ID   PCNA_COTJA              Reviewed;         262 AA.
AC   Q9DDF1;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Proliferating cell nuclear antigen;
DE            Short=PCNA;
GN   Name=PCNA;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Scaal M., Prols F., Fuechtbauer E.M., Christ B., Brand-Saberi B.;
RT   "BMP-2 induces cDermo-1 expression and ectopic feather development.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Component of the replisome complex
CC       (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12004}.
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; AJ301669; CAC17700.1; -; mRNA.
DR   RefSeq; NP_001310154.1; NM_001323225.1.
DR   GeneID; 107323623; -.
DR   KEGG; cjo:107323623; -.
DR   CTD; 5111; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0070557; C:PCNA-p21 complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030337; F:DNA polymerase processivity factor activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   2: Evidence at transcript 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_0000149162"
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;  28916 MW;  E04064CA65D0472A CRC64;
     MFEARLVQGS VLKRVLEALK DLITEACWDL GSGGISLQSM DSSHVSLVQL TLRSEGFDTY
     RCDRNIAMGV NLNSMSKILK CAGNEDIITL RAEDNADTLA LVFETPNQEK VSDYEMKLMD
     LDVEQLGIPE QEYSCVVKMP SAEFARICRD LSHIGDAVVI SCAKDGVKFS ANGELGNGNI
     KLSQTSNVDK EEEAVTIEMN EPVQLTFALR YLNFFTKATP LSPTVTLSMS ADVPLVVEYK
     IADMGHXKYY LAPKIEDQQE GS