POLZ2_DROME
ID POLZ2_DROME Reviewed; 198 AA.
AC Q9VNE1; B3LF70;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=DNA polymerase zeta subunit 2 {ECO:0000312|FlyBase:FBgn0037345};
DE AltName: Full=DNA polymerase zeta Rev7 subunit {ECO:0000303|PubMed:15175013};
DE AltName: Full=DNA polymerase zeta processivity subunit {ECO:0000305};
DE AltName: Full=Revertibility protein 7 {ECO:0000305};
GN Name=PolZ2 {ECO:0000312|FlyBase:FBgn0037345};
GN Synonyms=mad2B {ECO:0000312|EMBL:AAF52000.1},
GN Rev7 {ECO:0000303|PubMed:15175013};
GN ORFNames=CG2948 {ECO:0000312|FlyBase:FBgn0037345};
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:BAC82838.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND IDENTIFICATION IN THE DNA
RP POLYMERASE ZETA COMPLEX.
RX PubMed=15175013; DOI=10.1042/bj20031833;
RA Takeuchi R., Oshige M., Uchida M., Ishikawa G., Takata K., Shimanouchi K.,
RA Kanai Y., Ruike T., Morioka H., Sakaguchi K.;
RT "Purification of Drosophila DNA polymerase zeta by REV1 protein-affinity
RT chromatography.";
RL Biochem. J. 382:535-543(2004).
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:ACE82581.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE ZETA COMPLEX, INTERACTION
RP WITH RRP1, 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).
CC -!- FUNCTION: As the accessory component of the DNA polymerase zeta
CC complex, involved in translesion DNA synthesis (TLS) and various DNA
CC repair mechanisms (PubMed:15175013, PubMed:16507570). Promotes the
CC apurinic/apyrimidinic (AP) endonuclease activity of Rrp1 and is
CC therefore likely to be involved in the base excision repair (BER)
CC pathway responsible for repair of DNA lesions (PubMed:16507570). It
CC does not appear to influence the synthesis activity of the catalytic
CC component Dmpol-zeta (PubMed:15175013). {ECO:0000269|PubMed:15175013,
CC ECO:0000269|PubMed:16507570}.
CC -!- SUBUNIT: Accessory subunit of the zeta DNA polymerase complex, which
CC consists of the catalytic component PolZ1/DNApol-zeta and PolZ2/Rev7
CC (PubMed:16507570, PubMed:15175013). Interacts with the
CC apurinic/apyrimidinic (AP) endonuclease Rrp1 (via the N-terminus)
CC (PubMed:16507570). {ECO:0000269|PubMed:15175013,
CC ECO:0000269|PubMed:16507570}.
CC -!- INTERACTION:
CC Q9VNE1; Q9VL21: Dmel\CG5708; NbExp=3; IntAct=EBI-157610, EBI-119676;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, with slightly
CC higher levels of expression in 0-4 hour embryos, larvae and adults.
CC {ECO:0000269|PubMed:16507570}.
CC -!- SIMILARITY: Belongs to the MAD2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACE82581.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB115908; BAC82838.1; -; mRNA.
DR EMBL; AE014297; AAF52000.1; -; Genomic_DNA.
DR EMBL; BT033058; ACE82581.1; ALT_INIT; mRNA.
DR RefSeq; NP_649555.1; NM_141298.2.
DR AlphaFoldDB; Q9VNE1; -.
DR SMR; Q9VNE1; -.
DR DIP; DIP-20675N; -.
DR IntAct; Q9VNE1; 99.
DR STRING; 7227.FBpp0078348; -.
DR PaxDb; Q9VNE1; -.
DR DNASU; 40677; -.
DR EnsemblMetazoa; FBtr0078699; FBpp0078348; FBgn0037345.
DR GeneID; 40677; -.
DR KEGG; dme:Dmel_CG2948; -.
DR UCSC; CG2948-RA; d. melanogaster.
DR CTD; 40677; -.
DR FlyBase; FBgn0037345; PolZ2.
DR VEuPathDB; VectorBase:FBgn0037345; -.
DR eggNOG; KOG3186; Eukaryota.
DR GeneTree; ENSGT00940000153395; -.
DR HOGENOM; CLU_050394_2_0_1; -.
DR InParanoid; Q9VNE1; -.
DR OMA; QYQEFPW; -.
DR OrthoDB; 1630737at2759; -.
DR PhylomeDB; Q9VNE1; -.
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; Q9VNE1; -.
DR BioGRID-ORCS; 40677; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40677; -.
DR PRO; PR:Q9VNE1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037345; Expressed in Malpighian tubule and 23 other tissues.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IPI:FlyBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:1902380; P:positive regulation of endoribonuclease activity; IDA:FlyBase.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR003511; HORMA_dom.
DR InterPro; IPR036570; HORMA_dom_sf.
DR InterPro; IPR045091; Mad2-like.
DR PANTHER; PTHR11842; PTHR11842; 1.
DR Pfam; PF02301; HORMA; 1.
DR SUPFAM; SSF56019; SSF56019; 1.
DR PROSITE; PS50815; HORMA; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Reference proteome.
FT CHAIN 1..198
FT /note="DNA polymerase zeta subunit 2"
FT /id="PRO_0000448744"
FT DOMAIN 4..196
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
SQ SEQUENCE 198 AA; 23147 MW; 1C4BBE51A9D8B098 CRC64;
MQAEIKADII VEAMEVLVNH ILYVRGIYPS HIFKMKRMYN SPIYVSIFPP LNNYLAGVLK
SAQELLRRRE LQCLELIVYQ KENEKLESYK MQLETQRSGL PAEDHLMEFE QNMRSVIYKI
SQRLNQAPKL PAGSCQFKVH LHTTQEAFIR FSHDSQYQEF PWLQTQKTES QATGRTVYLL
PLARVDDLGL KMDVLIVN
