BHA15_RAT
ID BHA15_RAT Reviewed; 197 AA.
AC P70562;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Class A basic helix-loop-helix protein 15;
DE Short=bHLHa15;
DE AltName: Full=Class B basic helix-loop-helix protein 8;
DE Short=bHLHb8;
DE AltName: Full=Muscle, intestine and stomach expression 1;
DE Short=MIST-1;
GN Name=Bhlha15; Synonyms=Bhlhb8, Mist1;
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], TISSUE SPECIFICITY, AND CHARACTERIZATION.
RC STRAIN=Sprague-Dawley; TISSUE=Olfactory epithelium;
RX PubMed=9073453; DOI=10.1006/dbio.1996.8454;
RA Lemercier C., To R.Q., Swanson B.J., Lyons G.E., Konieczny S.F.;
RT "Mist1: a novel basic helix-loop-helix transcription factor exhibits a
RT developmentally regulated expression pattern.";
RL Dev. Biol. 182:101-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=10721714; DOI=10.1016/s0378-1119(99)00523-5;
RA Lemercier C., Brown A., Mamani M., Ripoche J., Reiffers J.;
RT "The rat Mist1 gene: structure and promoter characterization.";
RL Gene 242:209-218(2000).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in controlling the transcriptional activity of
CC MyoD, ensuring that expanding myoblast populations remain
CC undifferentiated. Repression may occur through muscle-specific E-box
CC occupancy by homodimers. May also negatively regulate bHLH-mediated
CC transcription through an N-terminal repressor domain. Serves as a key
CC regulator of acinar cell function, stability, and identity. Also
CC required for normal organelle localization in exocrine cells and for
CC mitochondrial calcium ion transport. May function as a unique regulator
CC of gene expression in several different embryonic and postnatal cell
CC lineages. Binds to the E-box consensus sequence 5'-CANNTG-3' (By
CC similarity). {ECO:0000250|UniProtKB:Q9QYC3}.
CC -!- SUBUNIT: Forms homodimers or heterodimers with TCF3 gene products E12
CC and E47. These dimers bind to the E-box site, however, heterodimer with
CC MYOD1 does not bind target DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, spleen and olfactory
CC epithelium. Weaker expression is seen in skeletal muscle, cardiac
CC muscle, eye and brain tissue. {ECO:0000269|PubMed:9073453}.
CC -!- DOMAIN: Lacks a classic transcription activation domain and instead
CC possesses an N-terminal region capable of inhibiting heterologous
CC activators. {ECO:0000250}.
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DR EMBL; U58279; AAC53111.1; -; mRNA.
DR EMBL; AF049874; AAF17707.1; -; Genomic_DNA.
DR EMBL; BC061868; AAH61868.1; -; mRNA.
DR RefSeq; NP_036995.1; NM_012863.1.
DR AlphaFoldDB; P70562; -.
DR SMR; P70562; -.
DR BioGRID; 247373; 1.
DR STRING; 10116.ENSRNOP00000035219; -.
DR iPTMnet; P70562; -.
DR PhosphoSitePlus; P70562; -.
DR PaxDb; P70562; -.
DR PRIDE; P70562; -.
DR GeneID; 25334; -.
DR KEGG; rno:25334; -.
DR CTD; 168620; -.
DR RGD; 3091; Bhlha15.
DR VEuPathDB; HostDB:ENSRNOG00000025164; -.
DR eggNOG; KOG3898; Eukaryota.
DR HOGENOM; CLU_097977_2_0_1; -.
DR InParanoid; P70562; -.
DR OMA; HRYSTQI; -.
DR OrthoDB; 1528350at2759; -.
DR PhylomeDB; P70562; -.
DR TreeFam; TF315153; -.
DR PRO; PR:P70562; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000025164; Expressed in pancreas and 10 other tissues.
DR Genevisible; P70562; RN.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0007267; P:cell-cell signaling; ISO:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:RGD.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
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 DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..197
FT /note="Class A basic helix-loop-helix protein 15"
FT /id="PRO_0000127152"
FT DOMAIN 72..124
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC3"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 197 AA; 22196 MW; 067AEAC33B5D49CE CRC64;
MKTKNRPPRR RTPMQDAEAT PGEQTPDRSQ SGSGASEVTK GLRSRTARAS GTRAEVSRRR
QGSSSRRENS VQRRLESNER ERQRMHKLNN AFQALREVIP HVRADKKLSK IETLTLAKNY
IKSLTATILT MSSSRLPGLE APGPAPGPKL YQHYHHQQQQ QQQQQQVAGA VLGVTEDQPQ
GHLQRYSTQI HSFREGS
