HLH11_CAEEL
ID HLH11_CAEEL Reviewed; 431 AA.
AC P34474; Q7JMU4; Q7YXC9; Q86DA4; Q9U3E1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Helix-loop-helix protein 11;
GN Name=hlh-11 {ECO:0000312|WormBase:F58A4.7b};
GN ORFNames=F58A4.7 {ECO:0000312|WormBase:F58A4.7b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 112-MET--VAL-389.
RX PubMed=19855932; DOI=10.1007/s10059-009-0145-5;
RA Lee S.U., Song H.O., Lee W., Singaravelu G., Yu J.R., Park W.Y.;
RT "Identification and characterization of a putative basic helix-loop-helix
RT (bHLH) transcription factor interacting with calcineurin in C. elegans.";
RL Mol. Cells 28:455-461(2009).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=33078707; DOI=10.7554/elife.58815;
RA Littlejohn N.K., Seban N., Liu C.C., Srinivasan S.;
RT "A feedback loop governs the relationship between lipid metabolism and
RT longevity.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Transcriptional regulator (PubMed:33078707). Component of a
CC feedback loop involving atfs-1, atgl-1 and hlh-11 (PubMed:33078707).
CC Binds to the promoter of the atgl-1 lipase to negatively regulate the
CC expression of atgl-1, and thereby promoting fat oxidation in response
CC to mitochondrial stress and mitochondrial respiration in the intestine
CC (PubMed:33078707). In addition, functions with atfs-1 to maintain
CC lifespan (PubMed:33078707). May have a role in fertility and in
CC positively regulating body size (PubMed:19855932).
CC {ECO:0000269|PubMed:19855932, ECO:0000269|PubMed:33078707}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:33078707}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:F58A4.7b};
CC IsoId=P34474-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F58A4.7a};
CC IsoId=P34474-2; Sequence=VSP_020162;
CC Name=d {ECO:0000312|WormBase:F58A4.7d};
CC IsoId=P34474-4; Sequence=VSP_020161, VSP_020163;
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx, nerve cords, the H-shaped
CC excretory cell, vulva muscles, and the anal depressor (at protein
CC level) (PubMed:19855932). Expressed in the intestine (at protein level)
CC (PubMed:19855932, PubMed:33078707). In males, it is also expressed in
CC the spicules and hyp7 cells of the hypodermis (at protein level)
CC (PubMed:19855932). {ECO:0000269|PubMed:19855932,
CC ECO:0000269|PubMed:33078707}.
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DR EMBL; BX284603; CAA80167.2; -; Genomic_DNA.
DR EMBL; BX284603; CAA80170.2; -; Genomic_DNA.
DR EMBL; BX284603; CAD91636.1; -; Genomic_DNA.
DR PIR; B88561; B88561.
DR PIR; S40979; S40979.
DR RefSeq; NP_001022626.1; NM_001027455.3.
DR RefSeq; NP_001022627.1; NM_001027456.3.
DR RefSeq; NP_499129.2; NM_066728.5. [P34474-1]
DR RefSeq; NP_499130.2; NM_066729.6. [P34474-2]
DR AlphaFoldDB; P34474; -.
DR BioGRID; 41555; 7.
DR IntAct; P34474; 6.
DR STRING; 6239.F58A4.7b.1; -.
DR EPD; P34474; -.
DR PaxDb; P34474; -.
DR EnsemblMetazoa; F58A4.7a.1; F58A4.7a.1; WBGene00001955. [P34474-2]
DR EnsemblMetazoa; F58A4.7a.2; F58A4.7a.2; WBGene00001955. [P34474-2]
DR EnsemblMetazoa; F58A4.7b.1; F58A4.7b.1; WBGene00001955. [P34474-1]
DR EnsemblMetazoa; F58A4.7b.2; F58A4.7b.2; WBGene00001955. [P34474-1]
DR EnsemblMetazoa; F58A4.7b.3; F58A4.7b.3; WBGene00001955. [P34474-1]
DR EnsemblMetazoa; F58A4.7b.4; F58A4.7b.4; WBGene00001955. [P34474-1]
DR EnsemblMetazoa; F58A4.7d.1; F58A4.7d.1; WBGene00001955. [P34474-4]
DR EnsemblMetazoa; F58A4.7d.2; F58A4.7d.2; WBGene00001955. [P34474-4]
DR GeneID; 176360; -.
DR KEGG; cel:CELE_F58A4.7; -.
DR UCSC; F58A4.7a.1; c. elegans. [P34474-1]
DR CTD; 176360; -.
DR WormBase; F58A4.7a; CE32193; WBGene00001955; hlh-11. [P34474-2]
DR WormBase; F58A4.7b; CE32194; WBGene00001955; hlh-11. [P34474-1]
DR WormBase; F58A4.7d; CE34038; WBGene00001955; hlh-11. [P34474-4]
DR eggNOG; KOG0561; Eukaryota.
DR GeneTree; ENSGT00390000015189; -.
DR HOGENOM; CLU_634967_0_0_1; -.
DR InParanoid; P34474; -.
DR OMA; TIGHAPM; -.
DR OrthoDB; 1117968at2759; -.
DR PRO; PR:P34474; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001955; Expressed in larva and 4 other tissues.
DR GO; GO:0005634; C:nucleus; 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..431
FT /note="Helix-loop-helix protein 11"
FT /id="PRO_0000127509"
FT DOMAIN 112..163
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 88..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 109..136
FT /note="RSRMRRQIANCNERRRMQSINAGFLALR -> SIDPECVGKLPIATSGGGCR
FT ASMRDSWL (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_020161"
FT VAR_SEQ 110..111
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_020162"
FT VAR_SEQ 137..431
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_020163"
FT MUTAGEN 112..389
FT /note="Missing: In jh139; reduces brood size and body
FT length."
FT /evidence="ECO:0000269|PubMed:19855932"
SQ SEQUENCE 431 AA; 46108 MW; 096E928B8B293661 CRC64;
MVRSDSAEED QIIIDDGFDL TEEDEEMMSS GTGALPVTIA DWNSVTNARM APPSIMSAAS
AFDLTASGMQ NSLRSVLPTS TIGHAPMLAN RSLSQPAPLS PTSLDPDRRS RMRRQIANCN
ERRRMQSINA GFLALRALLP RKEGEKLSKA AILQQTADMV HQLLGHKGED IPDGGEPKKL
KLEEDHHDAD HQAQIAHLQT ILETERAARK ALESQVIQLR ELLQMTTTSS QASSPVTPRS
NGSGGFTLPS SYASSALPTP LRESPERKPS FQDTTSTPLS LLTLNGSPTS SESLASQRIF
HPPPTLPSLE TTVIRPTPLP PISVEISSPS LSTPSPLTAA PIIFSTAVPT QSSILFQTAA
AAVTSAMSTG NSTPVALPHH LQGHNSAFVS TQPSLTLSQS MQTIVEAIRH LEGSHFIPTS
PPPTSQTSLV R
