PCNA_DROME
ID PCNA_DROME Reviewed; 260 AA.
AC P17917; Q540V1; Q9V909;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Proliferating cell nuclear antigen {ECO:0000303|PubMed:1968224};
DE Short=PCNA {ECO:0000303|PubMed:1968224};
DE AltName: Full=Cyclin {ECO:0000303|PubMed:1968224};
DE AltName: Full=Mutagen-sensitive 209 protein {ECO:0000312|FlyBase:FBgn0005655};
GN Name=PCNA {ECO:0000303|PubMed:1968224, ECO:0000312|FlyBase:FBgn0005655};
GN Synonyms=mus209 {ECO:0000312|FlyBase:FBgn0005655},
GN PCNA1 {ECO:0000303|PubMed:17087725};
GN ORFNames=CG9193 {ECO:0000312|FlyBase:FBgn0005655};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=1968224; DOI=10.1128/mcb.10.3.872-879.1990;
RA Yamaguchi M., Nishida Y., Moriuchi T., Hirose F., Hui C.C., Suzuki Y.,
RA Matsukage A.;
RT "Drosophila proliferating cell nuclear antigen (cyclin) gene: structure,
RT expression during development, and specific binding of homeodomain proteins
RT to its 5'-flanking region.";
RL Mol. Cell. Biol. 10:872-879(1990).
RN [2]
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [5]
RP PROTEIN SEQUENCE OF 1-22.
RC STRAIN=Oregon-R;
RX PubMed=1973166; DOI=10.1016/s0021-9258(19)38492-3;
RA Ng L., Prelich G., Anderson C.W., Stillman B., Fisher P.A.;
RT "Drosophila proliferating cell nuclear antigen. Structural and functional
RT homology with its mammalian counterpart.";
RL J. Biol. Chem. 265:11948-11954(1990).
RN [6]
RP FUNCTION.
RX PubMed=1360647; DOI=10.1093/nar/20.21.5779;
RA Peck V.M., Gerner E.W., Cress A.E.;
RT "Delta-type DNA polymerase characterized from Drosophila melanogaster
RT embryos.";
RL Nucleic Acids Res. 20:5779-5784(1992).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=7907981; DOI=10.1002/j.1460-2075.1994.tb06399.x;
RA Henderson D.S., Banga S.S., Grigliatto T.A., Boyd J.B.;
RT "Mutagen sensitivity and suppression of position-effect variegation result
RT from mutations in mus209, the Drosophila gene encoding PCNA.";
RL EMBO J. 13:1450-1459(1994).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=9310333; DOI=10.1242/dev.124.17.3385;
RA Yamamoto Y., Girard F., Bello B., Affolter M., Gehring W.J.;
RT "The cramped gene of Drosophila is a member of the polycomb-group, and
RT interacts with mus209, the gene encoding proliferating cell nuclear
RT antigen.";
RL Development 124:3385-3394(1997).
RN [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH POLD1 AND POLE1, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=17087725; DOI=10.1111/j.1742-4658.2006.05504.x;
RA Ruike T., Takeuchi R., Takata K., Oshige M., Kasai N., Shimanouchi K.,
RA Kanai Y., Nakamura R., Sugawara F., Sakaguchi K.;
RT "Characterization of a second proliferating cell nuclear antigen (PCNA2)
RT from Drosophila melanogaster.";
RL FEBS J. 273:5062-5073(2006).
RN [10]
RP INTERACTION WITH E2F.
RX PubMed=19081076; DOI=10.1016/j.devcel.2008.10.003;
RA Shibutani S.T., de la Cruz A.F., Tran V., Turbyfill W.J. III, Reis T.,
RA Edgar B.A., Duronio R.J.;
RT "Intrinsic negative cell cycle regulation provided by PIP box- and
RT Cul4Cdt2-mediated destruction of E2f1 during S phase.";
RL Dev. Cell 15:890-900(2008).
CC -!- FUNCTION: Likely to be an auxiliary protein of DNA polymerase delta
CC complex and is probably involved in the control of DNA replication and
CC repair by increasing the polymerase's processibility.
CC {ECO:0000269|PubMed:1360647}.
CC -!- SUBUNIT: Homotrimer (PubMed:17087725). Forms a complex with activator 1
CC heteropentamer in the presence of ATP (By similarity). Interacts with
CC E2f (PubMed:19081076). Interacts with the catalytic subunits of two DNA
CC polymerase complexes: PolD1 from the delta complex and PolE1/DNApol-
CC epsilon255 from the epsilon complex (PubMed:17087725).
CC {ECO:0000250|UniProtKB:P12004, ECO:0000269|PubMed:17087725,
CC ECO:0000269|PubMed:19081076}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17087725,
CC ECO:0000269|PubMed:9310333}. Chromosome {ECO:0000269|PubMed:17087725}.
CC Cytoplasm {ECO:0000269|PubMed:17087725}. Note=Colocalizes with crm in
CC polytene nuclei during embryogenesis (PubMed:9310333). Increased
CC association with chromatin in response to DNA damage caused by methyl
CC methanesulfonate (MMS), hydrogen peroxide (H2O2) and UV
CC (PubMed:17087725). {ECO:0000269|PubMed:17087725,
CC ECO:0000269|PubMed:9310333}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in adult ovary.
