NDF1_XENLA
ID NDF1_XENLA Reviewed; 352 AA.
AC Q91616;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Neurogenic differentiation factor 1;
DE Short=NeuroD1;
GN Name=neurod1; Synonyms=neurod;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryonic head;
RX PubMed=7754368; DOI=10.1126/science.7754368;
RA Lee J.E., Hollenberg S.M., Snider L., Turner D.L., Lipnick N.,
RA Weintraub H.;
RT "Conversion of Xenopus ectoderm into neurons by NeuroD, a basic helix-loop-
RT helix protein.";
RL Science 268:836-844(1995).
RN [2]
RP FUNCTION.
RX PubMed=9828091; DOI=10.1006/mcne.1998.0713;
RA Marcus E.A., Kintner C., Harris W.;
RT "The role of GSK3beta in regulating neuronal differentiation in Xenopus
RT laevis.";
RL Mol. Cell. Neurosci. 12:269-280(1998).
RN [3]
RP FUNCTION, MUTAGENESIS OF 274-SER--SER-278, AND DEVELOPMENTAL STAGE.
RX PubMed=11970861; DOI=10.1016/s0896-6273(02)00666-9;
RA Moore K.B., Schneider M.L., Vetter M.L.;
RT "Posttranslational mechanisms control the timing of bHLH function and
RT regulate retinal cell fate.";
RL Neuron 34:183-195(2002).
RN [4]
RP INTERACTION WITH HEY1.
RX PubMed=15531363; DOI=10.1016/j.ydbio.2004.08.019;
RA Taelman V., Van Wayenbergh R., Soelter M., Pichon B., Pieler T.,
RA Christophe D., Bellefroid E.J.;
RT "Sequences downstream of the bHLH domain of the Xenopus hairy-related
RT transcription factor-1 act as an extended dimerization domain that
RT contributes to the selection of the partners.";
RL Dev. Biol. 276:47-63(2004).
RN [5]
RP INTERACTION WITH HES2.
RX PubMed=17008450; DOI=10.1242/dev.02567;
RA Soelter M., Locker M., Boy S., Taelman V., Bellefroid E.J., Perron M.,
RA Pieler T.;
RT "Characterization and function of the bHLH-O protein XHes2: insight into
RT the mechanisms controlling retinal cell fate decision.";
RL Development 133:4097-4108(2006).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF SER-258; SER-266 AND SER-274.
RX PubMed=15797719; DOI=10.1016/j.mcn.2004.12.004;
RA Dufton C., Marcora E., Chae J.H., McCullough J., Eby J., Hausburg M.,
RA Stein G.H., Khoo S., Cobb M.H., Lee J.E.;
RT "Context-dependent regulation of NeuroD activity and protein
RT accumulation.";
RL Mol. Cell. Neurosci. 28:727-736(2005).
CC -!- FUNCTION: Acts as a transcriptional activator. Plays a role as a
CC differentiation factor during neurogenesis. Required for the conversion
CC of cells within the neural plate and ventral ectoderm into
CC differentiated neurons. Promotes the differentiation of late-born
CC retinal amacrine cells, but not early-born retinal ganglion cells. Its
CC function is inhibited at early stages of retinal cells differentiation.
CC {ECO:0000269|PubMed:11970861, ECO:0000269|PubMed:15797719,
CC ECO:0000269|PubMed:7754368, ECO:0000269|PubMed:9828091}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein (By similarity). Forms a heterodimer with the bHLH protein
CC hes2, and weakly interacts with hey1/hrt1.
CC {ECO:0000250|UniProtKB:Q60867, ECO:0000269|PubMed:15531363,
CC ECO:0000269|PubMed:17008450}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Expressed in differentiating neurons of both the
CC central and peripheral nervous systems. {ECO:0000269|PubMed:7754368}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the neural plate at stage 14 and
CC expression continues throughout embryonic development. Expressed in the
CC developing retina. {ECO:0000269|PubMed:11970861,
CC ECO:0000269|PubMed:7754368}.
CC -!- PTM: Phosphorylation on Ser-266 and Ser-274 reduces protein
CC accumulation and inhibits ectopic neurogenic activity.
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DR EMBL; U28067; AAC59675.1; -; mRNA.
DR PIR; I51687; I51687.
DR RefSeq; NP_001079263.1; NM_001085794.1.
DR AlphaFoldDB; Q91616; -.
DR SMR; Q91616; -.
DR BioGRID; 97123; 1.
DR GeneID; 378541; -.
DR KEGG; xla:378541; -.
DR CTD; 378541; -.
DR Xenbase; XB-GENE-6252655; neurod1.L.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 378541; Expressed in camera-type eye and 7 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0048666; P:neuron development; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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..352
FT /note="Neurogenic differentiation factor 1"
FT /id="PRO_0000127386"
FT DOMAIN 102..154
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 88..94
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 29..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MUTAGEN 258
FT /note="S->A: Does not induce protein accumulation. Does not
FT stimulate neurogenic activity. Does not alter subcellular
FT localization; when associated with A-266 and A-274."
FT /evidence="ECO:0000269|PubMed:15797719"
FT MUTAGEN 266
FT /note="S->A: Induces protein accumulation. Stimulates
FT ectopic neurogenic activity. Does not alter subcellular
FT localization; when associated with A-258 and A-274."
FT /evidence="ECO:0000269|PubMed:15797719"
FT MUTAGEN 274..278
FT /note="SPPLS->APPLA: Promotes the formation of
FT differentiated early retinal ganglion cells."
FT /evidence="ECO:0000269|PubMed:11970861"
FT MUTAGEN 274
FT /note="S->A: Induces protein accumulation. Stimulates
FT ectopic neurogenic activity. Does not alter subcellular
FT localization; when associated with A-258 and A-266."
FT /evidence="ECO:0000269|PubMed:15797719"
SQ SEQUENCE 352 AA; 39662 MW; 226298DB3D48233E CRC64;
MTKSYGENGL ILAETPGCRG WVDECLSSQD ENDLEKKEGE LMKEDDEDSL NHHNGEENEE
EDEGDEEEED DEDDDEDDDQ KPKRRGPKKK KMTKARVERF KVRRMKANAR ERNRMHGLND
ALDSLRKVVP CYSKTQKLSK IETLRLAKNY IWALSEILRS GKSPDLVSFV QTLCKGLSQP
TTNLVAGCLQ LNPRTFLPEQ SQDIQSHMQT ASSSFPLQGY PYQSPGLPSP PYGTMDSSHV
FHVKPHSYGA ALEPFFDSST VTECTSPSFD GPLSPPLSVN GNFTFKHEHS EYDKNYTFTM
HYPAATISQG HGPLFSTGGP RCEIPIDTIM SYDGHSHHER VMSAQLNAIF HD
