PDIP2_MOUSE
ID PDIP2_MOUSE Reviewed; 368 AA.
AC Q91VA6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Polymerase delta-interacting protein 2 {ECO:0000250|UniProtKB:Q9Y2S7};
DE Flags: Precursor;
GN Name=Poldip2 {ECO:0000312|MGI:MGI:1915061};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in DNA damage tolerance by regulating translesion
CC synthesis (TLS) of templates carrying DNA damage lesions such as 8oxoG
CC and abasic sites. May act by stimulating activity of DNA polymerases
CC involved in TLS, such as PRIMPOL and polymerase delta (POLD1).
CC {ECO:0000250|UniProtKB:Q9Y2S7}.
CC -!- SUBUNIT: Interacts with PCNA and POLD2. Interacts with SSBP1. Interacts
CC with PRIMPOL; leading to enhance DNA polymerase activity of PRIMPOL.
CC Interacts with POLH. Interacts with POLD1; leading to stimulate DNA
CC polymerase activity of POLD1. {ECO:0000250|UniProtKB:Q9Y2S7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9Y2S7}. Nucleus {ECO:0000250|UniProtKB:Q9Y2S7}.
CC Note=Mainly localizes to the mitochondrial matrix; a small fraction
CC localizes in the nucleus. {ECO:0000250|UniProtKB:Q9Y2S7}.
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; BC006833; AAH06833.1; -; mRNA.
DR EMBL; BC012879; AAH12879.1; -; mRNA.
DR CCDS; CCDS25109.1; -.
DR RefSeq; NP_080665.1; NM_026389.3.
DR AlphaFoldDB; Q91VA6; -.
DR SMR; Q91VA6; -.
DR BioGRID; 212455; 5.
DR STRING; 10090.ENSMUSP00000001127; -.
DR iPTMnet; Q91VA6; -.
DR PhosphoSitePlus; Q91VA6; -.
DR SwissPalm; Q91VA6; -.
DR EPD; Q91VA6; -.
DR jPOST; Q91VA6; -.
DR MaxQB; Q91VA6; -.
DR PaxDb; Q91VA6; -.
DR PeptideAtlas; Q91VA6; -.
DR PRIDE; Q91VA6; -.
DR ProteomicsDB; 288082; -.
DR Antibodypedia; 69152; 221 antibodies from 30 providers.
DR DNASU; 67811; -.
DR Ensembl; ENSMUST00000001127; ENSMUSP00000001127; ENSMUSG00000001100.
DR GeneID; 67811; -.
DR KEGG; mmu:67811; -.
DR UCSC; uc007kjo.1; mouse.
DR CTD; 26073; -.
DR MGI; MGI:1915061; Poldip2.
DR VEuPathDB; HostDB:ENSMUSG00000001100; -.
DR eggNOG; KOG4408; Eukaryota.
DR GeneTree; ENSGT00940000153571; -.
DR HOGENOM; CLU_051858_0_0_1; -.
DR InParanoid; Q91VA6; -.
DR OMA; MGCRESQ; -.
DR OrthoDB; 805515at2759; -.
DR PhylomeDB; Q91VA6; -.
DR TreeFam; TF314882; -.
DR BioGRID-ORCS; 67811; 9 hits in 72 CRISPR screens.
DR ChiTaRS; Poldip2; mouse.
DR PRO; PR:Q91VA6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91VA6; protein.
DR Bgee; ENSMUSG00000001100; Expressed in spermatocyte and 275 other tissues.
DR ExpressionAtlas; Q91VA6; baseline and differential.
DR Genevisible; Q91VA6; MM.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0070987; P:error-free translesion synthesis; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:MGI.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:MGI.
DR GO; GO:1904531; P:positive regulation of actin filament binding; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:MGI.
DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; IEA:Ensembl.
DR GO; GO:2001108; P:positive regulation of Rho guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR Gene3D; 2.60.40.1470; -; 1.
DR InterPro; IPR007474; ApaG_domain.
DR InterPro; IPR036767; ApaG_sf.
DR InterPro; IPR011722; Hemimethylated_DNA-bd_dom.
DR InterPro; IPR036623; Hemimethylated_DNA-bd_sf.
DR Pfam; PF04379; DUF525; 1.
DR Pfam; PF08755; YccV-like; 1.
DR SMART; SM00992; YccV-like; 1.
DR SUPFAM; SSF110069; SSF110069; 1.
DR SUPFAM; SSF141255; SSF141255; 1.
DR PROSITE; PS51087; APAG; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..368
FT /note="Polymerase delta-interacting protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000197976"
FT DOMAIN 235..360
FT /note="ApaG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00412"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2S7"
SQ SEQUENCE 368 AA; 41870 MW; 4A399A13C795FCBB CRC64;
MAGCVARRAL AVGSRWWSRS LATTRGSRPL CAVGGAGGLP PVATATTRRH LSSRNRAEGK
VLETVGVFEV PKQNGKYETG QLFLHSVFGY RGVVLFPWQA RLYDRDVASA TPEKAENPAG
HGSKEVKGKT HTYYQVLIDA RDCPHISQRS QTEAVTFLAN HDDSRALYAI PGLDYVSHED
ILPYTSTDQV PIQHELFERF LLYDQTKAPP FVARETLRAW QEKNHPWLEL SDVHRETTEN
IRVTVIPFYM GMREAQNSHV YWWRYCIRLE NLDSDVVQLR ERHWRIFSLS GTLETVRGRG
VVGREPVLSK EQPAFQYSSH VSLQASSGHM WGTFRFERPD GSHFDVRIPP FSLESNKDEK
TPPSGLHW
