REV1_DROME
ID REV1_DROME Reviewed; 995 AA.
AC Q9W0P2; A9UNE7; Q8T9I8;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DNA repair protein Rev1 {ECO:0000255|PIRNR:PIRNR036573};
DE EC=2.7.7.- {ECO:0000255|PIRNR:PIRNR036573};
DE AltName: Full=Reversionless protein 1 {ECO:0000303|PubMed:11297519};
GN Name=Rev1 {ECO:0000303|PubMed:11297519, ECO:0000312|FlyBase:FBgn0035150};
GN ORFNames=CG12189 {ECO:0000312|FlyBase:FBgn0035150};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:BAB15801.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11297519; DOI=10.1074/jbc.m009822200;
RA Ishikawa T., Uematsu N., Mizukoshi T., Iwai S., Iwasaki H., Masutani C.,
RA Hanaoka F., Ueda R., Ohmori H., Todo T.;
RT "Mutagenic and nonmutagenic bypass of DNA lesions by Drosophila DNA
RT polymerases dpoleta and dpoliota.";
RL J. Biol. Chem. 276:15155-15163(2001).
RN [2] {ECO:0000312|Proteomes:UP000000803}
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 [3] {ECO:0000312|Proteomes:UP000000803}
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 [4] {ECO:0000312|EMBL:ABY21724.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABY21724.1};
RC TISSUE=Head {ECO:0000312|EMBL:ABY21724.1};
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAL39416.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 659-995.
RC STRAIN=Berkeley; TISSUE=Ovary;
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 [6] {ECO:0000305}
RP INTERACTION WITH POLH AND POLI, AND REGION.
RX PubMed=18242152; DOI=10.1016/j.dnarep.2007.11.016;
RA Kosarek J.N., Woodruff R.V., Rivera-Begeman A., Guo C., D'Souza S.,
RA Koonin E.V., Walker G.C., Friedberg E.C.;
RT "Comparative analysis of in vivo interactions between Rev1 protein and
RT other Y-family DNA polymerases in animals and yeasts.";
RL DNA Repair 7:439-451(2008).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22532806; DOI=10.1371/journal.pgen.1002659;
RA Kane D.P., Shusterman M., Rong Y., McVey M.;
RT "Competition between replicative and translesion polymerases during
RT homologous recombination repair in Drosophila.";
RL PLoS Genet. 8:E1002659-E1002659(2012).
CC -!- FUNCTION: Deoxycytidyl transferase involved in DNA repair
CC (PubMed:22532806). Transfers a dCMP residue from dCTP to the 3'-end of
CC a DNA primer in a template-dependent reaction. May assist in the first
CC step in the bypass of abasic lesions by the insertion of a nucleotide
CC opposite the lesion. Required for normal induction of mutations by
CC physical and chemical agents (By similarity). During homologous
CC recombination (HR) repair of DNA double-strand breaks (DSBs) regulates
CC the extent of repair synthesis (PubMed:22532806). Possibly recruits the
CC DNA polymerase zeta complex or another translesion polymerase to early
CC DSB repair intermediates to initiate repair synthesis, while also
CC blocking the access of more processive polymerases preventing them from
CC acting during the initial stages of HR repair (PubMed:22532806).
CC {ECO:0000250|UniProtKB:P12689, ECO:0000269|PubMed:22532806}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 magnesium ions. {ECO:0000250|UniProtKB:P12689};
CC -!- SUBUNIT: Interacts (via C-terminus) with PolH/DNApol-eta (via C-
CC terminal regions). Interacts (via C-terminus) with PolI.
CC {ECO:0000269|PubMed:18242152}.
CC -!- INTERACTION:
CC Q9W0P2; Q9VNX1: DNApol-eta; NbExp=2; IntAct=EBI-95229, EBI-115702;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PIRNR:PIRNR036573}.
CC -!- DISRUPTION PHENOTYPE: Highly sensitive to ionizing radiation due to
CC defects in homologous recombination (HR) repair. The percentage of full
CC HR repair is normal but the length of the repair synthesis tracts is
CC increased. {ECO:0000269|PubMed:22532806}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABY21724.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB049435; BAB15801.1; -; mRNA.
DR EMBL; AE014296; AAF47401.1; -; Genomic_DNA.
DR EMBL; BT031311; ABY21724.1; ALT_INIT; mRNA.
DR EMBL; AY069271; AAL39416.1; -; mRNA.
DR RefSeq; NP_612047.1; NM_138203.3.
DR AlphaFoldDB; Q9W0P2; -.
DR SMR; Q9W0P2; -.
DR IntAct; Q9W0P2; 8.
DR STRING; 7227.FBpp0072456; -.
DR PaxDb; Q9W0P2; -.
DR EnsemblMetazoa; FBtr0072557; FBpp0072456; FBgn0035150.
DR GeneID; 38079; -.
DR KEGG; dme:Dmel_CG12189; -.
DR UCSC; CG12189-RA; d. melanogaster.
