REV3_ARATH
ID REV3_ARATH Reviewed; 1890 AA.
AC Q766Z3; O64795; Q9CAG6;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=DNA polymerase zeta catalytic subunit;
DE EC=2.7.7.7;
DE AltName: Full=Protein reversionless 3-like;
DE Short=AtREV3;
GN Name=REV3; OrderedLocusNames=At1g67500; ORFNames=F12B7.5, T1F15.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12953110; DOI=10.1105/tpc.012369;
RA Sakamoto A., Vo L.T., Hase Y., Shikazono N., Matsunaga T., Tanaka A.;
RT "Disruption of the AtREV3 gene causes hypersensitivity to ultraviolet B
RT light and gamma-rays in Arabidopsis: implication of the presence of a
RT translesion synthesis mechanism in plants.";
RL Plant Cell 15:2042-2057(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION.
RX PubMed=15908599; DOI=10.1104/pp.105.060236;
RA Takahashi S., Sakamoto A., Sato S., Kato T., Tabata S., Tanaka A.;
RT "Roles of Arabidopsis AtREV1 and AtREV7 in translesion synthesis.";
RL Plant Physiol. 138:870-881(2005).
RN [5]
RP FUNCTION.
RX PubMed=21030509; DOI=10.1104/pp.110.166082;
RA Nakagawa M., Takahashi S., Tanaka A., Narumi I., Sakamoto A.N.;
RT "Role of AtPolzeta, AtRev1, and AtPoleta in UV light-induced mutagenesis in
RT Arabidopsis.";
RL Plant Physiol. 155:414-420(2011).
RN [6]
RP FUNCTION.
RX PubMed=21549648; DOI=10.1016/j.dnarep.2011.04.009;
RA Wang S., Wen R., Shi X., Lambrecht A., Wang H., Xiao W.;
RT "RAD5a and REV3 function in two alternative pathways of DNA-damage
RT tolerance in Arabidopsis.";
RL DNA Repair 10:620-628(2011).
CC -!- FUNCTION: Catalytic subunit of the error prone DNA polymerase zeta.
CC Involved in damage-tolerance mechanisms through translesion DNA
CC synthesis. {ECO:0000269|PubMed:12953110, ECO:0000269|PubMed:15908599,
CC ECO:0000269|PubMed:21030509, ECO:0000269|PubMed:21549648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster.;
CC -!- SUBUNIT: Forms DNA polymerase zeta with REV7. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q766Z3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:12953110}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are hypersensitive to UV-B light and
CC gamma rays. {ECO:0000269|PubMed:12953110}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB114052; BAC82450.1; -; mRNA.
DR EMBL; AC004393; AAC18785.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011020; AAG52299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34655.1; -; Genomic_DNA.
DR PIR; D96698; D96698.
DR PIR; T02155; T02155.
DR RefSeq; NP_176917.2; NM_105417.4. [Q766Z3-1]
DR AlphaFoldDB; Q766Z3; -.
DR SMR; Q766Z3; -.
DR STRING; 3702.AT1G67500.2; -.
DR iPTMnet; Q766Z3; -.
DR PaxDb; Q766Z3; -.
DR PRIDE; Q766Z3; -.
DR ProteomicsDB; 236920; -. [Q766Z3-1]
DR EnsemblPlants; AT1G67500.1; AT1G67500.1; AT1G67500. [Q766Z3-1]
DR GeneID; 843071; -.
DR Gramene; AT1G67500.1; AT1G67500.1; AT1G67500. [Q766Z3-1]
DR KEGG; ath:AT1G67500; -.
DR Araport; AT1G67500; -.
DR eggNOG; KOG0968; Eukaryota.
DR HOGENOM; CLU_000203_3_0_1; -.
DR PhylomeDB; Q766Z3; -.
DR PRO; PR:Q766Z3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q766Z3; baseline and differential.
