HES1A_XENLA
ID HES1A_XENLA Reviewed; 267 AA.
AC Q6IRB2; Q91635;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Transcription factor HES-1-A;
DE AltName: Full=Hairy and enhancer of split 1-A;
DE AltName: Full=Protein hairy-1;
DE Short=Xhairy-1 {ECO:0000303|PubMed:11677053};
DE Short=Xhairy1 {ECO:0000303|PubMed:15531363, ECO:0000303|PubMed:16818449, ECO:0000303|PubMed:17008450};
DE Short=Xlh1 {ECO:0000303|PubMed:8524259};
GN Name=hes1-a; Synonyms=hairy1 {ECO:0000303|PubMed:8524259};
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] {ECO:0000312|EMBL:AAA79185.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8524259; DOI=10.1128/mcb.15.12.6923;
RA Dawson S.R., Turner D.L., Weintraub H., Parkhurst S.M.;
RT "Specificity for the hairy/enhancer of split basic helix-loop-helix (bHLH)
RT proteins maps outside the bHLH domain and suggests two separable modes of
RT transcriptional repression.";
RL Mol. Cell. Biol. 15:6923-6931(1995).
RN [2] {ECO:0000312|EMBL:AAH70988.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH70988.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH HES6.
RX PubMed=10976052; DOI=10.1242/dev.127.19.4203;
RA Koyano-Nakagawa N., Kim J., Anderson D., Kintner C.;
RT "Hes6 acts in a positive feedback loop with the neurogenins to promote
RT neuronal differentiation.";
RL Development 127:4203-4216(2000).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11703945; DOI=10.1016/s1534-5807(01)00054-5;
RA Davis R.L., Turner D.L., Evans L.M., Kirschner M.W.;
RT "Molecular targets of vertebrate segmentation: two mechanisms control
RT segmental expression of Xenopus hairy2 during somite formation.";
RL Dev. Cell 1:553-565(2001).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DOMAIN FUNCTION.
RX PubMed=11677053; DOI=10.1016/s0925-4773(01)00517-2;
RA Umbhauer M., Boucaut J.-C., Shi D.-L.;
RT "Repression of XMyoD expression and myogenesis by Xhairy-1 in Xenopus early
RT embryo.";
RL Mech. Dev. 109:61-68(2001).
RN [6] {ECO:0000305}
RP INTERACTION WITH HEY1.
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 [7] {ECO:0000305}
RP INTERACTION WITH HEY1, AND TISSUE SPECIFICITY.
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 [8] {ECO:0000305}
RP TISSUE SPECIFICITY.
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).
RN [9] {ECO:0000305}
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: Transcriptional repressor of a subset of early mesodermal
CC genes including myod1 and t/bra. Binds DNA on N-box motifs: 5'-CACNAG-
CC 3'. Acts as a negative regulator of myogenesis, mediating Notch
CC signaling to repress expression of myod1. {ECO:0000269|PubMed:10976052,
CC ECO:0000269|PubMed:11677053}.
CC -!- SUBUNIT: Transcription repression requires formation of a complex with
CC a corepressor protein of the Groucho/TLE family (By similarity).
CC Interacts with the bHLH protein hes2, and binds DNA in the form of a
CC heterodimer with the bHLH protein hey1/hrt1. Interacts with the bHLH
CC protein hes6; this interaction may inhibit the transcriptional
CC repressor activity. {ECO:0000250, ECO:0000269|PubMed:10976052,
CC ECO:0000269|PubMed:14648848, ECO:0000269|PubMed:15531363,
CC ECO:0000269|PubMed:17008450}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14469,
CC ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-
CC ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Starting from late neurula stage, weakly expressed
CC in midline neural cells, where expression is restricted to the
CC superficial layer of the prospective floorplate. Expressed in the
CC posterior somitic mesoderm (PSM) at tailbud stage. During early tailbud
CC stages, broadly expressed within the pronephric mesoderm both around
CC and inside the developing pronephros. During late tailbud to early
CC tadpole stages, expressed more ventrally in the pronephros, and
CC although initially expressed in both the lateral and medial layers, by
CC these later stages expression is predominantly in the lateral layer.
CC Pronephric expression is no longer detectable in late tadpoles (stage
CC 35). {ECO:0000269|PubMed:11677053, ECO:0000269|PubMed:11703945,
CC ECO:0000269|PubMed:15531363, ECO:0000269|PubMed:16818449}.
CC -!- DEVELOPMENTAL STAGE: Expression begins soon after the mid-blastula
CC transition. {ECO:0000269|PubMed:11677053}.
CC -!- DOMAIN: Has a particular type of basic domain (presence of a helix-
CC interrupting proline) that binds to the N-box (CACNAG), rather than the
CC canonical E-box (CANNTG). {ECO:0000250|UniProtKB:P14003}.
CC -!- DOMAIN: The bHLH, as well as cooperation between the central Orange
CC domain and the C-terminal WRPW motif, is required for transcriptional
CC repressor activity. {ECO:0000269|PubMed:11677053}.
CC -!- DOMAIN: The C-terminal WRPW motif is a transcriptional repression
CC domain necessary for the interaction with Groucho/TLE family members,
CC transcriptional corepressors recruited to specific target DNA by Hairy-
CC related proteins. {ECO:0000250}.
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DR EMBL; U36194; AAA79185.1; -; mRNA.
DR EMBL; BC070988; AAH70988.1; -; mRNA.
DR RefSeq; NP_001081396.1; NM_001087927.1.
DR AlphaFoldDB; Q6IRB2; -.
DR SMR; Q6IRB2; -.
DR ELM; Q6IRB2; -.
DR DNASU; 397813; -.
DR GeneID; 397813; -.
DR KEGG; xla:397813; -.
DR CTD; 397813; -.
DR Xenbase; XB-GENE-865756; hes1.L.
DR OMA; HLANCMS; -.
DR OrthoDB; 1427802at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 397813; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0048635; P:negative regulation of muscle organ development; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; 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..267
FT /note="Transcription factor HES-1-A"
FT /id="PRO_0000370738"
FT DOMAIN 34..91
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 110..143
FT /note="Orange"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00380"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 264..267
FT /note="WRPW motif"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 156..159
FT /note="PTQP -> LPA (in Ref. 1; AAA79185)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="M -> S (in Ref. 1; AAA79185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 28725 MW; 54433B7C3FC5DBFF CRC64;
MPADVMEKNS SSPVAATPAS VSNTPDKPKT ASEHRKSSKP IMEKRRRARI NESLGQLKTL
ILDALKKDSS RHSKLEKADI LEMTVKHLRN LQRVQMSAAL STDPSVLGKY RAGFSECMNE
VTRFLSTCEG VNTDVRTRLL GHLANCMNQI NGMNYPTQPQ MPSAAAPHPA YGQPMVQLPG
AAPQSSPAPI ACKMGGPPVE AAKVYGGFQL VPAPDGQFAF LITNPAFPHN GSVIPVYTNS
NVGTALPPSV SPSVMPSVTI DSVWRPW
