ASL1A_DANRE
ID ASL1A_DANRE Reviewed; 196 AA.
AC Q90259;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Achaete-scute homolog 1a;
DE Short=Zash-1a;
DE AltName: Full=Pituitary-absent protein;
GN Name=ascl1a {ECO:0000312|ZFIN:ZDB-GENE-980526-90};
GN Synonyms=ash {ECO:0000312|EMBL:AAA78898.1},
GN ash1a {ECO:0000303|PubMed:12702659},
GN asha {ECO:0000312|ZFIN:ZDB-GENE-980526-90},
GN pia {ECO:0000303|PubMed:16481349};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA78898.1}
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo {ECO:0000269|PubMed:7813774};
RX PubMed=7813774; DOI=10.1006/dbio.1994.1334;
RA Allende M.L., Weinberg E.S.;
RT "The expression pattern of two zebrafish achaete-scute homolog (ash) genes
RT is altered in the embryonic brain of the cyclops mutant.";
RL Dev. Biol. 166:509-530(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000312|EMBL:CAI21097.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye {ECO:0000312|EMBL:AAH98521.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12702659; DOI=10.1242/dev.00452;
RA Cau E., Wilson S.W.;
RT "Ash1a and neurogenin1 function downstream of floating head to regulate
RT epiphysial neurogenesis.";
RL Development 130:2455-2466(2003).
RN [5] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15659486; DOI=10.1242/dev.01616;
RA Amoyel M., Cheng Y.-C., Jiang Y.-J., Wilkinson D.G.;
RT "Wnt1 regulates neurogenesis and mediates lateral inhibition of boundary
RT cell specification in the zebrafish hindbrain.";
RL Development 132:775-785(2005).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16481349; DOI=10.1242/dev.02296;
RA Pogoda H.-M., von der Hardt S., Herzog W., Kramer C., Schwarz H.,
RA Hammerschmidt M.;
RT "The proneural gene ascl1a is required for endocrine differentiation and
RT cell survival in the zebrafish adenohypophysis.";
RL Development 133:1079-1089(2006).
CC -!- FUNCTION: Transcriptional regulator. May mediate transcription
CC activation by binding to the E box-containing promoter (By similarity).
CC Involved in neurogenesis. Required for the development of neurons in
CC the epiphysis, acting partially redundantly with neurog1 and downstream
CC of flh. Involved in maintaining rhombomere boundaries in the hindbrain,
CC probably via up-regulation of delta expression. Also involved in
CC pituitary development; required cell-autonomously in adenohypophyseal
CC cells for endocrine differentiation and for survival of a subset of
CC cells. {ECO:0000250, ECO:0000269|PubMed:12702659,
CC ECO:0000269|PubMed:15659486, ECO:0000269|PubMed:16481349}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. {ECO:0000250|UniProtKB:P50553}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In the 24 hours embryo, expressed in the dorsal
CC hindbrain in two bilaterally symmetrical lines of cells marking the
CC boundary between the alar and basal plates, and ventrally in rhombomere
CC 1 near the floor plate. Also expressed in embryonic adenohypophysis,
CC telencephalon, diencephalon, epiphysis, ventral tegmentum, neural
CC retina and spinal cord, in discrete regions distinct from those
CC expressing ascl1b. In the 30 hours embryo, hindbrain expression is in
CC stripes adjacent to rhombomere boundaries.
CC {ECO:0000269|PubMed:12702659, ECO:0000269|PubMed:15659486,
CC ECO:0000269|PubMed:16481349, ECO:0000269|PubMed:7813774}.
CC -!- DEVELOPMENTAL STAGE: First detected at 12 hours post-fertilization
CC (hpf), increasing over the next 24 hours, then decreasing between 48
CC and 72 hours. Not detected in adult. {ECO:0000269|PubMed:7813774}.
CC -!- DISRUPTION PHENOTYPE: In pituitary absent (pia) mutants,
CC adenohypophyseal cells fail to express hormone genes and some become
CC apoptotic. {ECO:0000269|PubMed:16481349}.
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DR EMBL; U14587; AAA78898.1; -; mRNA.
DR EMBL; BX510924; CAK04833.1; -; Genomic_DNA.
DR EMBL; BX511171; CAI21097.1; -; Genomic_DNA.
DR EMBL; BC098521; AAH98521.1; -; mRNA.
DR PIR; I50507; I50507.
DR RefSeq; NP_571294.1; NM_131219.1.
DR AlphaFoldDB; Q90259; -.
DR SMR; Q90259; -.
DR STRING; 7955.ENSDARP00000056004; -.
DR PaxDb; Q90259; -.
DR Ensembl; ENSDART00000056005; ENSDARP00000056004; ENSDARG00000038386.
DR GeneID; 30466; -.
DR KEGG; dre:30466; -.
DR CTD; 30466; -.
DR ZFIN; ZDB-GENE-980526-90; ascl1a.
DR eggNOG; KOG4029; Eukaryota.
DR GeneTree; ENSGT00940000166611; -.
DR HOGENOM; CLU_063523_3_0_1; -.
DR InParanoid; Q90259; -.
DR OMA; QLIPPAC; -.
DR OrthoDB; 1131543at2759; -.
DR PhylomeDB; Q90259; -.
DR TreeFam; TF322889; -.
DR PRO; PR:Q90259; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000038386; Expressed in regional part of brain and 73 other tissues.
DR GO; GO:0005634; C:nucleus; IC:ZFIN.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IPI:ZFIN.
DR GO; GO:0021984; P:adenohypophysis development; IMP:UniProtKB.
DR GO; GO:0031103; P:axon regeneration; IMP:ZFIN.
DR GO; GO:0043697; P:cell dedifferentiation; IGI:ZFIN.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:ZFIN.
DR GO; GO:0002070; P:epithelial cell maturation; IMP:ZFIN.
DR GO; GO:0021575; P:hindbrain morphogenesis; IMP:UniProtKB.
DR GO; GO:0060575; P:intestinal epithelial cell differentiation; IMP:ZFIN.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ZFIN.
DR GO; GO:0007399; P:nervous system development; IMP:ZFIN.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ZFIN.
DR GO; GO:0031099; P:regeneration; IMP:ZFIN.
DR GO; GO:0050767; P:regulation of neurogenesis; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070654; P:sensory epithelium regeneration; IGI:ZFIN.
DR GO; GO:0007423; P:sensory organ development; IBA:GO_Central.
DR GO; GO:0061549; P:sympathetic ganglion development; IMP:ZFIN.
DR GO; GO:0061195; P:taste bud formation; IMP:ZFIN.
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 Developmental protein; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..196
FT /note="Achaete-scute homolog 1a"
FT /id="PRO_0000271235"
FT DOMAIN 78..130
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 33..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 196 AA; 21928 MW; 462E3A35DCBA183A CRC64;
MDITAKMEIS VNQQQFMPPA CFFASQSIQL SPTDSQCSNK SASKQAKRQR SSSPELLRCK
RRLNFAGFGY SLPQQQPHAV ARRNERERNR VKLVNNGFAT LREHVPNGAA NKKMSKVETL
RSAVEYIRAL QQLLDEHDAV SAAFQSGVLS PTISQNYSND MNSMAGSPVS SYSSDEGSYD
PLSPEEQELL DFTNWF