ID   REV1_MOUSE              Reviewed;        1249 AA.
AC   Q920Q2; Q9QXV2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=DNA repair protein REV1;
DE            EC=2.7.7.-;
DE   AltName: Full=Rev1-like terminal deoxycytidyl transferase;
GN   Name=Rev1; Synonyms=Rev1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC   STRAIN=C3H/He; TISSUE=Liver;
RX   PubMed=11711549; DOI=10.1074/jbc.m110149200;
RA   Masuda Y., Takahashi M., Fukuda S., Sumii M., Kamiya K.;
RT   "Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1
RT   protein.";
RL   J. Biol. Chem. 277:3040-3046(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Poltoratsky V.P., Scharff M.D.;
RT   "Mus musculus REV1 protein (Rev1) mRNA, complete cds.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH MAD2L2; POLH; POLI AND POLK.
RX   PubMed=14657033; DOI=10.1093/emboj/cdg626;
RA   Guo C., Fischhaber P.L., Luk-Paszyc M.J., Masuda Y., Zhou J., Kamiya K.,
RA   Kisker C., Friedberg E.C.;
RT   "Mouse Rev1 protein interacts with multiple DNA polymerases involved in
RT   translesion DNA synthesis.";
RL   EMBO J. 22:6621-6630(2003).
CC   -!- FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a
CC       dCMP residue from dCTP to the 3'-end of a DNA primer in a template-
CC       dependent reaction. May assist in the first step in the bypass of
CC       abasic lesions by the insertion of a nucleotide opposite the lesion.
CC       Required for normal induction of mutations by physical and chemical
CC       agents. {ECO:0000269|PubMed:11711549}.
CC   -!- SUBUNIT: Interacts with FAAP20 (By similarity). Monomer. Interacts with
CC       the DNA polymerase zeta which is composed of REV3L and MAD2L2; the
CC       interaction with MAD2L2 is direct and requires that REV3L is in its
CC       closed conformation. Interacts with POLH, POLI and POLK. {ECO:0000250,
CC       ECO:0000269|PubMed:11711549, ECO:0000269|PubMed:14657033}.
CC   -!- INTERACTION:
CC       Q920Q2; Q6NZ36-1: FAAP20; Xeno; NbExp=7; IntAct=EBI-2114764, EBI-15965017;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11711549}.
CC   -!- DOMAIN: The C-terminal domain is necessary for protein interactions.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR   EMBL; AB057418; BAB64933.1; -; mRNA.
DR   EMBL; AF179302; AAF23323.1; -; mRNA.
DR   EMBL; BC058093; AAH58093.1; -; mRNA.
DR   CCDS; CCDS14899.1; -.
DR   RefSeq; NP_062516.2; NM_019570.3.
DR   RefSeq; XP_006496216.1; XM_006496153.3.
DR   RefSeq; XP_006496221.1; XM_006496158.2.
DR   PDB; 2LSG; NMR; -; A=1150-1249.
DR   PDB; 2LSJ; NMR; -; A=1135-1249.
DR   PDB; 4FJO; X-ray; 2.72 A; A=1153-1249.
DR   PDB; 6C59; X-ray; 2.03 A; A=1150-1249.
DR   PDB; 6C8C; X-ray; 1.50 A; A/B=1150-1249.
DR   PDBsum; 2LSG; -.
DR   PDBsum; 2LSJ; -.
DR   PDBsum; 4FJO; -.
DR   PDBsum; 6C59; -.
DR   PDBsum; 6C8C; -.
DR   AlphaFoldDB; Q920Q2; -.
DR   BMRB; Q920Q2; -.
DR   SMR; Q920Q2; -.
DR   BioGRID; 207845; 15.
DR   DIP; DIP-41772N; -.
DR   IntAct; Q920Q2; 5.
DR   STRING; 10090.ENSMUSP00000027251; -.
DR   iPTMnet; Q920Q2; -.
DR   PhosphoSitePlus; Q920Q2; -.
DR   EPD; Q920Q2; -.
DR   PaxDb; 10090-ENSMUSP00000027251; -.
