NDF4_XENLA
ID NDF4_XENLA Reviewed; 315 AA.
AC P79920;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Neurogenic differentiation factor 4;
DE Short=NeuroD4;
DE AltName: Full=Helix-loop-helix protein xATH-3;
DE Short=xATH3;
DE AltName: Full=Protein atonal homolog 3;
GN Name=neurod4; Synonyms=ath3, atoh3;
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, MUTAGENESIS OF
RP SER-89, AND PHOSPHORYLATION AT SER-89.
RC TISSUE=Embryo;
RX PubMed=9029157; DOI=10.1093/emboj/16.2.384;
RA Takebayashi K., Takahashi S., Yokota C., Tsuda H., Nakanishi S.,
RA Asashima M., Kageyama R.;
RT "Conversion of ectoderm into a neural fate by ATH-3, a vertebrate basic
RT helix-loop-helix gene homologous to Drosophila proneural gene atonal.";
RL EMBO J. 16:384-395(1997).
RN [2]
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 [3]
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).
CC -!- FUNCTION: Probably acts as a transcriptional activator. Mediates
CC neuronal differentiation. Required for the regulation of amacrine cell
CC fate specification in the retina (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9029157}.
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. {ECO:0000250,
CC ECO:0000269|PubMed:15531363, ECO:0000269|PubMed:17008450}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: First expressed weakly at stage 12 in primary
CC neuronal precursors. At stages 18 and 21, strongly expressed in the
CC cranial ganglions, with weaker expression remaining in the spinal cord.
CC Later, strongly expressed at sites of neuronal differentiation, namely
CC the eye, forebrain and cranial ganglions. {ECO:0000269|PubMed:9029157}.
CC -!- PTM: Serine or threonine phosphorylation within the basic region may
CC regulate neurogenic activity. {ECO:0000269|PubMed:9029157}.
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DR EMBL; D85188; BAA12738.1; -; mRNA.
DR RefSeq; NP_001081213.1; NM_001087744.1.
DR AlphaFoldDB; P79920; -.
DR SMR; P79920; -.
DR iPTMnet; P79920; -.
DR PRIDE; P79920; -.
DR GeneID; 397714; -.
DR KEGG; xla:397714; -.
DR CTD; 397714; -.
DR Xenbase; XB-GENE-972708; neurod4.L.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 397714; Expressed in camera-type eye and 1 other tissue.
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:0035881; P:amacrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IEA:InterPro.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISS:UniProtKB.
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; IPR032651; Neurod4.
DR InterPro; IPR022575; Neurogenic_DUF.
DR InterPro; IPR016637; TF_bHLH_NeuroD.
DR PANTHER; PTHR19290:SF86; PTHR19290:SF86; 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; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..315
FT /note="Neurogenic differentiation factor 4"
FT /id="PRO_0000127392"
FT DOMAIN 78..130
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 39..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:9029157"
FT MUTAGEN 89
FT /note="S->D: Mimics a phosphorylated residue. Retains a
FT general neurogenic activity but severely impairs anterior
FT marker-inducing abilities."
FT /evidence="ECO:0000269|PubMed:9029157"
FT MUTAGEN 89
FT /note="S->N: Retains ability to induce both general and
FT anterior neural markers."
FT /evidence="ECO:0000269|PubMed:9029157"
SQ SEQUENCE 315 AA; 35417 MW; 5C3E32ECD89CFA48 CRC64;
MSEMVNVHGW MEEALSSQDE MKERNQSAYD IISGLCHEER GSIDGEEDDE EEEDGEKPKK
RGPKKKKMTK ARVERFRVRR VKANARERSR MHGLNDALEN LRRVMPCYSK TQKLSKIETL
RLARNYIWAL SDILEQGQNA EGKGFLEILC KGLSQPTSNL VAGCLQLGPQ AMFLDKHEEK
SHICDSSLTG HTYNYQSPGL PSPPYGNIDV HHLHLKPSSF KPVMDPSVVT HTLNCTTPPY
EGALTPPLSI GGNFSLKQDS SPDMDKSYAF RSPYPALGLG GSHGHASHFH TSVPRYELPI
DMAYEPYPHH AIFTE
