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Database: UniProt
Entry: HLH34_CAEEL
LinkDB: HLH34_CAEEL
Original site: HLH34_CAEEL 
ID   HLH34_CAEEL             Reviewed;         322 AA.
AC   P90953; Q963J3;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 3.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Helix-loop-helix 34;
GN   Name=hlh-34; ORFNames=T01D3.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|EMBL:CAB03258.2};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=11427734; DOI=10.1073/pnas.141234698;
RA   Jiang H., Guo R., Powell-Coffman J.A.;
RT   "The Caenorhabditis elegans hif-1 gene encodes a bHLH-PAS protein that is
RT   required for adaptation to hypoxia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7916-7921(2001).
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, AND TISSUE SPECIFICITY.
RX   PubMed=22768843; DOI=10.1016/j.cmet.2012.05.014;
RA   Cunningham K.A., Hua Z., Srinivasan S., Liu J., Lee B.H., Edwards R.H.,
RA   Ashrafi K.;
RT   "AMP-activated kinase links serotonergic signaling to glutamate release for
RT   regulation of feeding behavior in C. elegans.";
RL   Cell Metab. 16:113-121(2012).
RN   [4]
RP   FUNCTION.
RX   PubMed=34165428; DOI=10.7554/elife.64903;
RA   Berghoff E.G., Glenwinkel L., Bhattacharya A., Sun H., Varol E.,
RA   Mohammadi N., Antone A., Feng Y., Nguyen K., Cook S.J., Wood J.F.,
RA   Masoudi N., Cros C.C., Ramadan Y.H., Ferkey D.M., Hall D.H., Hobert O.;
RT   "The Prop1-like homeobox gene unc-42 specifies the identity of synaptically
RT   connected neurons.";
RL   Elife 10:0-0(2021).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=34604715; DOI=10.17912/micropub.biology.000467;
RA   Cook S.J., Vidal B., Hobert O.;
RT   "The bHLH-PAS gene hlh-34 is expressed in the AVH, not AVJ interneurons.";
RL   MicroPubl. Biol. 2021:0-0(2021).
CC   -!- FUNCTION: Transcription factor (By similarity). Involved in specifying
CC       AVH neuron identity, acting in concert with unc-42 (PubMed:34165428).
CC       Involved in serotonin-mediated feeding behavior, probably acting by
CC       modulating expression of genes involved in glutamate signaling
CC       (PubMed:22768843). {ECO:0000250|UniProtKB:Q14190,
CC       ECO:0000269|PubMed:22768843, ECO:0000269|PubMed:34165428}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. {ECO:0000250|UniProtKB:Q14190}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- TISSUE SPECIFICITY: Expressed in a small subset of neurons, probably
CC       AVJL and AVJR (PubMed:22768843). Expressed in the AVH neurons
CC       (PubMed:34604715). {ECO:0000269|PubMed:22768843,
CC       ECO:0000269|PubMed:34604715}.
CC   -!- CAUTION: Was reported to probably be expressed in the AVJL and AVJR
CC       neurons (PubMed:22768843). However, this has been claimed to be an
CC       anatomical error and that expression is restricted to the AVH neurons
CC       (PubMed:34604715). {ECO:0000269|PubMed:22768843,
CC       ECO:0000269|PubMed:34604715}.
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DR   EMBL; AF370362; AAK52515.1; -; mRNA.
DR   EMBL; BX284605; CAB03258.2; -; Genomic_DNA.
DR   PIR; T24292; T24292.
DR   RefSeq; NP_506391.2; NM_073990.3.
DR   AlphaFoldDB; P90953; -.
DR   SMR; P90953; -.
DR   BioGRID; 44875; 2.
DR   IntAct; P90953; 2.
DR   STRING; 6239.T01D3.2.1; -.
DR   PaxDb; 6239-T01D3-2; -.
DR   EnsemblMetazoa; T01D3.2.1; T01D3.2.1; WBGene00011327.
DR   GeneID; 179860; -.
DR   KEGG; cel:CELE_T01D3.2; -.
DR   UCSC; T01D3.2; c. elegans.
DR   AGR; WB:WBGene00011327; -.
DR   WormBase; T01D3.2; CE30446; WBGene00011327; hlh-34.
DR   eggNOG; KOG3559; Eukaryota.
DR   HOGENOM; CLU_863913_0_0_1; -.
DR   InParanoid; P90953; -.
DR   OMA; SALNYCD; -.
DR   OrthoDB; 5396877at2759; -.
DR   PhylomeDB; P90953; -.
DR   PRO; PR:P90953; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00011327; Expressed in pharyngeal muscle cell (C elegans) and 1 other cell type or tissue.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0043050; P:nematode pharyngeal pumping; IMP:UniProtKB.
DR   GO; GO:0048665; P:neuron fate specification; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB.
DR   CDD; cd11391; bHLH_PAS; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   PANTHER; PTHR23043; HYPOXIA-INDUCIBLE FACTOR 1 ALPHA; 1.
DR   PANTHER; PTHR23043:SF26; PROTEIN TRACHEALESS; 1.
DR   Pfam; PF00989; PAS; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..322
FT                   /note="Helix-loop-helix 34"
FT                   /id="PRO_0000127443"
FT   DOMAIN          8..62
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          82..152
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140,
FT                   ECO:0000305"
FT   DOMAIN          203..276
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q14190,
FT                   ECO:0000255|PROSITE-ProRule:PRU00140"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   322 AA;  36762 MW;  487A9403447337CD CRC64;
     METNLSEEKQ KPSKSQAQQR RQMENYEFSQ LANELPLARA ISGQHIDKTT MVRLATAYIK
     LHNIFGQSQR AYSSADYYYG SDSLWTNNHL DLLDGFFVIL DRRGDVLYIS ETISIYLGLS
     QVEMTGNAMV DYIHEQDINC FNSALNYCDL NWPQMCNVRV KSSLTKRANK DAVRASPGYK
     VLRLEITMGP NTNTRMIACY PMPTPVLSTV TIPSNSFVII TSIDLHITFA DEKAHQLLNN
     PFYPDSNIKG MSLYSLIDIS DSEVISKMHF DIFNLGAYKT PYYRMILNQT SETFYVESNI
     FRHTSISSKQ FNDSITFVSS IL
//
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