ID   RFC3_BOVIN              Reviewed;         356 AA.
AC   Q2TBV1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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       {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 (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:Q8R323}.
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; BC109606; AAI09607.1; -; mRNA.
DR   RefSeq; NP_001033636.1; NM_001038547.2.
DR   AlphaFoldDB; Q2TBV1; -.
DR   SMR; Q2TBV1; -.
DR   CORUM; Q2TBV1; -.
DR   STRING; 9913.ENSBTAP00000014278; -.
DR   PaxDb; Q2TBV1; -.
DR   PRIDE; Q2TBV1; -.
DR   Ensembl; ENSBTAT00000014278; ENSBTAP00000014278; ENSBTAG00000010787.
DR   GeneID; 515602; -.
DR   KEGG; bta:515602; -.
DR   CTD; 5983; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010787; -.
DR   VGNC; VGNC:33887; RFC3.
DR   eggNOG; KOG2035; Eukaryota.
DR   GeneTree; ENSGT00550000075006; -.
DR   HOGENOM; CLU_042324_5_0_1; -.
DR   InParanoid; Q2TBV1; -.
DR   OMA; LMCEACK; -.
DR   OrthoDB; 1071197at2759; -.
DR   TreeFam; TF105724; -.
DR   Reactome; R-BTA-110312; Translesion synthesis by REV1.
DR   Reactome; R-BTA-110320; Translesion Synthesis by POLH.
DR   Reactome; R-BTA-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-BTA-5656169; Termination of translesion DNA synthesis.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000010787; Expressed in oocyte and 109 other tissues.
DR   GO; GO:0031390; C:Ctf18 RFC-like complex; ISS:UniProtKB.
DR   GO; GO:0005663; C:DNA replication factor C complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:Ensembl.
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   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   2: Evidence at transcript 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_0000239457"
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;  40465 MW;  4B0FC2FAF147D8EA CRC64;
     MSLWVDKYRP CSLGQLDYHK EQAAQLRNLV QCGDFPHLLV YGPSGAGKKT RIMCILRELY
     GVGVEKLRIE HQTITTPSKK KIEISTIASN YHLEVNPSDA GNSDRVVIQE MLKTVAQSQQ
     LETSSQKDFK VVLLTEVDKL TKDAQHALRR TMEKYMSTCR LILCCNSTSK VIPPIRSRCL
     AVRVPAPSIE DICHVLSTVC KKEGLNLPPQ LAHRLAEKSC RNLRKALLMC EACRVQQYPF
     TADQEIPETD WEVYLRETAN AIVSQQTPQR LLEVRGRLYE LLTHCIPPEI IMKGLLSELL
     HNCDGQLKGE VAQMAAYYEH RLQLGSKAIY HLEAFVAKFM ALYKKFMEDG LEGMIF