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Class A basic helix-loop-helix protein 15 (bHLHa15) (Class B basic helix-loop-helix protein 8) (bHLHb8) (Muscle, intestine and stomach expression 1) (MIST-1)

 BHA15_MOUSE             Reviewed;         197 AA.
Q9QYC3; Q9QYE4;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=Class A basic helix-loop-helix protein 15;
Short=bHLHa15;
AltName: Full=Class B basic helix-loop-helix protein 8;
Short=bHLHb8;
AltName: Full=Muscle, intestine and stomach expression 1;
Short=MIST-1;
Name=Bhlha15; Synonyms=Bhlhb8, Mist1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10575209;
Pin C.L., Lemercier C., Konieczny S.F.;
"Cloning of the murine Mist1 gene and assignment to mouse chromosome
band 5G2-5G3.";
Cytogenet. Cell Genet. 86:219-222(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
Lemercier C., Konieczny S.F.;
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DEVELOPMENTAL STAGE.
PubMed=9073453; DOI=10.1006/dbio.1996.8454;
Lemercier C., To R.Q., Swanson B.J., Lyons G.E., Konieczny S.F.;
"Mist1: a novel basic helix-loop-helix transcription factor exhibits a
developmentally regulated expression pattern.";
Dev. Biol. 182:101-113(1997).
[6]
FUNCTION.
PubMed=9482738; DOI=10.1093/emboj/17.5.1412;
Lemercier C., To R.Q., Carrasco R.A., Konieczny S.F.;
"The basic helix-loop-helix transcription factor Mist1 functions as a
transcriptional repressor of myoD.";
EMBO J. 17:1412-1422(1998).
[7]
TISSUE SPECIFICITY.
PubMed=11696558; DOI=10.1083/jcb.200105060;
Pin C.L., Rukstalis J.M., Johnson C., Konieczny S.F.;
"The bHLH transcription factor Mist1 is required to maintain exocrine
pancreas cell organization and acinar cell identity.";
J. Cell Biol. 155:519-530(2001).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15003629; DOI=10.1016/j.mod.2004.01.003;
Johnson C.L., Kowalik A.S., Rajakumar N., Pin C.L.;
"Mist1 is necessary for the establishment of granule organization in
serous exocrine cells of the gastrointestinal tract.";
Mech. Dev. 121:261-272(2004).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15665001; DOI=10.1074/jbc.M411973200;
Luo X., Shin D.M., Wang X., Konieczny S.F., Muallem S.;
"Aberrant localization of intracellular organelles, Ca2+ signaling,
and exocytosis in Mist1 null mice.";
J. Biol. Chem. 280:12668-12675(2005).
[10]
FUNCTION, AND INDUCTION.
PubMed=17612490; DOI=10.1016/j.molcel.2007.06.011;
Acosta-Alvear D., Zhou Y., Blais A., Tsikitis M., Lents N.H.,
Arias C., Lennon C.J., Kluger Y., Dynlacht B.D.;
"XBP1 controls diverse cell type- and condition-specific
transcriptional regulatory networks.";
Mol. Cell 27:53-66(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12 AND THR-25, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Plays a role in controlling the transcriptional activity
of MyoD, ensuring that expanding myoblast populations remain
undifferentiated (PubMed:17612490). Repression may occur through
muscle-specific E-box occupancy by homodimers. May also negatively
regulate bHLH-mediated transcription through an N-terminal
repressor domain. Serves as a key regulator of acinar cell
function, stability, and identity. Also required for normal
organelle localization in exocrine cells and for mitochondrial
calcium ion transport. May function as a unique regulator of gene
expression in several different embryonic and postnatal cell
lineages. Binds to the E-box consensus sequence 5'-CANNTG-3'.
{ECO:0000269|PubMed:15003629, ECO:0000269|PubMed:15665001,
ECO:0000269|PubMed:17612490, ECO:0000269|PubMed:9482738}.
-!- SUBUNIT: Forms homodimers or heterodimers with TCF3 gene products
E12 and E47. These dimers bind to the E-box site, however,
heterodimer with MYOD1 does not bind target DNA.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in pancreatic tissue only in acinar
cells. There is a complete absence of expression in intra- or
interlobular pancreatic ducts and in all islet cells.
{ECO:0000269|PubMed:11696558}.
