nucleic Acids Res. 24:3926-3933(1996).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH POLZ1 AND POLZ2,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=16507570; DOI=10.1074/jbc.m512959200;
RA Takeuchi R., Ruike T., Nakamura R., Shimanouchi K., Kanai Y., Abe Y.,
RA Ihara A., Sakaguchi K.;
RT "Drosophila DNA polymerase zeta interacts with recombination repair protein
RT 1, the Drosophila homologue of human abasic endonuclease 1.";
RL J. Biol. Chem. 281:11577-11585(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133; THR-140; SER-142 AND
RP SER-258, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Plays a role in the cellular response to oxidative stress by
CC promoting DNA repair mechanisms such as base excision repair and
CC possibly homologous recombination repair (PubMed:1713691,
CC PubMed:16507570). Functions as an apurinic/apyrimidinic (AP)
CC endodeoxyribonuclease in the DNA base excision repair (BER) pathway of
CC DNA lesions induced by oxidative and alkylating agents
CC (PubMed:16507570). Likely to initiate repair of AP sites in DNA by
CC catalyzing hydrolytic incision of the phosphodiester backbone
CC immediately adjacent to the damage, generating a single-strand break
CC with 5'-deoxyribose phosphate and 3'-hydroxyl ends (By similarity). Has
CC a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at
CC the 3' termini of nicked or gapped DNA molecules during short-patch BER
CC (PubMed:16507570). Has apurinic endonuclease and double-stranded DNA
CC 3'-exonuclease activities and carries out single-stranded DNA
CC renaturation in a Mg(2+)-dependent manner (PubMed:1713691,
CC PubMed:8918793). Activity is more efficient in purine-rich regions of
CC dsDNA than in pyrimidine-rich regions (PubMed:8918793).
CC {ECO:0000250|UniProtKB:P27695, ECO:0000269|PubMed:16507570,
CC ECO:0000269|PubMed:1713691, ECO:0000269|PubMed:8918793}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.2;
CC Evidence={ECO:0000269|PubMed:16507570, ECO:0000269|PubMed:1713691,
CC ECO:0000269|PubMed:8918793};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16507570, ECO:0000269|PubMed:1713691,
CC ECO:0000269|PubMed:8918793};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P27695};
CC Note=Probably binds two magnesium or manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P27695};
CC -!- SUBUNIT: Interacts with the zeta DNA polymerase complex; interacts (via
CC the N-terminus) with the accessory subunit PolZ2/Rev7 and also
CC interacts with the catalytic component PolZ1, however the interaction
CC with PolZ1 is likely via PolZ2. {ECO:0000269|PubMed:16507570}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00764,
CC ECO:0000269|PubMed:1713691, ECO:0000269|PubMed:8918793}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, with slightly
CC higher levels of expression in 0-12 hour embryos and adult females.
CC {ECO:0000269|PubMed:16507570}.
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC {ECO:0000305}.
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DR EMBL; M62472; AAA62769.1; -; mRNA.
DR EMBL; AF073994; AAC27621.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51175.1; -; Genomic_DNA.
DR EMBL; AY118605; AAM49974.1; -; mRNA.
DR PIR; S28366; S28366.
DR RefSeq; NP_476841.1; NM_057493.4.
DR AlphaFoldDB; P27864; -.
DR SMR; P27864; -.
DR BioGRID; 59720; 3.
DR IntAct; P27864; 2.
DR STRING; 7227.FBpp0288680; -.
DR iPTMnet; P27864; -.
DR PaxDb; P27864; -.
DR PRIDE; P27864; -.
DR DNASU; 33500; -.
DR EnsemblMetazoa; FBtr0077678; FBpp0077362; FBgn0004584.
DR GeneID; 33500; -.
DR KEGG; dme:Dmel_CG3178; -.
DR CTD; 8568; -.
DR FlyBase; FBgn0004584; Rrp1.
DR VEuPathDB; VectorBase:FBgn0004584; -.
DR eggNOG; KOG1294; Eukaryota.
DR eggNOG; KOG2992; Eukaryota.
DR GeneTree; ENSGT00530000063540; -.
DR InParanoid; P27864; -.
DR OMA; YLICTYV; -.
DR PhylomeDB; P27864; -.
DR Reactome; R-DME-110357; Displacement of DNA glycosylase by APEX1.
DR Reactome; R-DME-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
DR Reactome; R-DME-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DME-73933; Resolution of Abasic Sites (AP sites).
DR BioGRID-ORCS; 33500; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Rrp1; fly.
DR GenomeRNAi; 33500; -.
DR PRO; PR:P27864; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004584; Expressed in eye disc (Drosophila) and 51 other tissues.
DR ExpressionAtlas; P27864; baseline and differential.
DR Genevisible; P27864; DM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:FlyBase.
DR GO; GO:0052720; F:class II DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:FlyBase.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:FlyBase.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR004808; AP_endonuc_1.
DR InterPro; IPR020847; AP_endonuclease_F1_BS.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR PANTHER; PTHR22748; PTHR22748; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR TIGRFAMs; TIGR00633; xth; 1.
DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 1.
DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..679
FT /note="Recombination repair protein 1"
FT /id="PRO_0000200017"
FT REGION 1..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..679
FT /note="AP endonuclease"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 533
FT /evidence="ECO:0000250"
FT ACT_SITE 572
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 572
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 574
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 669
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT SITE 574
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 644
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 670
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 133
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 76
FT /note="A -> V (in Ref. 1; no nucleotide entry, 2; AAA62769
FT and 3; AAC27621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 679 AA; 74635 MW; A05CC54A5A2C52DD CRC64;
MPRVKAVKKQ AEALASEPTD PTPNANGNGV DENADSAAEE LKVPAKGKPR ARKATKTAVS
AENSEEVEPQ KAPTAAARGK KKQPKDTDEN GQMEVVAKPK GRAKKATAEA EPEPKVDLPA
GKATKPRAKK EPTPAPDEVT SSPPKGRAKA EKPTNAQAKG RKRKELPAEA NGGAEEAAEP
PKQRARKEAV PTLKEQAEPG TISKEKVQKA ETAAKRARGT KRLADSEIAA ALDEPEVDEV
PPKAASKRAK KGKMVEPSPE TVGDFQSVQE EVESPPKTAA APKKRAKKTT NGETAVELEP
KTKAKPTKQR AKKEGKEPAP GKKQKKSADK ENGVVEEEAK PSTETKPAKG RKKAPVKAED
VEDIEEAAEE SKPARGRKKA AAKAEEPDVD EESGSKTTKK AKKAETKTTV TLDKDAFALP
ADKEFNLKIC SWNVAGLRAW LKKDGLQLID LEEPDIFCLQ ETKCANDQLP EEVTRLPGYH
PYWLCMPGGY AGVAIYSKIM PIHVEYGIGN EEFDDVGRMI TAEYEKFYLI NVYVPNSGRK
LVNLEPRMRW EKLFQAYVKK LDALKPVVIC GDMNVSHMPI DLENPKNNTK NAGFTQEERD
KMTELLGLGF VDTFRHLYPD RKGAYTFWTY MANARARNVG WRLDYCLVSE RFVPKVVEHE
IRSQCLGSDH CPITIFFNI