DR   PeptideAtlas; Q920Q2; -.
DR   ProteomicsDB; 253224; -.
DR   Antibodypedia; 32824; 185 antibodies from 29 providers.
DR   DNASU; 56210; -.
DR   Ensembl; ENSMUST00000027251.12; ENSMUSP00000027251.7; ENSMUSG00000026082.12.
DR   GeneID; 56210; -.
DR   KEGG; mmu:56210; -.
DR   UCSC; uc007asp.1; mouse.
DR   AGR; MGI:1929074; -.
DR   CTD; 51455; -.
DR   MGI; MGI:1929074; Rev1.
DR   VEuPathDB; HostDB:ENSMUSG00000026082; -.
DR   eggNOG; KOG2093; Eukaryota.
DR   GeneTree; ENSGT00940000156374; -.
DR   HOGENOM; CLU_003901_0_1_1; -.
DR   InParanoid; Q920Q2; -.
DR   OMA; IKNGMWM; -.
DR   OrthoDB; 169741at2759; -.
DR   PhylomeDB; Q920Q2; -.
DR   TreeFam; TF314488; -.
DR   Reactome; R-MMU-110312; Translesion synthesis by REV1.
DR   Reactome; R-MMU-5655862; Translesion synthesis by POLK.
DR   Reactome; R-MMU-5656121; Translesion synthesis by POLI.
DR   Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR   BioGRID-ORCS; 56210; 4 hits in 114 CRISPR screens.
DR   ChiTaRS; Rev1; mouse.
DR   PRO; PR:Q920Q2; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q920Q2; Protein.
DR   Bgee; ENSMUSG00000026082; Expressed in dorsal pancreas and 256 other cell types or tissues.
DR   ExpressionAtlas; Q920Q2; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0017125; F:deoxycytidyl transferase activity; IDA:MGI.
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:0070987; P:error-free translesion synthesis; IBA:GO_Central.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IDA:MGI.
DR   GO; GO:0009411; P:response to UV; ISO:MGI.
DR   CDD; cd17719; BRCT_Rev1; 1.
DR   CDD; cd01701; PolY_Rev1; 1.
DR   CDD; cd12145; Rev1_C; 1.
DR   CDD; cd19318; Rev1_UBM2; 2.
DR   DisProt; DP02625; -.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.40.1170.60; -; 1.
DR   Gene3D; 6.10.250.1490; -; 1.
DR   Gene3D; 6.10.250.1630; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
DR   Gene3D; 1.20.58.1280; DNA repair protein Rev1, C-terminal domain; 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; IPR025527; HUWE1/Rev1_UBM.
DR   InterPro; IPR012112; REV1.
DR   InterPro; IPR031991; Rev1_C.
DR   InterPro; IPR038401; Rev1_C_sf.
DR   InterPro; IPR047346; Rev1_UBM1/2.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   PANTHER; PTHR45990; DNA REPAIR PROTEIN REV1; 1.
DR   PANTHER; PTHR45990:SF1; DNA REPAIR PROTEIN REV1; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF00817; IMS; 2.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF21704; POLH-Rev1_HhH; 1.
DR   Pfam; PF16727; REV1_C; 1.
DR   Pfam; PF14377; UBM; 2.
DR   PIRSF; PIRSF036573; REV1; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50173; UMUC; 1.