DR Genevisible; Q766Z3; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0071494; P:cellular response to UV-C; IMP:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; PTHR45812; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Alternative splicing; DNA damage; DNA repair; DNA replication;
KW DNA-binding; DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1890
FT /note="DNA polymerase zeta catalytic subunit"
FT /id="PRO_0000424418"
FT ZN_FING 1789..1806
FT /note="CysA-type"
FT /evidence="ECO:0000250"
FT REGION 508..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1835..1856
FT /note="CysB motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 508..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1789
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1792
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1803
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1806
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1835
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1838
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1851
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1856
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1890 AA; 210848 MW; 7E3E5BF3C140C105 CRC64;
MADSQSGSNV FSLRIVSIDY YMASPIPGYN ICYSSFQGSE VNEVPVIRIY GSTPAGQKTC
LHIHRALPYL YIPCSEIPLE HHKGVDGSTL ALSLELEKAL KLKGNAASKR QHIHDCEIVR
AKKFYGYHST EEAFVKIYLS YHPPDVARAA SLLLAGAVLG KSLQPYESHI PFILQFLVDY
NLYGMGHVHI SKMKFRSPVP HHFRPRRFDL DDCPGQRIDE VAITKANSSA AASVSFPVWS
LSTIPGQWMW NLSEESDTPL SQSQHRHQHH YRRQSLCELE GDATSSDILN QQFKMYNSLS
QAQSDTNMVQ SLVAIWEEEY ERTGVHDAPI PPDPGKPSAA DVLQTMSDYV GFGNMLKEML
NKVELSPPGM KPTAVSSAGP DMHAKPEITD LQALNHMVGT CSEFPASEQL SPLGEKSEEA
SMENDEYMKT PTDRDTPAQI QDAEALGLFK WFASSQAAED INSDDEILRE TILSPLLPLA
SINKVLEMAS TDYVSQSQKE CQDILDSQEN LPDFGSSTKR ALPSNPDSQN LRTSSDKQSL
EIEVASDVPD SSTSNGASEN SFRRYRKSDL HTSEVMEYKN RSFSKSNKPS NSVWGPLPFT
LTKNLQKDFD STNASDKLGL TKISSYPMNE MTDNYIVPVK EHQADVCNTI DRNVLAGCSL
RDLMRKKRLC HGESPVSQHM KSRKVRDSRH GEKNECTLRC EAKKQGPALS AEFSEFVCGD
TPNLSPIDSG NCECNISTES SELHSVDRCS AKETASQNSD EVLRNLSSTT VPFGKDPQTV
ESGTLVSSNI HVGIEIDSVQ KSGREQESTA NETDETGRLI CLTLSKKPPS LDCLSAGLQD
SAHSHEIHAR EKQHDEYEGN SNDIPFFPLE DNKEEKKHFF QGTSLGIPLH HLNDGSNLYL
LTPAFSPPSV DSVLQWISND KGDSNIDSEK QPLRDNHNDR GASFTDLASA SNVVSVSEHV
EQHNNLFVNS ESNAYTESEI DLKPKGTFLN LNLQASVSQE LSQISGPDGK SGPTPLSQMG
FRDPASMGAG QQLTILSIEV HAESRGDLRP DPRFDSVNVI ALVVQNDDSF VAEVFVLLFS
PDSIDQRNVD GLSGCKLSVF LEERQLFRYF IETLCKWDPD VLLGWDIQGG SIGFLAERAA
QLGIRFLNNI SRTPSPTTTN NSDNKRKLGN NLLPDPLVAN PAQVEEVVIE DEWGRTHASG
VHVGGRIVLN AWRLIRGEVK LNMYTIEAVS EAVLRQKVPS IPYKVLTEWF SSGPAGARYR
CIEYVIRRAN LNLEIMSQLD MINRTSELAR VFGIDFFSVL SRGSQYRVES MLLRLAHTQN
YLAISPGNQQ VASQPAMECV PLVMEPESAF YDDPVIVLDF QSLYPSMIIA YNLCFSTCLG
KLAHLKMNTL GVSSYSLDLD VLQDLNQILQ TPNSVMYVPP EVRRGILPRL LEEILSTRIM
VKKAMKKLTP SEAVLHRIFN ARQLALKLIA NVTYGYTAAG FSGRMPCAEL ADSIVQCGRS
TLEKAISFVN ANDNWNARVV YGDTDSMFVL LKGRTVKEAF VVGQEIASAI TEMNPHPVTL
KMEKVYHPCF LLTKKRYVGY SYESPNQREP IFDAKGIETV RRDTCEAVAK TMEQSLRLFF
EQKNISKVKS YLYRQWKRIL SGRVSLQDFI FAKEVRLGTY STRDSSLLPP AAIVATKSMK
ADPRTEPRYA ERVPYVVIHG EPGARLVDMV VDPLVLLDVD TPYRLNDLYY INKQIIPALQ
RVFGLVGADL NQWFLEMPRL TRSSLGQRPL NSKNSHKTRI DYFYLSKHCI LCGEVVQESA
QLCNRCLQNK SAAAATIVWK TSKLEREMQH LATICRHCGG GDWVVQSGVK CNSLACSVFY
ERRKVQKELR GLSSIATESE LYPKCMAEWF
