ID2_BOVIN
ID ID2_BOVIN Reviewed; 134 AA.
AC Q3ZC46;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DNA-binding protein inhibitor ID-2;
DE AltName: Full=Inhibitor of DNA binding 2;
DE AltName: Full=Inhibitor of differentiation 2;
GN Name=ID2;
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=Pancreas;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Inhibits skeletal muscle and cardiac myocyte
CC differentiation. Regulates the circadian clock by repressing the
CC transcriptional activator activity of the CLOCK-ARNTL/BMAL1
CC heterodimer. Restricts the CLOCK and ARNTL/BMAL1 localization to the
CC cytoplasm. Plays a role in both the input and output pathways of the
CC circadian clock: in the input component, is involved in modulating the
CC magnitude of photic entrainment and in the output component,
CC contributes to the regulation of a variety of liver clock-controlled
CC genes involved in lipid metabolism (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with other HLH proteins. Interacts with GATA4,
CC IFI204, NR0B2 and NKX2-5. Interacts with CLOCK and ARNTL/BMAL1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41136}. Nucleus
CC {ECO:0000250|UniProtKB:P41136}.
CC -!- DOMAIN: The bHLH domain is essential for its repressor activity towards
CC the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000250}.
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DR EMBL; BC102921; AAI02922.1; -; mRNA.
DR RefSeq; NP_001029403.1; NM_001034231.2.
DR RefSeq; XP_005212992.1; XM_005212935.3.
DR AlphaFoldDB; Q3ZC46; -.
DR SMR; Q3ZC46; -.
DR STRING; 9913.ENSBTAP00000028235; -.
DR PaxDb; Q3ZC46; -.
DR PRIDE; Q3ZC46; -.
DR Ensembl; ENSBTAT00000028235; ENSBTAP00000028235; ENSBTAG00000021187.
DR GeneID; 505025; -.
DR KEGG; bta:505025; -.
DR CTD; 3398; -.
DR VEuPathDB; HostDB:ENSBTAG00000021187; -.
DR VGNC; VGNC:59229; ID2.
DR eggNOG; ENOG502RZP5; Eukaryota.
DR GeneTree; ENSGT00940000156464; -.
DR HOGENOM; CLU_116790_2_1_1; -.
DR InParanoid; Q3ZC46; -.
DR OMA; SFRKNGA; -.
DR OrthoDB; 1624054at2759; -.
DR TreeFam; TF326217; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000021187; Expressed in mammary gland fat and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB.
DR GO; GO:0061031; P:endodermal digestive tract morphogenesis; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0061030; P:epithelial cell differentiation involved in mammary gland alveolus development; ISS:UniProtKB.
DR GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
DR GO; GO:0060749; P:mammary gland alveolus development; ISS:UniProtKB.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048663; P:neuron fate commitment; ISS:UniProtKB.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Biological rhythms; Cytoplasm; Developmental protein; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..134
FT /note="DNA-binding protein inhibitor ID-2"
FT /id="PRO_0000127239"
FT DOMAIN 23..75
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 106..115
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02363"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41136"
SQ SEQUENCE 134 AA; 14860 MW; F8748B9954C3172B CRC64;
MKAFSPVRSV RKNSLSDHGL GISRSKTPVD DPMSLLYNMN DCYSKLKELV PSIPQNKKVS
KMEILQHVID YILDLQIALD SHPTIVSLHH QRPGQSQASR TPLTTLNTDI SILSLQASEF
PSELMSNDSK ALCG