DR   Genevisible; Q920Q2; MM.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA repair; DNA synthesis; DNA-binding;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1249
FT                   /note="DNA repair protein REV1"
FT                   /id="PRO_0000173993"
FT   DOMAIN          44..131
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          417..651
FT                   /note="UmuC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   REGION          253..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..360
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          651..654
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          707..715
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          1035..1109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1150..1249
FT                   /note="Protein interaction domain; mediates interaction
FT                   with DNA polymerase zeta"
FT   MOTIF           1072..1078
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        256..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1060
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         355
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         421..425
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         421
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         421
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         508..514
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         520
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         568
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         568
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         569
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   SITE            768
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            781
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        438
FT                   /note="K -> T (in Ref. 2; AAF23323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        555
FT                   /note="L -> W (in Ref. 2; AAF23323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        638
FT                   /note="F -> S (in Ref. 2; AAF23323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        661
FT                   /note="L -> S (in Ref. 2; AAF23323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        684
FT                   /note="K -> R (in Ref. 2; AAF23323)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1163..1176
FT                   /evidence="ECO:0007829|PDB:6C8C"
FT   HELIX           1182..1197
FT                   /evidence="ECO:0007829|PDB:6C8C"
FT   HELIX           1201..1216
FT                   /evidence="ECO:0007829|PDB:6C8C"
FT   HELIX           1221..1241
FT                   /evidence="ECO:0007829|PDB:6C8C"
FT   TURN            1242..1245
FT                   /evidence="ECO:0007829|PDB:6C8C"
FT   STRAND          1246..1248
FT                   /evidence="ECO:0007829|PDB:6C8C"
SQ   SEQUENCE   1249 AA;  137341 MW;  F82E0B6171AA3F75 CRC64;
     MRRGGWRKRT ENDGWEKWGG YMAAKVQKLE EQFRTDAANQ KDGTASAIFS GVAIYVNGYT
     DPSAEELRNL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI KELKGEKVIR PEWIVESIKA
     GRLLSSAPYQ LYTKPSAAQK SLNFNPVCKP EDPGPGPSNR AKQLNNRVNH IIKKIETESE
     VKANGLSSWN EDGVNDDFSF EDLEHTFPGR KQNGVMHPRD TAVIFNGHTH SSNGALKTQD
     CLVPVGNSVA SRLSLDSTQE EKRAEKSNAD FRDCTVQHLQ HSTRSADALR SPHRTNSLSP
     SLHSNTKING AHHSTVQGPS STKSTSVLTL SKVAPSVPSK PSDCNFISDF YSRSRLHHIS
     TWKCELTEFV NTLQRQSSGI FPGREKLKKV KTGRSSLVVT DTGTMSVLSS PRHQSCVMHV
     DMDCFFVSVG IRNRPDLKGK PVAVTSNRGT GTAPLRPGAN PQLEWQYYQN RALRGKAADI
     PDSSVWENQD STQTNGIDSV LSKAEIASCS YEARQVGIKN GMFFGYAKQL CPNLQAVPYD
     FHACREVAQA MYETLASYTH SIEAVSCDEA LIDVTDILAE TKLSPEEFAA ALRIEIKDKT
     KCAASVGIGS NILLARMATK KAKPDGQYHL QPDEVDDFIR GQLVTNLPGV GRSMESKLAS
     LGIKTCGDLQ CLTMAKLQKE FGPKTGQMLY RFCRGLDDRP VRTEKERKSV SAEINYGIRF
     TQPKEAEAFL LSLSEEIQRR LEAAGMKGKR LTLKIMVRKP GAPIETAKFG GHGICDNIAR
     TVTLDQATDS AKIIGKATLN MFHTMKLNIS DMRGVGIQVN QLVPANSNLS TCSSRPSAQS
     SLFSGRPHSV RDLFQLQKAK KPTEEEHKEV FLAAVDLEVS STSRACGLLS PLSAHLAASV
     SPDTNSGECS RKWNGLHSPV SGQSRLNLSI EVPSPSQIDQ SVLEALPLDL REQIEQVCAA
     QQGEPRGKKK EPVNGCSSGV LPHPVGTVLL QIPEPQEPCN SDSKISVIAL PAFSQVDPDV
     FAALPAELQK ELKAAYDQRQ RQGEDTTHQQ PTSTSVPKNP LLQLKPPAMK DKRNKRKNLI
     GSPRKSPLKN KLLSSPAKTL PGAYGSPQKL MDGFLQHEGM ASERPLEEVS ASTPGAQDLS
     SLLPGQSSCF RPAAPNLAGA VEFSDVKTLL KEWITTISDP MEEDILQVVR YCTDLIEEKD
     LEKLDLVIKY MKRLMQQSVE SVWNMAFDFI LDNVQVVLQQ TYGSTLKVT
//