REV1_MOUSE
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 03-AUG-2022, entry version 151.
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; 14.
DR DIP; DIP-41772N; -.
DR IntAct; Q920Q2; 5.
DR STRING; 10090.ENSMUSP00000027251; -.
DR iPTMnet; Q920Q2; -.
DR PhosphoSitePlus; Q920Q2; -.
DR EPD; Q920Q2; -.
DR PaxDb; Q920Q2; -.
DR PeptideAtlas; Q920Q2; -.
DR PRIDE; Q920Q2; -.
DR ProteomicsDB; 253224; -.
DR Antibodypedia; 32824; 171 antibodies from 29 providers.
DR DNASU; 56210; -.
DR Ensembl; ENSMUST00000027251; ENSMUSP00000027251; ENSMUSG00000026082.
DR GeneID; 56210; -.
DR KEGG; mmu:56210; -.
DR UCSC; uc007asp.1; mouse.
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; PVKHLGH; -.
DR OrthoDB; 299766at2759; -.
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 109 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 253 other tissues.
DR ExpressionAtlas; Q920Q2; baseline and differential.
DR Genevisible; Q920Q2; MM.
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 DisProt; DP02625; -.
DR Gene3D; 1.20.58.1280; -; 1.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
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; IPR025527; HUWE1/Rev1_UBM.
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 Pfam; PF14377; UBM; 2.
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 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
