ID   TDIF1_BOVIN             Reviewed;         329 AA.
AC   A6H7A8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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; BC146175; AAI46176.1; -; mRNA.
DR   RefSeq; NP_001092346.1; NM_001098876.1.
DR   AlphaFoldDB; A6H7A8; -.
DR   BMRB; A6H7A8; -.
DR   SMR; A6H7A8; -.
DR   STRING; 9913.ENSBTAP00000022261; -.
DR   PaxDb; A6H7A8; -.
DR   PRIDE; A6H7A8; -.
DR   Ensembl; ENSBTAT00000022261; ENSBTAP00000022261; ENSBTAG00000016743.
DR   GeneID; 505524; -.
DR   KEGG; bta:505524; -.
DR   CTD; 116092; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016743; -.
DR   VGNC; VGNC:28151; DNTTIP1.
DR   eggNOG; KOG4801; Eukaryota.
DR   GeneTree; ENSGT00510000047836; -.
DR   HOGENOM; CLU_073342_0_0_1; -.
DR   InParanoid; A6H7A8; -.
DR   OMA; TENDHRA; -.
DR   OrthoDB; 622558at2759; -.
DR   TreeFam; TF329275; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000016743; Expressed in retina and 106 other tissues.
DR   ExpressionAtlas; A6H7A8; baseline.
DR   GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR   GO; GO:0000118; C:histone deacetylase complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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; IEA:Ensembl.
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_0000326136"
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..27
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          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   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H147"
SQ   SEQUENCE   329 AA;  37012 MW;  F8217ACF753BFE41 CRC64;
     MGATGDVEQP RGPGGAERGG PELGDAGAAG QLVLTNPWNI MIKHRQVQRR GRRSQMTTSF
     TDPAISMDLL RAVLQPSINE EIQTVFNKYM KFFQKAALNV RDNVGEEVDA EQLIQEACRS
     CLEQAKLLFS DGEKVIPRLT HELPGIKRGR QAEEECALRG SPIPKKRKGR PPGHILANDR
     AATGMVWKPK SCEPIRREGP KWDPARLNES TTFVLGSRAN KALGMGGTRG RIYIKHPHLF
     KYAADPQDKH WLAEQHHMRA TGGKMAYLLI EEDIRDLAAS DDYRGCLDLK LEELKSFVLP
     SWMVEKMRKY METLRTENEH RAVEAPPQT