RFC2_RAT
ID RFC2_RAT Reviewed; 349 AA.
AC Q641W4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Replication factor C subunit 2;
DE AltName: Full=Activator 1 subunit C2;
GN Name=Rfc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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 binds ATP (By 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. RFC2 also interacts with PRKAR1A; the
CC complex may be involved in cell survival. Interacts with DDX11.
CC {ECO:0000250|UniProtKB:P35250}.
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; BC082110; AAH82110.1; -; mRNA.
DR RefSeq; NP_446238.1; NM_053786.1.
DR AlphaFoldDB; Q641W4; -.
DR SMR; Q641W4; -.
DR STRING; 10116.ENSRNOP00000001989; -.
DR jPOST; Q641W4; -.
DR PaxDb; Q641W4; -.
DR PRIDE; Q641W4; -.
DR Ensembl; ENSRNOT00000094282; ENSRNOP00000077503; ENSRNOG00000001457.
DR GeneID; 116468; -.
DR KEGG; rno:116468; -.
DR UCSC; RGD:621198; rat.
DR CTD; 5982; -.
DR RGD; 621198; Rfc2.
DR eggNOG; KOG0991; Eukaryota.
DR GeneTree; ENSGT00550000075050; -.
DR HOGENOM; CLU_042324_0_1_1; -.
DR InParanoid; Q641W4; -.
DR OMA; SCNYSSQ; -.
DR OrthoDB; 1071197at2759; -.
DR PhylomeDB; Q641W4; -.
DR TreeFam; TF300585; -.
DR Reactome; R-RNO-110312; Translesion synthesis by REV1.
DR Reactome; R-RNO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-RNO-110320; Translesion Synthesis by POLH.
DR Reactome; R-RNO-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-RNO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-RNO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-RNO-5655862; Translesion synthesis by POLK.
DR Reactome; R-RNO-5656121; Translesion synthesis by POLI.
DR Reactome; R-RNO-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-RNO-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-RNO-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-RNO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-RNO-5696400; Dual Incision in GG-NER.
DR Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-RNO-69091; Polymerase switching.
DR Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
DR PRO; PR:Q641W4; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001457; Expressed in thymus and 20 other tissues.
DR Genevisible; Q641W4; RN.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; ISS:UniProtKB.
DR GO; GO:0005663; C:DNA replication factor C complex; ISO:RGD.
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; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; DNA replication; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..349
FT /note="Replication factor C subunit 2"
FT /id="PRO_0000330462"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71..78
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:P35250"
FT MOD_RES 158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35250"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35250"
SQ SEQUENCE 349 AA; 38657 MW; 0E9EDF01AFDB2092 CRC64;
MEVQESGSGS AESGTQEPSP VPSKTTGHYE LPWVEKYRPV KLNEIVGNED TVSRLEVFAR
EGNVPNIIIA GPPGTGKTTS ILCLARALLG PALKDAVLEL NASNDRGIDV VRNKIKMFAQ
QKVTLPKGRH KIIILDEADS MTDGAQQALR RTMEIYSKTT RFALACNASD KIIEPIQSRC
AVLRYTKLTD AQVLSRLMNV IEKEKVPYTD DGLEAIIFTA QGDMRQALNN LQSTFSGFGY
INSENVFKVC DEPHPLLVKE MIQHCVDANI DEAYKILAHL WHLGYSPEDV IGNIFRVCKT
FPMAEYLKLE FIKEIGYTHM KVAEGVNSLL QMAGLLARLC QKTMAPVAS
