ID   ASCL1_XENLA             Reviewed;         199 AA.
AC   Q06234;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Achaete-scute homolog 1;
DE            Short=XASH1 {ECO:0000303|PubMed:8443105};
GN   Name=ascl1; Synonyms=ash1;
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.
RX   PubMed=8443105; DOI=10.1016/0925-4773(93)90085-c;
RA   Ferreiro B., Skoglund P., Bailey A., Dorsky R., Harris W.A.;
RT   "XASH1, a Xenopus homolog of achaete-scute: a proneural gene in anterior
RT   regions of the vertebrate CNS.";
RL   Mech. Dev. 40:25-36(1993).
CC   -!- FUNCTION: Transcription factor that plays a key role in neuronal
CC       differentiation: acts as a pioneer transcription factor, accessing
CC       closed chromatin to allow other factors to bind and activate neural
CC       pathways (By similarity). Directly binds the E box motif (5'-CANNTG-3')
CC       on promoters and promotes transcription of neuronal genes
CC       (PubMed:8443105). The combination of three transcription factors,
CC       ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts
CC       and other somatic cells into induced neuronal (iN) cells in vitro (By
CC       similarity). {ECO:0000250|UniProtKB:Q02067,
CC       ECO:0000269|PubMed:8443105}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. {ECO:0000250|UniProtKB:P50553}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02067}.
CC   -!- TISSUE SPECIFICITY: Neuronal precursor cells.
CC       {ECO:0000269|PubMed:8443105}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the embryonic anterior central
CC       nervous system. In the forebrain, and then in the eye and hindbrain.
CC       {ECO:0000269|PubMed:8443105}.
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DR   EMBL; M98272; AAA49649.1; -; mRNA.
DR   PIR; A56548; A56548.
DR   RefSeq; NP_001079247.1; NM_001085778.1.
DR   AlphaFoldDB; Q06234; -.
DR   SMR; Q06234; -.
DR   GeneID; 378517; -.
DR   KEGG; xla:378517; -.
DR   CTD; 378517; -.
DR   Xenbase; XB-GENE-1032969; ascl1.L.
DR   OrthoDB; 1131543at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 378517; Expressed in oocyte and 13 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0048663; P:neuron fate commitment; ISS:UniProtKB.
DR   GO; GO:0048665; P:neuron fate specification; ISS:UniProtKB.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0060579; P:ventral spinal cord interneuron fate commitment; ISS:UniProtKB.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR015660; MASH1/Ascl1a-like.
DR   PANTHER; PTHR13935; PTHR13935; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   2: Evidence at transcript level;
KW   Activator; Developmental protein; Differentiation; DNA-binding;
KW   Neurogenesis; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..199
FT                   /note="Achaete-scute homolog 1"
FT                   /id="PRO_0000127129"
FT   DOMAIN          81..133
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          37..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   199 AA;  22374 MW;  238A9F92D5A8AC48 CRC64;
     MDNCVAAKIM DSNLSSQQQH FLQPHCFFPQ NVQQLSPAEE QQASKAKPIK RQRSASPELM
     RCKRRLNFNG FGYSLPQQQP AAVARRNERE RNRVKLVNLG FATLREHVPN GAANKKMSKV
     ETLRSAVEYI RALQQLLDEH DAVSAAFQSG VLSPTISPNY SHDMNSMAGS PVSSYSSDEG
     SYDPLSPEEQ ELLDFTTWF