ID   TDIF1_PONAB             Reviewed;         329 AA.
AC   Q5R595;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Deoxynucleotidyltransferase terminal-interacting protein 1;
DE   AltName: Full=Terminal deoxynucleotidyltransferase-interacting factor 1;
DE            Short=TdIF1;
DE            Short=TdT-interacting factor 1;
GN   Name=DNTTIP1; Synonyms=TDIF1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Increases DNTT terminal deoxynucleotidyltransferase activity
CC       (in vitro). Also acts as a transcriptional regulator, binding to the
CC       consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates
CC       with RAB20 promoter and positively regulates its transcription. Binds
CC       DNA and nucleosomes; may recruit HDAC1 complexes to nucleosomes or
CC       naked DNA. {ECO:0000250|UniProtKB:Q9H147}.
CC   -!- SUBUNIT: Monomer and homodimer. A minor proportion may form
CC       homotrimers. Interacts with ZNF541. Interacts with the terminal
CC       deoxynucleotidyltransferase DNTT. Interacts with TRERF1. Identified in
CC       a histone deacetylase complex that contains DNTTIP1, HDAC1 and MIDEAS;
CC       this complex assembles into a tetramer that contains four copies of
CC       each protein chain. Component of a histone deacetylase complex
CC       containing DNTTIP1, ZNF541, HDAC1 and HDAC2.
CC       {ECO:0000250|UniProtKB:Q99LB0, ECO:0000250|UniProtKB:Q9H147}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H147}.
CC   -!- DOMAIN: The N-terminal domain mediates dimerization.
CC       {ECO:0000250|UniProtKB:Q9H147}.
CC   -!- DOMAIN: The C-terminal domain mediates interaction with DNA and
CC       nucleosomes. It contains a HTH motif that mediates recognition of the
CC       consensus sequence. {ECO:0000250|UniProtKB:Q9H147}.
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DR   EMBL; CR860969; CAH93071.1; -; mRNA.
DR   RefSeq; NP_001126819.1; NM_001133347.1.
DR   AlphaFoldDB; Q5R595; -.
DR   BMRB; Q5R595; -.
DR   SMR; Q5R595; -.
DR   STRING; 9601.ENSPPYP00000012369; -.
DR   GeneID; 100173824; -.
DR   KEGG; pon:100173824; -.
DR   CTD; 116092; -.
DR   eggNOG; KOG4801; Eukaryota.
DR   HOGENOM; CLU_073342_0_0_1; -.
DR   InParanoid; Q5R595; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0000118; C:histone deacetylase complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR   InterPro; IPR041384; DNTTIP1_dimer.
DR   InterPro; IPR026064; TdIF1.
DR   PANTHER; PTHR23399; PTHR23399; 1.
DR   Pfam; PF18192; DNTTIP1_dimer; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..329
FT                   /note="Deoxynucleotidyltransferase terminal-interacting
FT                   protein 1"
FT                   /id="PRO_0000326137"
FT   DNA_BIND        159..173
FT                   /note="A.T hook"
FT                   /evidence="ECO:0000305"
FT   DNA_BIND        216..237
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000305"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..147
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H147"
FT   REGION          147..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..316
FT                   /note="Important for DNA and nucleosome binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H147"
FT   MOTIF           164..170
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        147..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H147"
SQ   SEQUENCE   329 AA;  36982 MW;  FB7828342CCCD24B CRC64;
     MGATGDAEQP RGPSGAERGG LELGDAGAAG QLVLTNPWNI MIKHRQVQRR GRRSQMTTSF
     TDPAISMDLL RAVLQPSINE EIQTVFNKYM KFFQKAALNV RDNVGEEVDA EQLIQEACRS
     CLEQAKLLFS DGEKVIPRLT HELPGIKRGR QAEEECAHRG SPLPKKRKGR PPGHILSSDR
     AAAGMVWKPK SCEPIRREGP KWDPARLNES TTFVLGSRAN KALGMGGTRG RIYIKHPHLF
     KYAADPQDKH WLAEPHHMRA TGGKMAYLLI EEDIRDLAAS DDYRGCLDLK LEELKSFVLP
     SWMVEKMRKY METLRTENEH RAVEAPPQT