DR CTD; 51455; -.
DR FlyBase; FBgn0035150; Rev1.
DR VEuPathDB; VectorBase:FBgn0035150; -.
DR eggNOG; KOG2093; Eukaryota.
DR GeneTree; ENSGT00940000156374; -.
DR HOGENOM; CLU_003901_0_2_1; -.
DR InParanoid; Q9W0P2; -.
DR OMA; CDEMFVE; -.
DR OrthoDB; 299766at2759; -.
DR PhylomeDB; Q9W0P2; -.
DR Reactome; R-DME-110312; Translesion synthesis by REV1.
DR Reactome; R-DME-5655862; Translesion synthesis by POLK.
DR Reactome; R-DME-5656121; Translesion synthesis by POLI.
DR SignaLink; Q9W0P2; -.
DR BioGRID-ORCS; 38079; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 38079; -.
DR PRO; PR:Q9W0P2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035150; Expressed in egg chamber and 23 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005657; C:replication fork; ISS:FlyBase.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0017125; F:deoxycytidyl transferase activity; ISS:FlyBase.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043150; P:DNA synthesis involved in double-strand break repair via homologous recombination; IMP:FlyBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
DR GO; GO:0070987; P:error-free translesion synthesis; IBA:GO_Central.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:FlyBase.
DR GO; GO:0019985; P:translesion synthesis; ISS:FlyBase.
DR Gene3D; 1.20.58.1280; -; 1.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR012112; REV1.
DR InterPro; IPR031991; Rev1_C.
DR InterPro; IPR038401; Rev1_C_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF16727; REV1_C; 1.
DR PIRSF; PIRSF036573; REV1; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA synthesis; DNA-binding; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..995
FT /note="DNA repair protein Rev1"
FT /id="PRO_0000448743"
FT DOMAIN 35..121
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 275..505
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT REGION 135..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..868
FT /note="Interaction with PolI"
FT /evidence="ECO:0000269|PubMed:18242152"
FT REGION 878..995
FT /note="Interaction with PolH/DNApol-eta"
FT /evidence="ECO:0000269|PubMed:18242152"
FT COMPBIAS 141..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT BINDING 361..367
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:P12689"
FT BINDING 373
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:P12689"
FT BINDING 421
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:P12689"
FT BINDING 421
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT SITE 284
FT /note="Substrate discrimination"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT CONFLICT 690
FT /note="E -> Q (in Ref. 5; AAL39416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 995 AA; 112414 MW; 8647D89E66ECB6B6 CRC64;
MTRDEDNGFS EWGGYFEAKK SKLEEQFAAA SDPFRKSDLF QGISIFVNGR TDPSADELKR
IMMVHGGTFH HYERSHTTYI IASVLPDVKV RNMNLSKFIS AKWVVDCLEK KKIVDYKPYL
LYTNQKTSQP MLIFGKPKDN GANESKSDVE PPKDKAEVEV DSTKDETQME LGGILKNLQQ
AVATSPEKEA SASESKITNL STTSNNSTTA RTAADPNFLS EFYKNSRLHH IATLGAGFKQ
YVCRLRQKHG TQGFPKRETL KSLANSHHNC LERYVMHIDM DCFFVSVGLR TRPELRGLPI
AVTHSKGGNA ATDVPVHPQA DRKAELELFA QRFEHHFHDG DKAEKVRSGF DKKMSLSEIA
SCSYEAREKG IRNGMFVGQA LKLCPELKTI PYDFEGYKEV AFTLYDTVAQ YTLNIEAVSC
DEMFVELTDL AHELNVDVMA FVSHLRQEVY SKTGCPCSAG VAGNKLLARM ATKEAKPNGQ
FLLDSSNDIL AYMAPMSLDL LPGVGSSISH KLKQAGLNNC GDVQNTTLEK MEKVLGKKLG
QNLFQNCRGI DDRPLAYEQI RKTVSAEMNF GIRFTNSVEC EQFLCQLSEE VTKRLVEIRR
KARSINLKIM VRAAEAPVET SKYMGHGVCD IINKSSLIKY ATDDVNVITT VVLDLMKDAD
IPPDELRGLG IHLTRLEDAN EVRKENNIKE MFGKMSEMRK DKPIPQGAVG DKSIGDDKVN
KPLVFENKPK PREPRNVLSM LTAAAVSRKS VTEDRSQRGT SKPITRPLSL VPKLDEDVLA
QLPEDIRLEV IANREEHLCI AEYDGYRSPQ YPTLRSPPLL NPYVTTNVSP LKATDLKPST
SRAAVARLQK RKERKEQEHY IRSDQIVADY IDDLPDFVNP HILKLISHPV EMPELLMGDN
YKDLLNDWVS REEVPKPNDV DLILKQVSRM IKNDQLDHVC DVMKYWCRII NMKRSSSCCW
HVAYKHIEES IQNQMLTIEG YSLLFIEYIR CIKCS
