HEY1_XENLA
ID HEY1_XENLA Reviewed; 294 AA.
AC Q9I8A3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Hairy/enhancer-of-split related with YRPW motif protein 1;
DE Short=XHey-1;
DE AltName: Full=Hairy and enhancer of split-related protein 1;
DE Short=Hesr-1;
DE AltName: Full=Hairy-related transcription factor 1;
DE Short=HRT-1;
DE Short=XHRT1;
DE Short=xHRT-1;
DE AltName: Full=Protein xbc8;
GN Name=hey1; Synonyms=bc8, hrt1;
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC TISSUE=Embryonic head;
RX PubMed=12424520; DOI=10.1007/s00427-002-0270-z;
RA Pichon B., Taelman V., Kricha S., Christophe D., Bellefroid E.J.;
RT "XHRT-1, a hairy and Enhancer of split related gene with expression in
RT floor plate and hypochord during early Xenopus embryogenesis.";
RL Dev. Genes Evol. 212:491-495(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12454931; DOI=10.1002/dvdy.10192;
RA Rones M.S., Woda J., Mercola M., McLaughlin K.A.;
RT "Isolation and characterization of Xenopus Hey-1: a downstream mediator of
RT Notch signaling.";
RL Dev. Dyn. 225:554-560(2002).
RN [4]
RP INTERACTION WITH HES1; HES4-B AND CCDC89, AND SUBCELLULAR LOCATION.
RX PubMed=14648848; DOI=10.1002/dvdy.10406;
RA Van Wayenbergh R., Taelman V., Pichon B., Fischer A., Kricha S.,
RA Gessler M., Christophe D., Bellefroid E.J.;
RT "Identification of BOIP, a novel cDNA highly expressed during
RT spermatogenesis that encodes a protein interacting with the orange domain
RT of the hairy-related transcription factor HRT1/Hey1 in Xenopus and mouse.";
RL Dev. Dyn. 228:716-725(2003).
RN [5]
RP FUNCTION, DNA-BINDING, AND DOMAIN FUNCTION.
RX PubMed=15451171; DOI=10.1016/j.bbaexp.2004.08.010;
RA Pichon B., Taelman V., Bellefroid E.J., Christophe D.;
RT "Transcriptional repression by the bHLH-Orange factor XHRT1 does not
RT involve the C-terminal YRPW motif.";
RL Biochim. Biophys. Acta 1680:46-52(2004).
RN [6]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH HES1; HES2; HES4-B; NEUROD1
RP AND NEUROD4, TISSUE SPECIFICITY, AND DOMAIN FUNCTION.
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16818449; DOI=10.1242/dev.02458;
RA Taelman V., Van Campenhout C., Soelter M., Pieler T., Bellefroid E.J.;
RT "The Notch-effector HRT1 gene plays a role in glomerular development and
RT patterning of the Xenopus pronephros anlagen.";
RL Development 133:2961-2971(2006).
CC -!- FUNCTION: Downstream effector of Notch signaling. Transcriptional
CC repressor which binds preferentially to the canonical E box sequence
CC 5'-CACGTG-3'. Acts as a suppressor of neurogenesis by antagonizing
CC proneural gene function. Functions during floorplate development. Plays
CC a role in pronephros formation in the inhibition of distal tubule and
CC duct cell fates and the promotion of glomus and proximal tubule
CC formation. {ECO:0000250|UniProtKB:Q9WV93, ECO:0000269|PubMed:15451171,
CC ECO:0000269|PubMed:15531363, ECO:0000269|PubMed:16818449}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA in the form of homodimer or more strongly as a
CC heterodimer with hes1/hairy1 or hes4-B/hairy2b. Also weakly interacts
CC with the bHLH proteins hes2, neurod1 and neurod4/ath3. Interacts (via
CC Orange domain) with ccdc89/boip (via C-terminus).
CC {ECO:0000269|PubMed:14648848, ECO:0000269|PubMed:15531363}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380,
CC ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:14648848}.