-!- DEVELOPMENTAL STAGE: First observed at E10.5 in the primitive gut
and in the developing lung bud. Expression in the gut persists
through E16.5 and remains restricted primarily to the epithelial
lining of the esophagus, stomach and intestine. Expression in the
lung is detected in the bronchial epithelium at E14.5 and at
E15.5. Expressed specifically in acinar cells during pancreatic
development. Detected in skeletal muscle tissues beginning at
E12.5, persisting throughout all embryonic stages examined
although, in older embryos expression becomes severely reduced.
{ECO:0000269|PubMed:9073453}.
-!- INDUCTION: Up-regulated by XBP1. Induced by chemical activators of
the unfolded protein response (UPR) such as tunicamycin and
thapsigargin, and also by glucose starvation (PubMed:17612490).
-!- DOMAIN: Lacks a classic transcription activation domain and
instead possesses an N-terminal region capable of inhibiting
heterologous activators.
-!- DISRUPTION PHENOTYPE: Mice display incorrect granule organization
in pancreatic acinar cells and other serous exocrine cells such as
parotid acini and gastric chief cells. They also display
mislocalization of mitochondria and Golgi apparatus and reduced
Ca(2+) uptake by mitochondria. {ECO:0000269|PubMed:15003629,
ECO:0000269|PubMed:15665001}.
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EMBL; AF091858; AAD51766.1; -; Genomic_DNA.
EMBL; AF049660; AAF17706.1; -; mRNA.
EMBL; AK020643; BAB32160.1; -; mRNA.
EMBL; BC011486; AAH11486.1; -; mRNA.
CCDS; CCDS19847.1; -.
RefSeq; NP_034930.1; NM_010800.4.
UniGene; Mm.386767; -.
ProteinModelPortal; Q9QYC3; -.
SMR; Q9QYC3; -.
BioGrid; 201426; 1.
iPTMnet; Q9QYC3; -.
PhosphoSitePlus; Q9QYC3; -.
PaxDb; Q9QYC3; -.
PRIDE; Q9QYC3; -.
Ensembl; ENSMUST00000060747; ENSMUSP00000055493; ENSMUSG00000052271.
GeneID; 17341; -.
KEGG; mmu:17341; -.
UCSC; uc009alh.1; mouse.
CTD; 168620; -.
MGI; MGI:891976; Bhlha15.
eggNOG; ENOG410KD2P; Eukaryota.
eggNOG; ENOG4111ZMK; LUCA.
GeneTree; ENSGT00680000099860; -.
HOGENOM; HOG000095227; -.
InParanoid; Q9QYC3; -.
KO; K08040; -.
OMA; HRYSTQI; -.
OrthoDB; EOG091G15AI; -.
PhylomeDB; Q9QYC3; -.
TreeFam; TF315153; -.
PRO; PR:Q9QYC3; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000052271; -.
Genevisible; Q9QYC3; MM.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0019722; P:calcium-mediated signaling; IMP:MGI.
GO; GO:0048469; P:cell maturation; IMP:MGI.
GO; GO:0007267; P:cell-cell signaling; IMP:MGI.
GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0007030; P:Golgi organization; IMP:MGI.
GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:MGI.
GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IMP:MGI.
GO; GO:0010832; P:negative regulation of myotube differentiation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 197 Class A basic helix-loop-helix protein
15.
/FTId=PRO_0000127151.
DOMAIN 72 124 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
COMPBIAS 152 189 Gln-rich.
MOD_RES 12 12 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 25 25 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 107 107 Missing (in Ref. 2; AAF17706).
{ECO:0000305}.
CONFLICT 166 166 Q -> QV (in Ref. 2; AAF17706).
{ECO:0000305}.
SEQUENCE 197 AA; 22150 MW; BB34F1EE76FEE787 CRC64;
MKTKNRPPRR RTPMQDTEAT PGEQTPDRPQ SGSGGSELTK GLRSRTARAS GGRGEVSRRR
QGSGGRRENS VQRRLESNER ERQRMHKLNN AFQALREVIP HVRADKKLSK IETLTLAKNY
IKSLTATILT MSSSRLPGLE APGPAPGPKL YQHYHHQQQQ QQQQQQVAGA MLGVTEDQPQ
GHLQRYSTQI HSFREGS


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