RFC5_MOUSE
ID RFC5_MOUSE Reviewed; 339 AA.
AC Q9D0F6;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Replication factor C subunit 5;
DE AltName: Full=Activator 1 36 kDa subunit;
DE Short=A1 36 kDa subunit;
DE AltName: Full=Activator 1 subunit 5;
DE AltName: Full=Replication factor C 36 kDa subunit;
DE Short=RF-C 36 kDa subunit;
DE Short=RFC36;
GN Name=Rfc5;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex either with RFC1 or with RAD17. The former interacts
CC with PCNA in the presence of ATP, while the latter has ATPase activity
CC but is not stimulated by PCNA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK011489; BAB27652.1; -; mRNA.
DR CCDS; CCDS39235.1; -.
DR RefSeq; NP_082404.1; NM_028128.1.
DR AlphaFoldDB; Q9D0F6; -.
DR SMR; Q9D0F6; -.
DR BioGRID; 215186; 12.
DR ComplexPortal; CPX-472; DNA replication factor C complex.
DR CORUM; Q9D0F6; -.
DR IntAct; Q9D0F6; 3.
DR MINT; Q9D0F6; -.
DR STRING; 10090.ENSMUSP00000083652; -.
DR iPTMnet; Q9D0F6; -.
DR PhosphoSitePlus; Q9D0F6; -.
DR EPD; Q9D0F6; -.
DR MaxQB; Q9D0F6; -.
DR PaxDb; Q9D0F6; -.
DR PRIDE; Q9D0F6; -.
DR ProteomicsDB; 255293; -.
DR Antibodypedia; 18857; 126 antibodies from 30 providers.
DR Ensembl; ENSMUST00000086461; ENSMUSP00000083652; ENSMUSG00000029363.
DR GeneID; 72151; -.
DR KEGG; mmu:72151; -.
DR UCSC; uc008zfs.1; mouse.
DR CTD; 5985; -.
DR MGI; MGI:1919401; Rfc5.
DR VEuPathDB; HostDB:ENSMUSG00000029363; -.
DR eggNOG; KOG0990; Eukaryota.
DR GeneTree; ENSGT00550000075072; -.
DR HOGENOM; CLU_042324_2_0_1; -.
DR InParanoid; Q9D0F6; -.
DR OMA; TRTIFCG; -.
DR OrthoDB; 1071197at2759; -.
DR PhylomeDB; Q9D0F6; -.
DR TreeFam; TF300810; -.
DR Reactome; R-MMU-110312; Translesion synthesis by REV1.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-110320; Translesion Synthesis by POLH.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-5651801; PCNA-Dependent Long Patch Base Excision Repair.
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 Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69091; Polymerase switching.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 72151; 29 hits in 73 CRISPR screens.
DR PRO; PR:Q9D0F6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D0F6; protein.
DR Bgee; ENSMUSG00000029363; Expressed in epiblast (generic) and 64 other tissues.
DR ExpressionAtlas; Q9D0F6; baseline and differential.
DR Genevisible; Q9D0F6; MM.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; ISS:UniProtKB.
DR GO; GO:0005663; C:DNA replication factor C complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0003689; F:DNA clamp loader activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; ISS:UniProtKB.
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; DNA replication; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..339
FT /note="Replication factor C subunit 5"
FT /id="PRO_0000121752"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 339 AA; 38096 MW; 8037E4F38FEA8867 CRC64;
MTAAAPSQQR PAAARARNLP WVEKYRPQTL ADLISHQDIL STIQKFISED RLPHLLLYGP
PGTGKTSTIL ACAKQLYKDK EFGSMVLELN ASDDRGIDIV RGPILSFAST RTIFKKGFKL
VILDEADAMT QDAQNALRRV IEKFTENTRF CLICNYLSKI IPALQSRCTR FRFGPLTPEL
MVPRLEHVVQ EENVDISEDG MKALVTLSSG DMRRALNILQ STNMAFGKVT EETVYTCTGH
PLKTDIANIL DWMLNQDFTT AYKNIMELKT LKGLALHDIL TEVHLFVHRV DFPSSVRIHL
LTKMADIEYR LSVGTSEKIQ LSSLIAAFQV TRDLIVAEA
