TDIF1_MOUSE
ID TDIF1_MOUSE Reviewed; 328 AA.
AC Q99LB0;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 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 [MRNA].
RC TISSUE=Thymus;
RX PubMed=11473582; DOI=10.1046/j.1365-2443.2001.00449.x;
RA Yamashita N., Shimazaki N., Ibe S., Kaneko R., Tanabe A., Toyomoto T.,
RA Fujita K., Hasegawa T., Toji S., Tamai K., Yamamoto H., Koiwai O.;
RT "Terminal deoxynucleotidyltransferase directly interacts with a novel
RT nuclear protein that is homologous to p65.";
RL Genes Cells 6:641-652(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP INTERACTION WITH ZNF541, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18849567; DOI=10.1074/jbc.m805590200;
RA Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H., Park Z.Y.,
RA Eddy E.M., Cho C.;
RT "A novel germ cell-specific protein, SHIP1, forms a complex with chromatin
RT remodeling activity during spermatogenesis.";
RL J. Biol. Chem. 283:35283-35294(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: 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 (By similarity). A minor proportion may
CC form homotrimers (By similarity). Interacts with ZNF541
CC (PubMed:18849567). Interacts with the terminal
CC deoxynucleotidyltransferase DNTT (By similarity). Interacts with TRERF1
CC (By similarity). Identified in a histone deacetylase complex that
CC contains DNTTIP1, HDAC1 and MIDEAS; this complex assembles into a
CC tetramer that contains four copies of each protein chain (By
CC similarity). Component of a histone deacetylase complex containing
CC DNTTIP1, ZNF541, HDAC1 and HDAC2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H147, ECO:0000269|PubMed:18849567}.
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; AB045974; BAB82521.1; -; mRNA.
DR EMBL; BC003486; AAH03486.1; -; mRNA.
DR CCDS; CCDS17054.1; -.
DR RefSeq; NP_598524.1; NM_133763.1.
DR AlphaFoldDB; Q99LB0; -.
DR BMRB; Q99LB0; -.
DR SMR; Q99LB0; -.
DR BioGRID; 218041; 2.
DR IntAct; Q99LB0; 1.
DR MINT; Q99LB0; -.
DR STRING; 10090.ENSMUSP00000017443; -.
DR iPTMnet; Q99LB0; -.
DR PhosphoSitePlus; Q99LB0; -.
DR EPD; Q99LB0; -.
DR jPOST; Q99LB0; -.
DR MaxQB; Q99LB0; -.
DR PaxDb; Q99LB0; -.
DR PRIDE; Q99LB0; -.
DR ProteomicsDB; 262844; -.
DR Antibodypedia; 12850; 264 antibodies from 23 providers.
DR DNASU; 76233; -.
DR Ensembl; ENSMUST00000017443; ENSMUSP00000017443; ENSMUSG00000017299.
DR GeneID; 76233; -.
DR KEGG; mmu:76233; -.
DR UCSC; uc008nvx.1; mouse.
DR CTD; 116092; -.
DR MGI; MGI:1923483; Dnttip1.
DR VEuPathDB; HostDB:ENSMUSG00000017299; -.
DR eggNOG; KOG4801; Eukaryota.
DR GeneTree; ENSGT00510000047836; -.
DR HOGENOM; CLU_073342_0_0_1; -.
DR InParanoid; Q99LB0; -.
DR OMA; TENDHRA; -.
DR OrthoDB; 622558at2759; -.
DR PhylomeDB; Q99LB0; -.
DR TreeFam; TF329275; -.
DR BioGRID-ORCS; 76233; 12 hits in 71 CRISPR screens.
DR ChiTaRS; Dnttip1; mouse.
DR PRO; PR:Q99LB0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99LB0; protein.
DR Bgee; ENSMUSG00000017299; Expressed in ear vesicle and 250 other tissues.
DR ExpressionAtlas; Q99LB0; baseline and differential.
DR Genevisible; Q99LB0; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR InterPro; IPR041384; DNTTIP1_dimer.
DR InterPro; IPR026064; TdIF1.
DR PANTHER; PTHR23399; PTHR23399; 1.
DR Pfam; PF18192; DNTTIP1_dimer; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..328
FT /note="Deoxynucleotidyltransferase terminal-interacting
FT protein 1"
FT /id="PRO_0000072474"
FT DNA_BIND 158..172
FT /note="A.T hook"
FT /evidence="ECO:0000305"
FT DNA_BIND 215..236
FT /note="H-T-H motif"
FT /evidence="ECO:0000305"
FT REGION 1..30
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 142..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..315
FT /note="Important for DNA and nucleosome binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H147"
FT MOTIF 163..169
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 142..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H147"
SQ SEQUENCE 328 AA; 36852 MW; 221D334D832F9AB1 CRC64;
MGATGDTEQP RGPGGAERGG LELGDAGAAG QPVLTNPWNI MIKHRQVQRR GRRSQMTTSF
TDPAISMDLL RAVLQPSINE EIQGVFNKYM KFFQKAALNV RDNVGEEVDA EQLIQEACRS
CLEQAKLLFS DGEKVIPRLA HELPGIKRGR QAEEESHRGS PIPKKRKGRP PGHVLSNDRA
AAGMVWKQKS CEPIRREGPK WDPARLNEST TFVLGSRANK ALGMGGTRGR IYIKHPHLFK
YAADPQDKHW LAEQHHMRAT GGKMAYLLIE EDIRDLAASD DYRGCLDLKL EELKSFVLPS
WMVEKMRKYM ETLRTENEHR AAEAPPQT
