RFC2_DROME
ID RFC2_DROME Reviewed; 331 AA.
AC P53034; Q9VZH9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Replication factor C subunit 2;
DE AltName: Full=Activator 1 40 kDa subunit;
DE Short=A1 40 kDa subunit;
DE AltName: Full=Activator 1 subunit 2;
DE AltName: Full=Replication factor C 40 kDa subunit;
DE Short=RF-C 40 kDa subunit;
DE Short=RFC40;
DE AltName: Full=Replication factor C subunit 4;
DE Short=DmRfc4;
GN Name=RfC4; Synonyms=RfC40; ORFNames=CG14999;
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], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Iso-1 / Kennison;
RX PubMed=7789770; DOI=10.1093/genetics/139.4.1701;
RA Harrison S.D., Solomon N., Rubin G.M.;
RT "A genetic analysis of the 63E-64A genomic region of Drosophila
RT melanogaster: identification of mutations in a replication factor C
RT subunit.";
RL Genetics 139:1701-1709(1995).
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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11438670; DOI=10.1128/mcb.21.15.5156-5168.2001;
RA Krause S.A., Loupart M.-L., Vass S., Schoenfelder S., Harrison S.,
RA Heck M.M.S.;
RT "Loss of cell cycle checkpoint control in Drosophila Rfc4 mutants.";
RL Mol. Cell. Biol. 21:5156-5168(2001).
CC -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC delta and epsilon requires the action of the accessory proteins
CC proliferating cell nuclear antigen (PCNA) and activator 1. Subunit 2
CC binds ATP. {ECO:0000269|PubMed:11438670}.
CC -!- SUBUNIT: Heteropentamer of subunits of 140/145, 40, 38, 37, and 36.5
CC kDa that forms a complex with PCNA in the presence of ATP.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P53034; Q9VKW3: RfC3; NbExp=3; IntAct=EBI-184606, EBI-118156;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11438670,
CC ECO:0000269|PubMed:7789770}. Note=Localizes to all replicating nuclei,
CC it is dispersed from chromatin in mitosis.
CC -!- DEVELOPMENTAL STAGE: Expressed in early embryos.
CC {ECO:0000269|PubMed:7789770}.
CC -!- DISRUPTION PHENOTYPE: Defects in mitotic chromosome cohesion and
CC condensation due to aberrant checkpoint control in response to DNA
CC replication inhibition or damage to chromosomes; premature chromosome
CC condensation and precocious sister chromatid separation figures.
CC {ECO:0000269|PubMed:11438670}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
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DR EMBL; U15967; AAB60241.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47843.1; -; Genomic_DNA.
DR EMBL; AY094829; AAM11182.1; -; mRNA.
DR PIR; S55020; S55020.
DR RefSeq; NP_523915.1; NM_079191.3.
DR AlphaFoldDB; P53034; -.
DR SMR; P53034; -.
DR BioGRID; 63972; 21.
DR DIP; DIP-22077N; -.
DR IntAct; P53034; 9.
DR STRING; 7227.FBpp0073120; -.
DR PaxDb; P53034; -.
DR PRIDE; P53034; -.
DR DNASU; 38492; -.
DR EnsemblMetazoa; FBtr0073264; FBpp0073120; FBgn0260985.
DR GeneID; 38492; -.
DR KEGG; dme:Dmel_CG14999; -.
DR CTD; 5984; -.
DR FlyBase; FBgn0260985; RfC4.
DR VEuPathDB; VectorBase:FBgn0260985; -.
DR eggNOG; KOG0991; Eukaryota.
DR GeneTree; ENSGT00550000075050; -.
DR HOGENOM; CLU_042324_0_1_1; -.
DR InParanoid; P53034; -.
DR OMA; SCNYSSQ; -.
DR OrthoDB; 1071197at2759; -.
DR PhylomeDB; P53034; -.
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-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-DME-176187; Activation of ATR in response to replication stress.
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-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DME-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-69091; Polymerase switching.
DR Reactome; R-DME-69473; G2/M DNA damage checkpoint.
DR SignaLink; P53034; -.
DR BioGRID-ORCS; 38492; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38492; -.
DR PRO; PR:P53034; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0260985; Expressed in secondary oocyte and 35 other tissues.
DR Genevisible; P53034; DM.
DR GO; GO:0005663; C:DNA replication factor C complex; ISS:FlyBase.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:FlyBase.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:FlyBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0006272; P:leading strand elongation; ISS:FlyBase.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013748; Rep_factorC_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA replication; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..331
FT /note="Replication factor C subunit 2"
FT /id="PRO_0000121769"
FT BINDING 56..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 331 AA; 37173 MW; 0ACE1C6DCBA8AF8F CRC64;
MPEEPEKTAD DKRSHLPWIE KYRPVKFKEI VGNEDTVARL SVFATQGNAP NIIIAGPPGV
GKTTTIQCLA RILLGDSYKE AVLELNASNE RGIDVVRNKI KMFAQQKVTL PRGRHKIVIL
DEADSMTEGA QQALRRTMEI YSSTTRFALA CNTSEKIIEP IQSRCAMLRF TKLSDAQVLA
KLIEVAKWEK LNYTEDGLEA IVFTAQGDMR QGLNNLQSTA QGFGDITAEN VFKVCDEPHP
KLLEEMIHHC AANDIHKAYK ILAKLWKLGY SPEDIIANIF RVCKRINIDE HLKLDFIREI
GITHMKIIDG INSLLQLTAL LAKLCIAAEK H
