ID3_CANLF
ID ID3_CANLF Reviewed; 119 AA.
AC Q712G9;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA-binding protein inhibitor ID-3;
DE AltName: Full=Inhibitor of DNA binding 3;
DE AltName: Full=Inhibitor of differentiation 3;
GN Name=ID3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=12213214; DOI=10.1006/excr.2002.5589;
RA Deleu S., Savonet V., Behrends J., Dumont J., Maenhaut C.;
RT "Study of gene expression in thyrotropin-stimulated thyroid cells by cDNA
RT expression array: ID3 transcription modulating factor as an early response
RT protein and tumor marker in thyroid carcinomas.";
RL Exp. Cell Res. 279:62-70(2002).
CC -!- FUNCTION: Transcriptional regulator (lacking a basic DNA binding
CC domain) which negatively regulates the basic helix-loop-helix (bHLH)
CC transcription factors by forming heterodimers and inhibiting their DNA
CC binding and transcriptional activity. Implicated in regulating a
CC variety of cellular processes, including cellular growth, senescence,
CC differentiation, apoptosis, angiogenesis, and neoplastic
CC transformation. Involved in myogenesis by inhibiting skeletal muscle
CC and cardiac myocyte differentiation and promoting muscle precursor
CC cells proliferation. Inhibits the binding of E2A-containing protein
CC complexes to muscle creatine kinase E-box enhancer. Regulates the
CC circadian clock by repressing the transcriptional activator activity of
CC the CLOCK-ARNTL/BMAL1 heterodimer (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer, and heterodimer with other HLH proteins. Interacts
CC with COPS5 and COPS7A. Interacts with IFI204. Interacts with GATA4 and
CC NKX2-5. Interacts with ANKRD2; both proteins cooperate in myoblast
CC differentiation. Interacts with CLOCK and ARNTL/BMAL1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR EMBL; AJ271644; CAB70600.1; -; mRNA.
DR RefSeq; NP_001003025.1; NM_001003025.2.
DR AlphaFoldDB; Q712G9; -.
DR BMRB; Q712G9; -.
DR SMR; Q712G9; -.
DR STRING; 9612.ENSCAFP00000019544; -.
DR PaxDb; Q712G9; -.
DR DNASU; 403547; -.
DR Ensembl; ENSCAFT00030002632; ENSCAFP00030002344; ENSCAFG00030001473.
DR Ensembl; ENSCAFT00040003263; ENSCAFP00040002800; ENSCAFG00040001727.
DR Ensembl; ENSCAFT00845026977; ENSCAFP00845021233; ENSCAFG00845015085.
DR GeneID; 403547; -.
DR KEGG; cfa:403547; -.
DR CTD; 3399; -.
DR VEuPathDB; HostDB:ENSCAFG00845015085; -.
DR VGNC; VGNC:41862; ID3.
DR eggNOG; ENOG502S53I; Eukaryota.
DR GeneTree; ENSGT00940000160504; -.
DR InParanoid; Q712G9; -.
DR OrthoDB; 1624054at2759; -.
DR Proteomes; UP000002254; Chromosome 2.
DR Bgee; ENSCAFG00000013269; Expressed in placenta and 49 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
DR GO; GO:1901707; F:leptomycin B binding; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0072750; P:cellular response to leptomycin B; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0001656; P:metanephros development; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030903; P:notochord development; IEA:Ensembl.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR026052; DNA-bd_prot-inh.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR11723; PTHR11723; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 3: Inferred from homology;
KW Biological rhythms; Myogenesis; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..119
FT /note="DNA-binding protein inhibitor ID-3"
FT /id="PRO_0000127246"
FT DOMAIN 28..80
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
SQ SEQUENCE 119 AA; 12969 MW; 7FC38B56B4DCFFBD CRC64;
MKALSPVRGC YEAVCCLSER SLAIARGRGK GPAAEEPLSL LDDMNHCYSR LRELVPGVPR
GTQLSQVEIL QRVIDYILDL QVVLAEPAPG PPDGPHLPIQ TAELAPELVI SNDKRSFCH