NDF1_MESAU
ID NDF1_MESAU Reviewed; 355 AA.
AC Q60430;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Neurogenic differentiation factor 1;
DE Short=NeuroD1;
DE AltName: Full=Beta-cell E-box transcriptional activator 2;
DE Short=Beta2;
GN Name=NEUROD1; Synonyms=NEUROD;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7774807; DOI=10.1101/gad.9.8.1009;
RA Naya F.J., Stellrecht C.M.M., Tsai M.-J.;
RT "Tissue-specific regulation of the insulin gene by a novel basic helix-
RT loop-helix transcription factor.";
RL Genes Dev. 9:1009-1019(1995).
RN [2]
RP INTERACTION WITH RREB1.
RX PubMed=12482979; DOI=10.1128/mcb.23.1.259-271.2003;
RA Ray S.K., Nishitani J., Petry M.W., Fessing M.Y., Leiter A.B.;
RT "Novel transcriptional potentiation of BETA2/NeuroD on the secretin gene
RT promoter by the DNA-binding protein Finb/RREB-1.";
RL Mol. Cell. Biol. 23:259-271(2003).
CC -!- FUNCTION: Acts as a transcriptional activator: mediates transcriptional
CC activation by binding to E box-containing promoter consensus core
CC sequences 5'-CANNTG-3'. Associates with the p300/CBP transcription
CC coactivator complex to stimulate transcription of the secretin gene as
CC well as the gene encoding the cyclin-dependent kinase inhibitor CDKN1A.
CC Contributes to the regulation of several cell differentiation pathways,
CC like those that promote the formation of early retinal ganglion cells,
CC inner ear sensory neurons, granule cells forming either the cerebellum
CC or the dentate gyrus cell layer of the hippocampus, endocrine islet
CC cells of the pancreas and enteroendocrine cells of the small intestine.
CC Together with PAX6 or SIX3, is required for the regulation of amacrine
CC cell fate specification. Also required for dendrite morphogenesis and
CC maintenance in the cerebellar cortex. Associates with chromatin to
CC enhancer regulatory elements in genes encoding key transcriptional
CC regulators of neurogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q60867}.
CC -!- SUBUNIT: Efficient DNA-binding requires dimerization with another bHLH
CC protein. Heterodimer with TCF3/E47; the heterodimer is inhibited in
CC presence of ID2, but not NR0B2, to E-box element. Interacts with EP300;
CC the interaction is inhibited by NR0B2 (By similarity). Interacts with
CC RREB1 (PubMed:12482979). Interacts with ATOH8 (By similarity).
CC {ECO:0000250|UniProtKB:Q60867, ECO:0000269|PubMed:12482979}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=In pancreatic islet cells,
CC shuttles to the nucleus in response to glucose stimulation. Colocalizes
CC with NR0B2 in the nucleus (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Most abundant in pancreatic alpha- and beta-cells,
CC less in brain and intestine.
CC -!- PTM: Phosphorylated. In islet cells, phosphorylated on Ser-273 upon
CC glucose stimulation; which may be required for nuclear localization. In
CC activated neurons, phosphorylated on Ser-334; which promotes dendritic
CC growth. Phosphorylated by MAPK1; phosphorylation regulates
CC heterodimerization and DNA-binding activities. Phosphorylation on Ser-
CC 265 and Ser-273 increases transactivation on the insulin promoter in
CC glucose-stimulated insulinoma cells (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA86518.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U24679; AAA86518.1; ALT_INIT; mRNA.
DR PIR; A57059; A57059.
DR RefSeq; XP_005065174.1; XM_005065117.2.
DR AlphaFoldDB; Q60430; -.
DR SMR; Q60430; -.
DR STRING; 10036.XP_005065174.1; -.
DR GeneID; 101829221; -.
DR CTD; 4760; -.
DR eggNOG; KOG3898; Eukaryota.
DR OrthoDB; 1096531at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0035881; P:amacrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; ISS:UniProtKB.
DR GO; GO:0021542; P:dentate gyrus development; ISS:UniProtKB.
DR GO; GO:0048562; P:embryonic organ morphogenesis; IEA:Ensembl.
DR GO; GO:0031018; P:endocrine pancreas development; ISS:UniProtKB.
DR GO; GO:0035883; P:enteroendocrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IEA:InterPro.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0003326; P:pancreatic A cell fate commitment; IEA:Ensembl.
DR GO; GO:0003329; P:pancreatic PP cell fate commitment; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0060730; P:regulation of intestinal epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR032652; Neurod1.
DR InterPro; IPR022575; Neurogenic_DUF.
DR InterPro; IPR016637; TF_bHLH_NeuroD.
DR PANTHER; PTHR19290:SF88; PTHR19290:SF88; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF12533; Neuro_bHLH; 1.
DR PIRSF; PIRSF015618; bHLH_NeuroD; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..355
FT /note="Neurogenic differentiation factor 1"
FT /id="PRO_0000127382"
FT DOMAIN 100..152
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 86..92
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 27..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60867"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60867"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60867"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60867"
FT MOD_RES 334
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:Q64289"
SQ SEQUENCE 355 AA; 39763 MW; F4344DFD360226B2 CRC64;
MTKSYSESGL MGEPQPQGPP SWTDECLSSQ DEDHEADKKE DELEAMNAEE DSLRNGGDEE
DEDEDLEEED EEEEEDDQKP KRRGPKKKKM TKARLERFKL RRMKANARER NRMHGLNAAL
DNLRKVVPCY SKTQKLSKIE TLRLAKNYIW ALSEILRSGK SPDLVSFVQT LCKGLSQPTT
NLVAGCLQLN PRTFLPEQNP DMPPHLPTAS ASFPVHPYSY QSPGLPSPPY GTMDSSHVFQ
VKPPPHAYSA TLEPFFESPL TDCTSPSFDG PLSPPLSING NFSFKHEPSA EFEKNYAFTM
HYPAATLAGP QSHGSIFSGA TAPRCEIPID NIMSFDSHSH HERVMSAQLN AIFHD
