ID1_RAT
ID ID1_RAT Reviewed; 164 AA.
AC P41135;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=DNA-binding protein inhibitor ID-1;
DE AltName: Full=Inhibitor of DNA binding 1;
DE AltName: Full=Inhibitor of differentiation 1;
GN Name=Id1; Synonyms=Id-1;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=8106493; DOI=10.1016/s0021-9258(17)37665-2;
RA Springhorn J.P., Singh K., Kelly R.A., Smith T.W.;
RT "Posttranscriptional regulation of Id1 activity in cardiac muscle.
RT Alternative splicing of novel Id1 transcript permits homodimerization.";
RL J. Biol. Chem. 269:5132-5136(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=1378442; DOI=10.1016/s0021-9258(19)49720-2;
RA Springhorn J.P., Ellingsen O., Berger H.J., Kelly R.A., Smith T.W.;
RT "Transcriptional regulation in cardiac muscle. Coordinate expression of Id
RT with a neonatal phenotype during development and following a hypertrophic
RT stimulus in adult rat ventricular myocytes in vitro.";
RL J. Biol. Chem. 267:14360-14365(1992).
RN [3]
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 [4]
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. Inhibits skeletal muscle and cardiac myocyte
CC differentiation. Regulates the circadian clock by repressing the
CC transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with other HLH proteins. Interacts with COPS5,
CC IFI204, GATA4, NKX2-5, CLOCK and ARNTL/BMAL1 (By similarity). Isoform
CC Short can form homodimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=P41135-1; Sequence=Displayed;
CC Name=Short; Synonyms=ID1.25;
CC IsoId=P41135-2; Sequence=VSP_002110;
CC -!- PTM: Phosphorylated in vitro by PKA and PKC.
CC {ECO:0000269|PubMed:7864897}.
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DR EMBL; L23148; AAA20403.1; -; mRNA.
DR EMBL; D10862; BAA01633.1; -; mRNA.
DR EMBL; M86708; AAA41090.1; -; mRNA.
DR PIR; A53334; A53334.
DR PIR; JC2111; JC2111.
DR RefSeq; NP_036929.2; NM_012797.2. [P41135-2]
DR AlphaFoldDB; P41135; -.
DR SMR; P41135; -.
DR BioGRID; 247301; 4.
DR IntAct; P41135; 2.
DR STRING; 10116.ENSRNOP00000052261; -.
DR PaxDb; P41135; -.
DR GeneID; 25261; -.
DR KEGG; rno:25261; -.
DR UCSC; RGD:2858; rat. [P41135-1]
DR CTD; 3397; -.
DR RGD; 2858; Id1.
DR VEuPathDB; HostDB:ENSRNOG00000021750; -.
DR eggNOG; ENOG502RZP5; Eukaryota.
DR HOGENOM; CLU_116790_0_0_1; -.
DR InParanoid; P41135; -.
DR OMA; QMNVFLQ; -.
DR OrthoDB; 1624054at2759; -.
DR PhylomeDB; P41135; -.
DR TreeFam; TF326217; -.
DR Reactome; R-RNO-2559585; Oncogene Induced Senescence.
DR PRO; PR:P41135; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000021750; Expressed in stomach and 19 other tissues.
DR ExpressionAtlas; P41135; baseline and differential.
DR Genevisible; P41135; RN.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0070628; F:proteasome binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:RGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR GO; GO:0043621; F:protein self-association; ISO:RGD.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:RGD.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0036164; P:cell-abiotic substrate adhesion; IEP:RGD.
DR GO; GO:1903351; P:cellular response to dopamine; IEP:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP: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:0032963; P:collagen metabolic process; ISO:RGD.
DR GO; GO:0001886; P:endothelial cell morphogenesis; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0060425; P:lung morphogenesis; ISO:RGD.
DR GO; GO:0060426; P:lung vasculature development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:0043392; P:negative regulation of DNA binding; IMP:RGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP: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:0032233; P:positive regulation of actin filament bundle assembly; IMP:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR GO; GO:0045765; P:regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
DR GO; GO:1901342; P:regulation of vasculature development; IMP:RGD.
DR GO; GO:0046677; P:response to antibiotic; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; 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 Alternative splicing; Biological rhythms; Cytoplasm; Developmental protein;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..164
FT /note="DNA-binding protein inhibitor ID-1"
FT /id="PRO_0000127238"
FT DOMAIN 46..98
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT MOTIF 91..104
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT VAR_SEQ 136..164
FT /note="VRSESEYYIILLWETKATGGGCPPYFSGA -> AACVPADDRILCR (in
FT isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_002110"
FT CONFLICT 113
FT /note="G -> A (in Ref. 3; BAA01633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 17397 MW; C782DDF4C4892D6D CRC64;
MKVASSSAAA TAGPSCSLKA GRTAGEVVLG LSEQSVAISR CAGTRLPALL DEQQVNVLLY
DMNGCYSRLK ELVPTLPQNR KVSKVEILQH VIDYIRDLQL ELNSESEVAT AGGRGLPVRA
PLSTLNGEIS ALAAEVRSES EYYIILLWET KATGGGCPPY FSGA
