PCNA_CHICK
ID PCNA_CHICK Reviewed; 262 AA.
AC Q9DEA3;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Proliferating cell nuclear antigen;
DE Short=PCNA;
GN Name=PCNA;
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], AND IN VITRO BINDING TO TOP2A.
RX PubMed=11453553; DOI=10.1007/s004120100140;
RA Niimi A., Suka N., Harata M., Kikuchi A., Mizuno S.;
RT "Co-localization of chicken DNA topoisomerase IIalpha, but not beta, with
RT sites of DNA replication and possible involvement of a C-terminal region of
RT alpha through its binding to PCNA.";
RL Chromosoma 110:102-114(2001).
RN [2]
RP INTERACTION WITH DNMT1.
RX PubMed=9302295; DOI=10.1126/science.277.5334.1996;
RA Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.;
RT "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for
RT p21WAF1.";
RL Science 277:1996-2000(1997).
RN [3]
RP INTERACTION WITH CHAF1A.
RX PubMed=17065558; DOI=10.1091/mbc.e06-05-0426;
RA Takami Y., Ono T., Fukagawa T., Shibahara K., Nakayama T.;
RT "Essential role of chromatin assembly factor-1-mediated rapid nucleosome
RT assembly for DNA replication and cell division in vertebrate cells.";
RL Mol. Biol. Cell 18:129-141(2007).
CC -!- FUNCTION: This protein is an auxiliary protein of DNA polymerase delta
CC and is involved in the control of eukaryotic DNA replication by
CC increasing the polymerase's processibility during elongation of the
CC leading strand. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Forms a complex with activator 1 heteropentamer in
CC the presence of ATP. Interacts with DNMT1 (By similarity). Interacts
CC with CHAF1A. Component of the replisome complex (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P12004,
CC ECO:0000269|PubMed:17065558, ECO:0000269|PubMed:9302295}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12004}.
CC -!- PTM: Monoubiquitinated by the UBE2B-RAD18 complex on Lys-164.
CC Monoubiquitination at Lys-164 also takes place in undamaged
CC proliferating cells, and is mediated by the DCX(DTL) complex, leading
CC to enhance PCNA-dependent translesion DNA synthesis (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
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DR EMBL; AB053163; BAB20424.1; -; mRNA.
DR RefSeq; NP_989501.1; NM_204170.2.
DR AlphaFoldDB; Q9DEA3; -.
DR SMR; Q9DEA3; -.
DR BioGRID; 675031; 3.
DR STRING; 9031.ENSGALP00000000224; -.
DR iPTMnet; Q9DEA3; -.
DR PaxDb; Q9DEA3; -.
DR Ensembl; ENSGALT00000083492; ENSGALP00000064149; ENSGALG00000029292.
DR GeneID; 373984; -.
DR KEGG; gga:373984; -.
DR CTD; 5111; -.
DR VEuPathDB; HostDB:geneid_373984; -.
DR eggNOG; KOG1636; Eukaryota.
DR GeneTree; ENSGT00390000004965; -.
DR HOGENOM; CLU_043978_3_0_1; -.
DR InParanoid; Q9DEA3; -.
DR OMA; EMKLINM; -.
DR OrthoDB; 1012066at2759; -.
DR PhylomeDB; Q9DEA3; -.
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-353299; RAD18 and ubiquitinated PCNA-mediated recruitment of translesion polymerases.
DR Reactome; R-GGA-353303; Nucleotide Excision Repair.
DR Reactome; R-GGA-4615885; SUMOylation of DNA replication proteins.
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-5685942; HDR through Homologous Recombination (HRR).
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-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-GGA-69091; Polymerase switching.
DR Reactome; R-GGA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR PRO; PR:Q9DEA3; -.
DR Proteomes; UP000000539; Chromosome 22.
DR Bgee; ENSGALG00000029292; Expressed in spermatid and 13 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0043626; C:PCNA complex; IBA:GO_Central.
DR GO; GO:0070557; C:PCNA-p21 complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:AgBase.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR InterPro; IPR000730; Pr_cel_nuc_antig.
DR InterPro; IPR022649; Pr_cel_nuc_antig_C.
DR InterPro; IPR022659; Pr_cel_nuc_antig_CS.
DR InterPro; IPR022648; Pr_cel_nuc_antig_N.
DR Pfam; PF02747; PCNA_C; 1.
DR Pfam; PF00705; PCNA_N; 1.
DR PRINTS; PR00339; PCNACYCLIN.
DR TIGRFAMs; TIGR00590; pcna; 1.
DR PROSITE; PS01251; PCNA_1; 1.
DR PROSITE; PS00293; PCNA_2; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..262
FT /note="Proliferating cell nuclear antigen"
FT /id="PRO_0000149163"
FT DNA_BIND 61..80
FT /evidence="ECO:0000255"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 262 AA; 28888 MW; BD5B14D7D302D0B1 CRC64;
MFEARLVQGS VLKRVLEALK DLITEACWDL GSGGISLQSM DSSHVSLVQL TLRSEGFDTY
RCDRNIAMGV NLNSMSKILK CAGNEDIITL RAEDNADTLA LVFEAPNQEK VSDYEMKLMD
LDVEQLGIPE QEYSCVVKMP SAEFARICRD LSHIGDAVVI SCAKDGVKFS ANGELGNGNI
KLSQTSNVDK EEEAVTIEMN EPVQLTFALR YLNFFTKATP LSPTVTLSMS ADVPLVVEYK
IADMGHLKYY LAPKIEDQQE GS
