PCNA1_PLAF7
ID PCNA1_PLAF7 Reviewed; 274 AA.
AC P61074; A0A5K1K8U9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Proliferating cell nuclear antigen 1 {ECO:0000303|PubMed:18554328};
DE Short=PfPCNA1 {ECO:0000303|PubMed:18554328};
GN Name=PCNA1 {ECO:0000303|PubMed:18554328};
GN Synonyms=PCNA {ECO:0000303|PubMed:18554328};
GN ORFNames=PF13_0328, PF3D7_1361900;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3]
RP INTERACTION WITH ORC1 AND ORC5, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18554328; DOI=10.1111/j.1365-2958.2008.06316.x;
RA Gupta A., Mehra P., Dhar S.K.;
RT "Plasmodium falciparum origin recognition complex subunit 5: functional
RT characterization and role in DNA replication foci formation.";
RL Mol. Microbiol. 69:646-665(2008).
RN [4]
RP INTERACTION WITH ORC1, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19633266; DOI=10.1128/ec.00170-09;
RA Gupta A., Mehra P., Deshmukh A., Dar A., Mitra P., Roy N., Dhar S.K.;
RT "Functional dissection of the catalytic carboxyl-terminal domain of origin
RT recognition complex subunit 1 (PfORC1) of the human malaria parasite
RT Plasmodium falciparum.";
RL Eukaryot. Cell 8:1341-1351(2009).
RN [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH ORC1 AND FEN1, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=26251451; DOI=10.1042/bj20150452;
RA Mitra P., Banu K., Deshmukh A.S., Subbarao N., Dhar S.K.;
RT "Functional dissection of proliferating-cell nuclear antigens (1 and 2) in
RT human malarial parasite Plasmodium falciparum: possible involvement in DNA
RT replication and DNA damage response.";
RL Biochem. J. 470:115-129(2015).
RN [6]
RP SUBUNIT, AND MUTAGENESIS OF SER-191 AND TYR-213.
RX PubMed=30052905; DOI=10.1093/femsle/fny182;
RA Banu K., Mitra P., Subbarao N., Dhar S.K.;
RT "Role of tyrosine residue (Y213) in nuclear retention of PCNA1 in human
RT malaria parasite Plasmodium falciparum.";
RL FEMS Microbiol. Lett. 365:0-0(2018).
CC -!- FUNCTION: Auxiliary protein of DNA polymerase delta and is involved in
CC the control of DNA replication by increasing the polymerase
CC processibility during elongation of the leading strand (By similarity).
CC Involved in DNA damage response (PubMed:26251451).
CC {ECO:0000250|UniProtKB:P31008, ECO:0000269|PubMed:26251451}.
CC -!- SUBUNIT: Homotrimer (PubMed:26251451, PubMed:30052905). Interacts with
CC ORC1 (via PIP-box motif); the interaction occurs during DNA replication
CC in trophozoites (PubMed:18554328, PubMed:26251451). Interacts with
CC ORC5; the interaction occurs during the trophozoite stage but not at
CC the late schizont stage (PubMed:18554328, PubMed:19633266,
CC PubMed:26251451). Interacts with FEN1 (PubMed:26251451).
CC {ECO:0000269|PubMed:18554328, ECO:0000269|PubMed:19633266,
CC ECO:0000269|PubMed:26251451, ECO:0000269|PubMed:30052905}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18554328,
CC ECO:0000269|PubMed:19633266, ECO:0000269|PubMed:26251451}. Chromosome
CC {ECO:0000269|PubMed:26251451}. Cytoplasm {ECO:0000269|PubMed:26251451}.
CC Note=During early-to mid replicating trophozoite stages, colocalizes
CC with ORC1 and ORC5 to distinct nuclear foci which probably are DNA
CC replication origin sites (PubMed:18554328, PubMed:19633266,
CC PubMed:26251451). Dissociates from ORC1 and ORC5 during the late
CC schizont stage (PubMed:18554328, PubMed:19633266).
CC {ECO:0000269|PubMed:18554328, ECO:0000269|PubMed:19633266,
CC ECO:0000269|PubMed:26251451}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage,
CC specifically during the trophozoite and schizont stages (at protein
CC level). {ECO:0000269|PubMed:18554328, ECO:0000269|PubMed:19633266,
CC ECO:0000269|PubMed:26251451}.
CC -!- INDUCTION: Induced by DNA damage (at protein level).
CC {ECO:0000269|PubMed:26251451}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
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DR EMBL; AL844509; VWP77936.1; -; Genomic_DNA.
DR RefSeq; XP_001350330.1; XM_001350294.1.
DR AlphaFoldDB; P61074; -.
DR SMR; P61074; -.
DR STRING; 5833.PF13_0328; -.
DR SwissPalm; P61074; -.
DR PRIDE; P61074; -.
DR EnsemblProtists; CAD52739; CAD52739; PF3D7_1361900.
DR GeneID; 814288; -.
DR KEGG; pfa:PF3D7_1361900; -.
DR VEuPathDB; PlasmoDB:PF3D7_1361900; -.
DR HOGENOM; CLU_043978_3_0_1; -.
DR InParanoid; P61074; -.
DR OMA; EMKLINM; -.
DR PhylomeDB; P61074; -.
DR Reactome; R-PFA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-PFA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-PFA-69091; Polymerase switching.
DR Reactome; R-PFA-69166; Removal of the Flap Intermediate.
DR Reactome; R-PFA-69183; Processive synthesis on the lagging strand.
DR Proteomes; UP000001450; Chromosome 13.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043626; C:PCNA complex; IBA:GO_Central.
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:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR GO; GO:0019985; P:translesion synthesis; IBA:GO_Central.
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 Chromosome; Cytoplasm; DNA replication; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..274
FT /note="Proliferating cell nuclear antigen 1"
FT /id="PRO_0000149173"
FT DNA_BIND 61..80
FT /evidence="ECO:0000255"
FT SITE 213
FT /note="May be important for nuclear localization"
FT /evidence="ECO:0000305|PubMed:30052905"
FT MUTAGEN 191
FT /note="S->A: No effect on homotrimerization and stability.
FT Slight reduction in protein stability; when associated with
FT F-213."
FT /evidence="ECO:0000269|PubMed:30052905"
FT MUTAGEN 213
FT /note="Y->F: No effect on homotrimerization and stability.
FT Slight reduction in protein stability; when associated with
FT A-191."
FT /evidence="ECO:0000269|PubMed:30052905"
SQ SEQUENCE 274 AA; 30587 MW; E3128F7397DD1687 CRC64;
MLEAKLNNAS ILKKLFECIK DLVNDANVDA DESGLKLQAL DGNHVSLVSL HLLDSGFSHY
RCDRERVLGV NIASLNKVFK LCGANESVVI SSKDDEDNLN FVFENNKEDK VTNFSLKLMS
IELDSLNIPD CEEGFDAEVE LSSKELTNIF RNLSEFSDTV FIEIDSNCIK FTTKGIVGDA
EVALKPRDST SEDDIGVTIK SKKKIKQSFA IKYLNLFSKS NILADVVVLG LSDSRPIEFK
YEIKDTSPDS DTLKIGFVKF FLAPKMDDDM DNKD