CC -!- TISSUE SPECIFICITY: Expression in late gastrula and early neurula
CC embryos is restricted to dorsal endodermal cells and the medial neural
CC plate and in dorsal endodermal cells. Expression fills exactly the gap
CC in between the two rows of motor neurons in the ventral neural tube. At
CC later stages, expressed in the floor plate, in hypochord cells and in
CC the somitogenic and anterior presomitic mesoderm. By tailbud stage,
CC also highly expressed in the dorsal hindbrain, telencephalon and eye
CC vesicles, olfactory placodes, branchial arches, tail fin and somites.
CC Expression in the somite, eye, head and branchial arches persists
CC throughout organogenesis. In addition, despite being absent in the
CC early heart field, expression begins within the linear heart tube at
CC stages 32-35. Also expressed from the early-tailbud stage in the
CC dorsoanterior region of the developing pronephros. During early tailbud
CC stages, localized to the most dorsoanterior portion of the pronephric
CC anlagen. During late tailbud to early tadpole stages, expression marks
CC the most dorsoanterior portion of the pronephros with expression
CC becoming progressively restricted to the tip of the forming tubules.
CC Pronephric expression is no longer detectable at late tadpole stages
CC (stage 35). In adults, strongest expression is observed in the brain,
CC eye, heart, lung, muscle, ovary, skin, spleen and testis.
CC {ECO:0000269|PubMed:12424520, ECO:0000269|PubMed:12454931,
CC ECO:0000269|PubMed:15531363, ECO:0000269|PubMed:16818449}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis, with
CC expression rising after neurulation. {ECO:0000269|PubMed:12424520}.
CC -!- INDUCTION: By Notch signaling. {ECO:0000269|PubMed:12424520,
CC ECO:0000269|PubMed:12454931, ECO:0000269|PubMed:16818449}.
CC -!- DOMAIN: The Orange domain, downstream sequence and the bHLH are
CC required for efficient heterodimerization with hes/hairy proteins, and
CC for transcriptional repressor activity.
CC -!- DOMAIN: The C-terminal YRPW motif is not required for transcriptional
CC repressor activity and is unable to recruit groucho.
CC -!- SIMILARITY: Belongs to the HEY family. {ECO:0000305}.
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DR EMBL; AJ401271; CAB96791.1; -; mRNA.
DR EMBL; BC084410; AAH84410.1; -; mRNA.
DR RefSeq; NP_001083926.1; NM_001090457.1.
DR AlphaFoldDB; Q9I8A3; -.
DR SMR; Q9I8A3; -.
DR BioGRID; 100520; 1.
DR ELM; Q9I8A3; -.
DR DNASU; 399195; -.
DR GeneID; 399195; -.
DR KEGG; xla:399195; -.
DR CTD; 399195; -.
DR Xenbase; XB-GENE-865637; hey1.S.
DR OMA; RENDENC; -.
DR OrthoDB; 1201152at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 399195; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0033504; P:floor plate development; IMP:UniProtKB.
DR GO; GO:0072013; P:glomus development; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:0048793; P:pronephros development; IMP:UniProtKB.
DR GO; GO:0072196; P:proximal/distal pattern formation involved in pronephric nephron development; IMP:UniProtKB.
DR GO; GO:0072082; P:specification of proximal tubule identity; IMP:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR003650; Orange_dom.
DR Pfam; PF07527; Hairy_orange; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00511; ORANGE; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS51054; ORANGE; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Notch signaling pathway; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..294
FT /note="Hairy/enhancer-of-split related with YRPW motif
FT protein 1"
FT /id="PRO_0000286426"
FT DOMAIN 44..99
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 117..153
FT /note="Orange"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00380"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 284..287
FT /note="YRPW motif"
FT COMPBIAS 27..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 32135 MW; B8A705A2F506C007 CRC64;
MKRGHDYSSS DSELDENIEV EKESADENGN LSSMSPSTSS QILARKRRRG IIEKRRRDRI
NNSLSELRRL VPSAFEKQGS AKLEKAEILQ MTVDHLKMLH TAGGKGYFDA HALAMDYRSL
GFRECLAEVA RYLSIIEGME TADPLRVRLV SHLNNYASQR EAASTAHTSI GHIPWGGTFA
HHPHLSHPLL LAQTAHTNST SSSTEAHHHN RLRGSPHAES SSLRVAPNGN IASVLPVVAS
SKLSPPLLSS MASLSAFPFS FGSFHLLSPN SLSPTTPTPS GKPYRPWGTE IGAF
