RFC4_MOUSE
ID RFC4_MOUSE Reviewed; 364 AA.
AC Q99J62;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Replication factor C subunit 4;
DE AltName: Full=Activator 1 subunit 4;
GN Name=Rfc4;
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=Liver;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 241-255, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
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).
RN [5]
RP INTERACTION WITH CNTD1.
RX PubMed=32640224; DOI=10.1016/j.celrep.2020.107858;
RA Gray S., Santiago E.R., Chappie J.S., Cohen P.E.;
RT "Cyclin N-Terminal Domain-Containing-1 Coordinates Meiotic Crossover
RT Formation with Cell-Cycle Progression in a Cyclin-Independent Manner.";
RL Cell Rep. 32:107858-107858(2020).
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. This subunit
CC may be involved in the elongation of the multiprimed DNA template (By
CC similarity). {ECO:0000250}.
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). Interacts with CNTD1;
CC this interaction facilitates crossover formation (PubMed:32640224).
CC {ECO:0000250, ECO:0000269|PubMed:32640224}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Despite of the presence of a putative ATP-binding motif,
CC this protein does not bind ATP. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
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DR EMBL; AK146954; BAE27563.1; -; mRNA.
DR EMBL; BC003335; AAH03335.1; -; mRNA.
DR CCDS; CCDS37301.1; -.
DR RefSeq; NP_663455.1; NM_145480.1.
DR AlphaFoldDB; Q99J62; -.
DR SMR; Q99J62; -.
DR BioGRID; 223040; 9.
DR ComplexPortal; CPX-472; DNA replication factor C complex.
DR IntAct; Q99J62; 3.
DR MINT; Q99J62; -.
DR STRING; 10090.ENSMUSP00000023598; -.
DR iPTMnet; Q99J62; -.
DR PhosphoSitePlus; Q99J62; -.
DR EPD; Q99J62; -.
DR MaxQB; Q99J62; -.
DR PaxDb; Q99J62; -.
DR PeptideAtlas; Q99J62; -.
DR PRIDE; Q99J62; -.
DR ProteomicsDB; 253227; -.
DR Antibodypedia; 3877; 293 antibodies from 33 providers.
DR DNASU; 106344; -.
DR Ensembl; ENSMUST00000023598; ENSMUSP00000023598; ENSMUSG00000022881.
DR GeneID; 106344; -.
DR KEGG; mmu:106344; -.
DR UCSC; uc007yth.1; mouse.
DR CTD; 5984; -.
DR MGI; MGI:2146571; Rfc4.
DR VEuPathDB; HostDB:ENSMUSG00000022881; -.
DR eggNOG; KOG0989; Eukaryota.
DR GeneTree; ENSGT00550000074917; -.
DR HOGENOM; CLU_042324_1_1_1; -.
DR InParanoid; Q99J62; -.
DR OMA; KIVMVFS; -.
DR OrthoDB; 1071197at2759; -.
DR PhylomeDB; Q99J62; -.
DR TreeFam; TF314424; -.
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; 106344; 22 hits in 77 CRISPR screens.
DR ChiTaRS; Rfc4; mouse.
DR PRO; PR:Q99J62; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q99J62; protein.
DR Bgee; ENSMUSG00000022881; Expressed in floor plate of midbrain and 256 other tissues.
DR ExpressionAtlas; Q99J62; baseline and differential.
DR Genevisible; Q99J62; 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:0031391; C:Elg1 RFC-like complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; 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 Acetylation; ATP-binding; Direct protein sequencing; DNA replication;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..364
FT /note="Replication factor C subunit 4"
FT /id="PRO_0000244008"
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P35249"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35249"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35249"
SQ SEQUENCE 364 AA; 39867 MW; 30855DE130D1FA96 CRC64;
MQAFLKGTSV SAKAQLTKDR GTPATAGSSG ETKKVKPVPW VEKYRPKCVD EVAFQDEVVA
VLRKSLEGAD LPNLLFYGPP GTGKTSTILA AARELFGPEL FRLRVLELNA SDERGIQVVR
EKVKNFAQLT VSGSRSDGKP CPPFKIVILD EADSMTSAAQ AALRRTMEKE SKTTRFCLIC
NYVSRIIEPL TSRCSKFRFK PLSDKIQQER LLDIAEKENV KIGNEEIAYL VKISEGDLRK
AITFLQSATR LTGGKEVSED VITDIAGVIP AATIDGIFTA CHSGSFDKLE AVVKNLIDEG
HAATQLVNQL HDAIIENENL SDKHKSIITE KLAEVDKCLA DGADEHLQLM SLCATVMQQL
TQNC
