ID   PAF15_XENLA             Reviewed;         123 AA.
AC   Q5HZL4;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=PCNA-associated factor {ECO:0000305};
DE   AltName: Full=PCNA-associated factor of 15 kDa;
DE            Short=PAF15;
DE            Short=p15PAF;
DE   AltName: Full=PCNA-clamp-associated factor {ECO:0000250|UniProtKB:Q15004};
GN   Name=pclaf {ECO:0000250|UniProtKB:Q15004}; Synonyms=paf;
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 [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PCNA-binding protein that acts as a regulator of DNA repair
CC       during DNA replication. Following DNA damage, the interaction with pcna
CC       is disrupted, facilitating the interaction between monoubiquitinated
CC       pcna and the translesion DNA synthesis DNA polymerase eta (polh) at
CC       stalled replisomes, facilitating the bypass of replication-fork-
CC       blocking lesions. Also acts as a regulator of centrosome number (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with pcna. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15004}.
CC       Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q15004}.
CC       Note=Following DNA damage, localizes to DNA damage sites. Colocalizes
CC       with centrosomes in perinuclear region. {ECO:0000250|UniProtKB:Q15004}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC088968; AAH88968.1; -; mRNA.
DR   RefSeq; NP_001088983.1; NM_001095514.1.
DR   AlphaFoldDB; Q5HZL4; -.
DR   BioGRID; 106445; 2.
DR   DNASU; 496365; -.
DR   GeneID; 496365; -.
DR   KEGG; xla:496365; -.
DR   CTD; 496365; -.
DR   Xenbase; XB-GENE-6486199; pclaf.S.
DR   OMA; NRCISDS; -.
DR   OrthoDB; 1508906at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 496365; Expressed in oocyte and 15 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR   GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR   InterPro; IPR040444; PCNA-AF.
DR   InterPro; IPR031444; PCNA-AF_dom.
DR   PANTHER; PTHR15679; PTHR15679; 1.
DR   Pfam; PF15715; PAF; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA damage; DNA repair; Nucleus; Reference proteome.
FT   CHAIN           1..123
FT                   /note="PCNA-associated factor"
FT                   /id="PRO_0000420482"
FT   REGION          1..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           26..37
FT                   /note="D-box"
FT   MOTIF           66..77
FT                   /note="PIP-box"
FT   MOTIF           83..85
FT                   /note="KEN box"
FT   MOTIF           93..105
FT                   /note="Initiation motif"
FT   COMPBIAS        27..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   123 AA;  12772 MW;  4C733B5C855BB5B2 CRC64;
     MVRTKADCAG SSSGSYRKAV AARAPRKTFG SSSSGSNHDT SPTGKKSECK YAGGNPVCVR
     PIPTWQKGIG DFFGSPSTSQ PEKENRIPSD DEEAGGSGAG KKPRKSRPLP PDPSEEAADS
     GDE