PCNA_SCHPO
ID PCNA_SCHPO Reviewed; 260 AA.
AC Q03392;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Proliferating cell nuclear antigen;
DE Short=PCNA;
GN Name=pcn1; Synonyms=pcn; ORFNames=SPBC16D10.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1361173; DOI=10.1002/j.1460-2075.1992.tb05618.x;
RA Waseem N.H., Labib K., Nurse P., Lane D.P.;
RT "Isolation and analysis of the fission yeast gene encoding polymerase delta
RT accessory protein PCNA.";
RL EMBO J. 11:5111-5120(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF LEU-2 AND ARG-64.
RX PubMed=8663159; DOI=10.1074/jbc.271.27.15971;
RA Arroyo M.P., Downey K.M., So A.G., Wang T.S.;
RT "Schizosaccharomyces pombe proliferating cell nuclear antigen mutations
RT affect DNA polymerase delta processivity.";
RL J. Biol. Chem. 271:15971-15980(1996).
RN [4]
RP SUBUNIT, AND MUTAGENESIS OF LEU-68 AND GLY-69.
RX PubMed=9592143; DOI=10.1093/nar/26.11.2598;
RA Piard K., Baldacci G., Tratner I.;
RT "Single point mutations located outside the inter-monomer domains abolish
RT trimerization of Schizosaccharomyces pombe PCNA.";
RL Nucleic Acids Res. 26:2598-2605(1998).
RN [5]
RP INTERACTION WITH CDC24 AND RFC1.
RX PubMed=9891039; DOI=10.1128/mcb.19.2.1038;
RA Tanaka H., Tanaka K., Murakami H., Okayama H.;
RT "Fission yeast cdc24 is a replication factor C- and proliferating cell
RT nuclear antigen-interacting factor essential for S-phase completion.";
RL Mol. Cell. Biol. 19:1038-1048(1999).
RN [6]
RP FUNCTION, AND UBIQUITINATION AT LYS-164.
RX PubMed=16641370; DOI=10.1091/mbc.e05-11-1008;
RA Frampton J., Irmisch A., Green C.M., Neiss A., Trickey M., Ulrich H.D.,
RA Furuya K., Watts F.Z., Carr A.M., Lehmann A.R.;
RT "Postreplication repair and PCNA modification in Schizosaccharomyces
RT pombe.";
RL Mol. Biol. Cell 17:2976-2985(2006).
RN [7]
RP INTERACTION WITH RTF2.
RX PubMed=19416828; DOI=10.1073/pnas.0812323106;
RA Inagawa T., Yamada-Inagawa T., Eydmann T., Mian I.S., Wang T.S.,
RA Dalgaard J.Z.;
RT "Schizosaccharomyces pombe Rtf2 mediates site-specific replication
RT termination by inhibiting replication restart.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7927-7932(2009).
RN [8]
RP UBIQUITINATION AT LYS-164.
RX PubMed=28481910; DOI=10.1371/journal.pgen.1006789;
RA Daigaku Y., Etheridge T.J., Nakazawa Y., Nakayama M., Watson A.T.,
RA Miyabe I., Ogi T., Osborne M.A., Carr A.M.;
RT "PCNA ubiquitylation ensures timely completion of unperturbed DNA
RT replication in fission yeast.";
RL PLoS Genet. 13:e1006789-e1006789(2017).
RN [9] {ECO:0007744|PDB:6QH1}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS).
RA Kragelund B.B., Olsen J.G., Kassem N., Prestel A.;
RT "The structure of Schizosaccharomyces pombe PCNA in complex with an Spd1
RT derived peptide.";
RL Submitted (JAN-2019) to the PDB data bank.
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 (PubMed:8663159). Involved in DNA repair
CC (PubMed:16641370). {ECO:0000269|PubMed:16641370,
CC ECO:0000269|PubMed:8663159}.
CC -!- SUBUNIT: Homotrimer (PubMed:9592143). Interacts with cdc24, rfc1, and
CC rtf2 (PubMed:19416828, PubMed:9891039). {ECO:0000269|PubMed:19416828,
CC ECO:0000269|PubMed:9592143, ECO:0000269|PubMed:9891039}.
CC -!- INTERACTION:
CC Q03392; P30261: cdc27; NbExp=5; IntAct=EBI-768724, EBI-866919;
CC Q03392; Q1MTN9: rlf2; NbExp=4; IntAct=EBI-768724, EBI-1560762;
CC Q03392; Q10154: rtf2; NbExp=3; IntAct=EBI-768724, EBI-15777832;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15873}.
CC -!- PTM: Monoubiquitinated on Lys-164 by the rhp6/rhp18 complex upon DNA
CC damage, and then polyubiquitinated through 'Lys-63'-linkage by
CC ubc13/mms2 (PubMed:16641370). Ubiquitination contributes to efficient
CC DNA replication in the absence of DNA damage (PubMed:28481910).
CC {ECO:0000269|PubMed:16641370, ECO:0000269|PubMed:28481910}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
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DR EMBL; X54857; CAA38636.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB38513.1; -; Genomic_DNA.
