ID   TDIF1_RAT               Reviewed;         327 AA.
AC   Q91Y53;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 77.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Uterus;
RA   Long X., Bigsby R.M., Nephew K.P.;
RT   "Rat novel gene identified from uterus, highly expressed in rat prostate
RT   and CNS tissue.";
RL   Submitted (FEB-2001) 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   -!- TISSUE SPECIFICITY: Expressed in thymus, bone marrow and spleen.
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; AF348701; AAK49953.1; -; mRNA.
DR   AlphaFoldDB; Q91Y53; -.
DR   BMRB; Q91Y53; -.
DR   SMR; Q91Y53; -.
DR   STRING; 10116.ENSRNOP00000020280; -.
DR   UCSC; RGD:621627; rat.
DR   RGD; 621627; Dnttip1.
DR   eggNOG; KOG4801; Eukaryota.
DR   InParanoid; Q91Y53; -.
DR   PRO; PR:Q91Y53; -.
DR   Proteomes; UP000002494; 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   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
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; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..327
FT                   /note="Deoxynucleotidyltransferase terminal-interacting
FT                   protein 1"
FT                   /id="PRO_0000072475"
FT   DNA_BIND        157..171
FT                   /note="A.T hook"
FT                   /evidence="ECO:0000305"
FT   DNA_BIND        214..235
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000305"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..146
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H147"
FT   REGION          146..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..314
FT                   /note="Important for DNA and nucleosome binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H147"
FT   MOTIF           162..168
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        146..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   327 AA;  36692 MW;  657B09069567841B CRC64;
     MGATGDTGGP RPGTESRRPG NVGNAGAAGQ PVLTNPWNIM IKPRQVQRRG RRSQMTTSFT
     DPAISMDLLR AVLQPSINEE IQSVFNKYMK FFQKAALNVR DNVGEEVDAE QLIQEACRSC
     VEQAKLLFSD GEKVIPRLAH ELPGIKRGRQ AEEESHREAP FPKRGKVGLP GHVLSNDRAA
     AGMVWKPKSC EPIRREGPKW DPARLNESTT FVLGSRANKA LGMGGTRGRI YIKHPHLFKY
     AADPQDKHWL AEQHHMRATG GKMAYLLIEE DIRDLAASDD YRGCLDLKLE ELKSFVLPSW
     MVEKMRKYME TLRTENEHRA AEATPQT