RFC2_CHICK
ID RFC2_CHICK Reviewed; 359 AA.
AC P53033;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Replication factor C subunit 2;
DE AltName: Full=Activator 1 40 kDa subunit;
DE Short=A1 40 kDa subunit;
DE AltName: Full=Activator 1 subunit 2;
DE AltName: Full=Replication factor C 40 kDa subunit;
DE Short=RF-C 40 kDa subunit;
DE Short=RFC40;
GN Name=RFC2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Leghorn; TISSUE=Cochlea;
RX PubMed=8068208; DOI=10.1089/dna.1994.13.857;
RA Oberholtzer J., Cohen E.L., Davis J.G.;
RT "Molecular cloning of a chick cochlea cDNA encoding a subunit of DNA
RT replication factor C/activator 1.";
RL DNA Cell Biol. 13:857-863(1994).
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 (By similarity). {ECO:0000250}.
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; U12438; AAA20552.1; -; mRNA.
DR PIR; I50704; I50704.
DR RefSeq; NP_990861.1; NM_205530.1.
DR AlphaFoldDB; P53033; -.
DR SMR; P53033; -.
DR STRING; 9031.ENSGALP00000001978; -.
DR PaxDb; P53033; -.
DR Ensembl; ENSGALT00000047466; ENSGALP00000052755; ENSGALG00000029449.
DR GeneID; 396542; -.
DR KEGG; gga:396542; -.
DR CTD; 5982; -.
DR VEuPathDB; HostDB:geneid_396542; -.
DR eggNOG; KOG0991; Eukaryota.
DR GeneTree; ENSGT00550000075050; -.
DR HOGENOM; CLU_042324_0_1_1; -.
DR InParanoid; P53033; -.
DR OMA; SCNYSSQ; -.
DR OrthoDB; 1071197at2759; -.
DR PhylomeDB; P53033; -.
DR TreeFam; TF300585; -.
DR Reactome; R-GGA-110312; Translesion synthesis by REV1.
DR Reactome; R-GGA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-GGA-110320; Translesion Synthesis by POLH.
DR Reactome; R-GGA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-GGA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-GGA-217106; Chk1-controlled and DNA-damage induced centrosome duplication.
DR Reactome; R-GGA-351451; Homologous recombination repair of replication-dependent double-strand breaks.
DR Reactome; R-GGA-353303; Nucleotide Excision Repair.
DR Reactome; R-GGA-5655862; Translesion synthesis by POLK.
DR Reactome; R-GGA-5656121; Translesion synthesis by POLI.
DR Reactome; R-GGA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-GGA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-GGA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-GGA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-GGA-5696400; Dual Incision in GG-NER.
DR Reactome; R-GGA-6782135; Dual incision in TC-NER.
DR Reactome; R-GGA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-GGA-69091; Polymerase switching.
DR PRO; PR:P53033; -.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000029449; Expressed in spleen and 12 other tissues.
DR ExpressionAtlas; P53033; baseline and differential.
DR GO; GO:0005663; C:DNA replication factor C complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
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 ATP-binding; DNA replication; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..359
FT /note="Replication factor C subunit 2"
FT /id="PRO_0000121768"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 359 AA; 39707 MW; A2FD38F964CD11F9 CRC64;
MEEEEVLEVV EDEKAGPAAA EKRGPTDTLG SAPAASGHYE LPWVEKYRPL KLCEVVGNED
TVSRLEVFAK EGNVPNIIIA GPPGTGKTTS ILCLARALLG PALKDAVLEL NASNDRGIDV
VRNKIKMFAQ QKVTLPKGRH KIIILDEADS MTDGAQQALR RTMEIYSKTT RFALACNASD
KIIEPIQSRC AVLRYTKLTD SQILARLLKI VEKEDVPYTD DGLEAIIFTA QGDMRQALNN
LQSTYSGFGF INSENVFKVC DEPHPLLVKE MIQHCINANI DEAYKILAHL WRLGYSPEDV
IGNIFRVCKT FQMPEYLKLE FIKEIGYTHM KIAEGVNSLL QMAGLLARLC QKTAAPAAS
