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ID3_RAT
ID   ID3_RAT                 Reviewed;         119 AA.
AC   P41138;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 142.
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; Synonyms=Id-3;
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].
RX   PubMed=7908517; DOI=10.1006/bbrc.1994.1380;
RA   Nagata Y., Todokoro K.;
RT   "Activation of helix-loop-helix proteins Id1, Id2 and Id3 during neural
RT   differentiation.";
RL   Biochem. Biophys. Res. Commun. 199:1355-1362(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   PHOSPHORYLATION.
RX   PubMed=7864897; DOI=10.1006/bbrc.1995.1273;
RA   Nagata Y., Shoji W., Obinata M., Todokoro K.;
RT   "Phosphorylation of helix-loop-helix proteins ID1, ID2 and ID3.";
RL   Biochem. Biophys. Res. Commun. 207:916-926(1995).
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.
CC   -!- PTM: Phosphorylated in vitro by CDC2 and PKC.
CC       {ECO:0000269|PubMed:7864897}.
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DR   EMBL; D10864; BAA01635.1; -; mRNA.
DR   EMBL; BC064658; AAH64658.1; -; mRNA.
DR   PIR; JC2113; JC2113.
DR   RefSeq; NP_037190.1; NM_013058.2.
DR   AlphaFoldDB; P41138; -.
DR   SMR; P41138; -.
DR   BioGRID; 247615; 4.
DR   STRING; 10116.ENSRNOP00000035270; -.
DR   PhosphoSitePlus; P41138; -.
DR   PaxDb; P41138; -.
DR   Ensembl; ENSRNOT00000035788; ENSRNOP00000035270; ENSRNOG00000026124.
DR   GeneID; 25585; -.
DR   KEGG; rno:25585; -.
DR   UCSC; RGD:2860; rat.
DR   CTD; 3399; -.
DR   RGD; 2860; Id3.
DR   eggNOG; ENOG502S53I; Eukaryota.
DR   GeneTree; ENSGT00940000160504; -.
DR   HOGENOM; CLU_116790_1_0_1; -.
DR   InParanoid; P41138; -.
DR   OMA; PARGCYE; -.
DR   OrthoDB; 1624054at2759; -.
DR   PhylomeDB; P41138; -.
DR   TreeFam; TF326217; -.
DR   PRO; PR:P41138; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000026124; Expressed in thymus and 19 other tissues.
DR   Genevisible; P41138; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD.
DR   GO; GO:1901707; F:leptomycin B binding; ISO:RGD.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:RGD.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0072750; P:cellular response to leptomycin B; ISO:RGD.
DR   GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0001656; P:metanephros development; ISO:RGD.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; TAS:RGD.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; ISO:RGD.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR   GO; GO:0030903; P:notochord development; ISO:RGD.
DR   GO; GO:0042476; P:odontogenesis; ISO:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:RGD.
DR   GO; GO:0006275; P:regulation of DNA replication; IMP:RGD.
DR   GO; GO:0009611; P:response to wounding; IEP:RGD.
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   1: Evidence at protein level;
KW   Biological rhythms; Myogenesis; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..119
FT                   /note="DNA-binding protein inhibitor ID-3"
FT                   /id="PRO_0000127249"
FT   DOMAIN          28..80
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
SQ   SEQUENCE   119 AA;  13059 MW;  A8B6AC04D2C9A5A4 CRC64;
     MKALSPVRGC YEAVCCLSER SLAIARGRGK SPSAEEPLSL LDDMNHCYSR LRELVPGVPR
     GTQLSQVEIL QRVIDYILDL QVVLAEPAPG PPDGPHLPIQ TAELTPELVI SKDKRSFCH
 
 
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