NDF2_RAT
ID NDF2_RAT Reviewed; 382 AA.
AC Q63689;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Neurogenic differentiation factor 2;
DE Short=NeuroD2;
DE AltName: Full=Brain bHLH protein KW8;
GN Name=Neurod2;
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=Wistar; TISSUE=Brain;
RX PubMed=8605021; DOI=10.1006/bbrc.1996.0267;
RA Kume H., Maruyama K., Tomita T., Iwatsubo T., Saido T.C., Obata K.;
RT "Molecular cloning of a novel basic helix-loop-helix protein from the rat
RT brain.";
RL Biochem. Biophys. Res. Commun. 219:526-530(1996).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=20346398; DOI=10.1016/j.mcn.2010.03.006;
RA Ravanpay A.C., Hansen S.J., Olson J.M.;
RT "Transcriptional inhibition of REST by NeuroD2 during neuronal
RT differentiation.";
RL Mol. Cell. Neurosci. 44:178-189(2010).
CC -!- FUNCTION: Transcriptional regulator implicated in neuronal
CC determination. Mediates calcium-dependent transcription activation by
CC binding to E box-containing promoter. Critical factor essential for the
CC repression of the genetic program for neuronal differentiation;
CC prevents the formation of synaptic vesicle clustering at active zone to
CC the presynaptic membrane in postmitotic neurons. Induces transcription
CC of ZEB1, which in turn represses neuronal differentiation by down-
CC regulating REST expression. Plays a role in the establishment and
CC maturation of thalamocortical connections; involved in the segregation
CC of thalamic afferents into distinct barrel domains within layer VI of
CC the somatosensory cortex. Involved in the development of the cerebellar
CC and hippocampal granular neurons, neurons in the basolateral nucleus of
CC amygdala and the hypothalamic-pituitary axis. Associates with chromatin
CC to the DPYSL3 E box-containing promoter (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TCF3, TCF4 and TCF12. Interacts with CDC20.
CC Efficient DNA-binding and transcription activation require dimerization
CC with another bHLH protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Detected only in neural tissue. Expressed in the
CC developing cerebellum and in primary granules neurons (at protein
CC level). {ECO:0000269|PubMed:20346398}.
CC -!- DOMAIN: The C-terminal region is necessary for depolarization-induced
CC and calcium-dependent transcription activation. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11615.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D82868; BAA11615.1; ALT_FRAME; mRNA.
DR PIR; JC4647; JC4647.
DR RefSeq; NP_062199.1; NM_019326.1.
DR AlphaFoldDB; Q63689; -.
DR GeneID; 54276; -.
DR KEGG; rno:54276; -.
DR UCSC; RGD:3166; rat.
DR CTD; 4761; -.
DR RGD; 3166; Neurod2.
DR InParanoid; Q63689; -.
DR OrthoDB; 1096531at2759; -.
DR PhylomeDB; Q63689; -.
DR PRO; PR:Q63689; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
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:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0071257; P:cellular response to electrical stimulus; ISS:UniProtKB.
DR GO; GO:0021695; P:cerebellar cortex development; ISS:UniProtKB.
DR GO; GO:2000297; P:negative regulation of synapse maturation; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; 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:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
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 InterPro; IPR032649; Neurod2.
DR InterPro; IPR022575; Neurogenic_DUF.
DR InterPro; IPR016637; TF_bHLH_NeuroD.
DR PANTHER; PTHR19290:SF83; PTHR19290:SF83; 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; Developmental protein; Differentiation; DNA-binding;
KW Neurogenesis; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..382
FT /note="Neurogenic differentiation factor 2"
FT /id="PRO_0000127389"
FT DOMAIN 121..173
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 107..113
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 20..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..95
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 41466 MW; 05214DE9BE0A8069 CRC64;
MLTRLFSEPG LLSDVPKFAS WGDGDDDEPR SDKGDAPPQP PPAPGSGAPG PARATKPVSL
RGEEVPEPTL AEVKEEGELG GEEEEEEEEE EGLDEAEGER PKKRGPKKRK MTKARLERSK
LRRQKANARE RNRMHDLNAA LDNLRKVVPC YSKTQKLSKI ETLRLAKNYI WALSEILRSG
KRPDLVSYVQ TLCKGLSQPT TNLVAGCLQL NSRNFLTEQG ADGAGRFHGS GGPFAMHPYP
YPCSRLAGDQ CQAAGGLGGG AAHALRTHGY CAAYETLYAA AGGGGASPDY NSSEYEGPLS
PPLCLNGNFS LKQDSSPDHE KSYHYSMHYS ALPGSRPAGH GLVFGSSAVR GGVHSENLLS
YDMHLHHDRG PMYEELNAFF HN
