RFC3_MOUSE
ID RFC3_MOUSE Reviewed; 356 AA.
AC Q8R323;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Replication factor C subunit 3;
DE AltName: Full=Activator 1 38 kDa subunit;
DE Short=A1 38 kDa subunit;
DE AltName: Full=Activator 1 subunit 3;
DE AltName: Full=Replication factor C 38 kDa subunit;
DE Short=RF-C 38 kDa subunit;
DE Short=RFC38;
GN Name=Rfc3;
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].
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, 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 [3]
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.
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 -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
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DR EMBL; BC026795; AAH26795.1; -; mRNA.
DR CCDS; CCDS39413.1; -.
DR RefSeq; NP_081285.1; NM_027009.2.
DR AlphaFoldDB; Q8R323; -.
DR SMR; Q8R323; -.
DR BioGRID; 213324; 9.
DR ComplexPortal; CPX-472; DNA replication factor C complex.
DR CORUM; Q8R323; -.
DR IntAct; Q8R323; 3.
DR STRING; 10090.ENSMUSP00000039621; -.
DR iPTMnet; Q8R323; -.
DR PhosphoSitePlus; Q8R323; -.
DR EPD; Q8R323; -.
DR MaxQB; Q8R323; -.
DR PaxDb; Q8R323; -.
DR PRIDE; Q8R323; -.
DR ProteomicsDB; 253226; -.
DR Antibodypedia; 7909; 252 antibodies from 32 providers.
DR Ensembl; ENSMUST00000038131; ENSMUSP00000039621; ENSMUSG00000033970.
DR GeneID; 69263; -.
DR KEGG; mmu:69263; -.
DR UCSC; uc009aus.1; mouse.
DR CTD; 5983; -.
DR MGI; MGI:1916513; Rfc3.
DR VEuPathDB; HostDB:ENSMUSG00000033970; -.
DR eggNOG; KOG2035; Eukaryota.
DR GeneTree; ENSGT00550000075006; -.
DR HOGENOM; CLU_042324_5_0_1; -.
DR InParanoid; Q8R323; -.
DR OMA; LMCEACK; -.
DR OrthoDB; 1071197at2759; -.
DR PhylomeDB; Q8R323; -.
DR TreeFam; TF105724; -.
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; 69263; 28 hits in 73 CRISPR screens.
DR PRO; PR:Q8R323; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R323; protein.
DR Bgee; ENSMUSG00000033970; Expressed in medial ganglionic eminence and 250 other tissues.
DR ExpressionAtlas; Q8R323; baseline and differential.
DR Genevisible; Q8R323; 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:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003689; F:DNA clamp loader activity; ISO:MGI.
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:0006260; P:DNA replication; ISO:MGI.
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 GO; GO:0046683; P:response to organophosphorus; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA replication; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..356
FT /note="Replication factor C subunit 3"
FT /id="PRO_0000121762"
FT MOD_RES 20
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40938"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40938"
SQ SEQUENCE 356 AA; 40526 MW; 795A37D28D475C64 CRC64;
MSLWVDKYRP SSLARLDYHK EQAAQLRNLV QCGDFPHLLV YGPSGAGKKT RIMCILRELY
GIGVEKLRIE HQTITTPSKK KIEISTIASN YHLEVNPSDA GNSDRVVIQE MLKTVAQSQQ
LETSSQRDFK VVLLTEVDKL TKDAQHALRR TMEKYMSTCR LILCCNSTSK VIPPIRSRCL
AVRVPAPSIE DICSVLSTVC RKEGLALPST LARRLAEKSC RNLRKALLMC EACRVQQYPF
TEDQEIPETD WEVYLRETAN AIVSQQTPQR LLEVRGRLYE LLTHCIPPEI IMKGLLSELL
HNCDGQLKGE VAQMAAYYEH RLQLGSKAIY HLEAFVAKFM ALYKKFMEDG LEGMMF
