ID   PCNA_ANGJA              Reviewed;         260 AA.
AC   Q9W644;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Proliferating cell nuclear antigen;
DE            Short=PCNA;
GN   Name=pcna;
OS   Anguilla japonica (Japanese eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=10466934; DOI=10.1046/j.1440-169x.1999.00445.x;
RA   Miura C., Miura T., Kudo N., Yamashita M., Yamauchi K.;
RT   "cDNA cloning of a stage specific gene expressed during HCG-induced
RT   spermatogenesis in the Japanese eel.";
RL   Dev. Growth Differ. 41:463-471(1999).
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; AB025357; BAA77390.1; -; mRNA.
DR   AlphaFoldDB; Q9W644; -.
DR   SMR; Q9W644; -.
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; Ubl conjugation.
FT   CHAIN           1..260
FT                   /note="Proliferating cell nuclear antigen"
FT                   /id="PRO_0000149164"
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   260 AA;  28601 MW;  6EF845827BE6FC4E CRC64;
     MFEARLVQGS ILKKVLEALK DLITEACWDV SSSGISLQSM DSSHVSLVQL TLRSDGFDSY
     RCDRNLALGV SLNSMSKMLK CAGNEDIITL RAEDNADTLA LVFETLNQEK VSDYEMKLMD
     LDVEQLGIPE QEYSCVVKMP SGEFARICRD LSQIGDAVMI SCAKDGVMFS ASGELGTGNV
     KLSQTSNVDE EDDAVTIEMN EPVQLIFALN YLNFFTKATP LSKTVTLSMS ADIPLVVEYK
     IADMGHVKYY LAPKIDEEAS