ID   PCNA_XENLA              Reviewed;         261 AA.
AC   P18248;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Proliferating cell nuclear antigen;
DE            Short=PCNA;
DE   AltName: Full=Cyclin;
GN   Name=pcna;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=1697269; DOI=10.1016/0012-1606(90)90113-w;
RA   Leibovici M., Gusse M., Bravo R., Mechali M.;
RT   "Characterization and developmental expression of Xenopus proliferating
RT   cell nuclear antigen (PCNA).";
RL   Dev. Biol. 141:183-192(1990).
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.
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:0000269|PubMed:1697269}.
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; M34080; AAA49926.1; -; mRNA.
DR   PIR; A37357; A37357.
DR   AlphaFoldDB; P18248; -.
DR   SMR; P18248; -.
DR   ComplexPortal; CPX-552; PCNA homotrimer.
DR   ELM; P18248; -.
DR   Proteomes; UP000186698; Genome assembly.
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:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
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..261
FT                   /note="Proliferating cell nuclear antigen"
FT                   /id="PRO_0000149167"
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   261 AA;  28897 MW;  CC371F82B612E900 CRC64;
     MFEARLVQGS ILKKVLEALK DLIDEACWDI TSSGISLQSM DSSHVSLVQL TLRSDGFDTY
     RCDRNQSIGV KMSSMSKILK CAASDDIITL RAEDNADTVT MVFESPNQEK VSDYEMKLMD
     LDVEQLGIPE QEYSCVIKMP SGEFARICRD LSQIGDAVVI SCAKDGVKFS ASGELGTGNV
     KLSQTSNVDK EEEAVTIEMN EPVQLTFALR YLNFFTKATP LSPTVILSMS ADIPLVVEYK
     IADMEHVKYY LAPKIEDEEA S