CC {ECO:0000269|PubMed:1968224}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically
CC (PubMed:1968224). Expressed at high levels in embryos at 0-2 and 8-12 h
CC of development (PubMed:17087725, PubMed:1968224). Moderate levels
CC detected at later stages of embryogenesis, in unfertilized eggs and
CC adult females, and relatively low levels of expression were detected in
CC larvae and adult males (PubMed:17087725). {ECO:0000269|PubMed:17087725,
CC ECO:0000269|PubMed:1968224}.
CC -!- DISRUPTION PHENOTYPE: Mutant flies show temperature-sensitive
CC lethality, hypersensitivity to DNA-damaging agents such as ionizing
CC radiation and methyl methanesulfonate, suppression of position-effect
CC variegation and female sterility. {ECO:0000269|PubMed:7907981}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
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DR EMBL; M33950; AAA28746.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57493.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64796.1; -; Genomic_DNA.
DR EMBL; AY122197; AAM52709.1; -; mRNA.
DR PIR; A34752; A34752.
DR RefSeq; NP_476905.1; NM_057557.4.
DR RefSeq; NP_995904.1; NM_206182.2.
DR PDB; 4HK1; X-ray; 2.00 A; A=1-260.
DR PDBsum; 4HK1; -.
DR AlphaFoldDB; P17917; -.
DR SMR; P17917; -.
DR BioGRID; 62946; 79.
DR ComplexPortal; CPX-543; PCNA homotrimer.
DR DIP; DIP-20560N; -.
DR ELM; P17917; -.
DR IntAct; P17917; 16.
DR STRING; 7227.FBpp0085619; -.
DR PaxDb; P17917; -.
DR PRIDE; P17917; -.
DR EnsemblMetazoa; FBtr0086307; FBpp0085619; FBgn0005655.
DR EnsemblMetazoa; FBtr0086308; FBpp0089395; FBgn0005655.
DR GeneID; 37290; -.
DR KEGG; dme:Dmel_CG9193; -.
DR CTD; 5111; -.
DR FlyBase; FBgn0005655; PCNA.
DR VEuPathDB; VectorBase:FBgn0005655; -.
DR eggNOG; KOG1636; Eukaryota.
DR GeneTree; ENSGT00390000004965; -.
DR HOGENOM; CLU_043978_3_0_1; -.
DR InParanoid; P17917; -.
DR OMA; EMKLINM; -.
DR OrthoDB; 1012066at2759; -.
DR PhylomeDB; P17917; -.
DR Reactome; R-DME-110312; Translesion synthesis by REV1.
DR Reactome; R-DME-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-DME-110320; Translesion Synthesis by POLH.
DR Reactome; R-DME-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-DME-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DME-5655862; Translesion synthesis by POLK.
DR Reactome; R-DME-5656121; Translesion synthesis by POLI.
DR Reactome; R-DME-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-DME-69091; Polymerase switching.
DR Reactome; R-DME-69166; Removal of the Flap Intermediate.
DR Reactome; R-DME-69183; Processive synthesis on the lagging strand.
DR SignaLink; P17917; -.
DR BioGRID-ORCS; 37290; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37290; -.
DR PRO; PR:P17917; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0005655; Expressed in secondary oocyte and 45 other tissues.
DR Genevisible; P17917; DM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0043626; C:PCNA complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IMP:FlyBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; TAS:FlyBase.
DR GO; GO:0007307; P:eggshell chorion gene amplification; TAS:FlyBase.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0006289; P:nucleotide-excision repair; TAS:FlyBase.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:ComplexPortal.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0072702; P:response to methyl methanesulfonate; IDA:UniProtKB.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; IBA:GO_Central.
DR HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR InterPro; IPR000730; Pr_cel_nuc_antig.
DR InterPro; IPR022649; Pr_cel_nuc_antig_C.
DR InterPro; IPR022659; Pr_cel_nuc_antig_CS.
DR InterPro; IPR022648; Pr_cel_nuc_antig_N.
DR Pfam; PF02747; PCNA_C; 1.
DR Pfam; PF00705; PCNA_N; 1.
DR PRINTS; PR00339; PCNACYCLIN.
DR TIGRFAMs; TIGR00590; pcna; 1.
DR PROSITE; PS01251; PCNA_1; 1.
DR PROSITE; PS00293; PCNA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; Direct protein sequencing;
KW DNA replication; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..260
FT /note="Proliferating cell nuclear antigen"
FT /id="PRO_0000149170"
FT DNA_BIND 61..80
FT /evidence="ECO:0000255"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4HK1"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:4HK1"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:4HK1"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4HK1"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:4HK1"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:4HK1"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:4HK1"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:4HK1"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:4HK1"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:4HK1"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:4HK1"
SQ SEQUENCE 260 AA; 28830 MW; 9A46280EA2C61FC5 CRC64;
MFEARLGQAT ILKKILDAIK DLLNEATFDC SDSGIQLQAM DNSHVSLVSL TLRSDGFDKF
RCDRNLSMGM NLGSMAKILK CANNEDNVTM KAQDNADTVT IMFESANQEK VSDYEMKLMN
LDQEHLGIPE TDFSCVVRMP AMEFARICRD LAQFSESVVI CCTKEGVKFS ASGDVGTANI
KLAQTGSVDK EEEAVIIEMQ EPVTLTFACR YLNAFTKATP LSTQVQLSMC ADVPLVVEYA
IKDLGHIRYY LAPKIEDNET