DR PIR; S28053; WMZPET.
DR RefSeq; NP_596504.1; NM_001022425.2.
DR PDB; 6QH1; X-ray; 2.90 A; A/B/C=1-260.
DR PDBsum; 6QH1; -.
DR AlphaFoldDB; Q03392; -.
DR SMR; Q03392; -.
DR BioGRID; 276564; 44.
DR ComplexPortal; CPX-547; PCNA homotrimer.
DR DIP; DIP-33811N; -.
DR IntAct; Q03392; 11.
DR STRING; 4896.SPBC16D10.09.1; -.
DR iPTMnet; Q03392; -.
DR MaxQB; Q03392; -.
DR PaxDb; Q03392; -.
DR PRIDE; Q03392; -.
DR EnsemblFungi; SPBC16D10.09.1; SPBC16D10.09.1:pep; SPBC16D10.09.
DR GeneID; 2540020; -.
DR KEGG; spo:SPBC16D10.09; -.
DR PomBase; SPBC16D10.09; pcn1.
DR VEuPathDB; FungiDB:SPBC16D10.09; -.
DR eggNOG; KOG1636; Eukaryota.
DR HOGENOM; CLU_043978_3_0_1; -.
DR InParanoid; Q03392; -.
DR OMA; EMKLINM; -.
DR PhylomeDB; Q03392; -.
DR Reactome; R-SPO-110312; Translesion synthesis by REV1.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-110320; Translesion Synthesis by POLH.
DR Reactome; R-SPO-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-SPO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-SPO-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-SPO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-SPO-5655862; Translesion synthesis by POLK.
DR Reactome; R-SPO-5656121; Translesion synthesis by POLI.
DR Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SPO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-69091; Polymerase switching.
DR Reactome; R-SPO-69166; Removal of the Flap Intermediate.
DR Reactome; R-SPO-69183; Processive synthesis on the lagging strand.
DR Reactome; R-SPO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR PRO; PR:Q03392; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0043626; C:PCNA complex; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IC:PomBase.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IDA:PomBase.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IDA:PomBase.
DR GO; GO:0070987; P:error-free translesion synthesis; IMP:PomBase.
DR GO; GO:0042276; P:error-prone translesion synthesis; IMP:PomBase.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:1903459; P:mitotic DNA replication lagging strand elongation; IMP:PomBase.
DR GO; GO:1903460; P:mitotic DNA replication leading strand elongation; ISO:PomBase.
DR GO; GO:0045739; P:positive regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0045740; P:positive regulation of DNA replication; IC:ComplexPortal.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0006301; P:postreplication repair; IGI:PomBase.
DR GO; GO:0019985; P:translesion synthesis; IBA:GO_Central.
DR GO; GO:0070914; P:UV-damage excision repair; IDA:PomBase.
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 PANTHER; PTHR11352:SF0; PTHR11352:SF0; 1.
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 3D-structure; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..260
FT /note="Proliferating cell nuclear antigen"
FT /id="PRO_0000149175"
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 SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:28481910"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:16641370,
FT ECO:0000269|PubMed:28481910"
FT MUTAGEN 2
FT /note="L->V: Reduces capacity in enhancing the processivity
FT of DNA polymerase delta but shows no deficiency in
FT stimulation of the ATPase activity of replication factor
FT C."
FT /evidence="ECO:0000269|PubMed:8663159"
FT MUTAGEN 64
FT /note="R->A: Reduces capacity in enhancing the processivity
FT of DNA polymerase delta but shows no deficiency in
FT stimulation of the ATPase activity of replication factor
FT C."
FT /evidence="ECO:0000269|PubMed:8663159"
FT MUTAGEN 68
FT /note="L->S: Impairs homotrimerization. Reduces capacity in
FT enhancing the processivity of DNA polymerase delta."
FT /evidence="ECO:0000269|PubMed:9592143"
FT MUTAGEN 69
FT /note="G->D: Impairs homotrimerization. Reduces capacity in
FT enhancing the processivity of DNA polymerase delta."
FT /evidence="ECO:0000269|PubMed:9592143"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:6QH1"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:6QH1"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6QH1"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:6QH1"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:6QH1"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:6QH1"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:6QH1"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:6QH1"
SQ SEQUENCE 260 AA; 28969 MW; 1EE5B2A27A899C4E CRC64;
MLEARFQQAA LLKKLLDAIK ELVTDANFDC NDNGISLQAM DSSHVALVSM LIKSDGFEPY
RCDRNIALGI NLNALSKVLR CAQNEDLVTL KAEDTPEVLN LVFESEKNDR ISDYDVKLMD
IDQEHLGIPD IEYDATITMP AAEFQRITRD LLTLSDSVTI NASKEGVRFS CKGDIGNGST
TLKQHTDLSD QDQSIEISLT QAVTLTFSLK YLAQFTKATP LATRVTLSMS NDVPLLVEYK
MESGFLRFYL APKIGEEDEE
