AHA1_CAEEL
ID AHA1_CAEEL Reviewed; 453 AA.
AC O02219; G5EGG7;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator homolog {ECO:0000250|UniProtKB:O15945, ECO:0000303|PubMed:14757639, ECO:0000303|PubMed:16919260};
DE Short=ARNT {ECO:0000303|PubMed:14757639, ECO:0000303|PubMed:16919260};
DE AltName: Full=AHR-associated protein {ECO:0000303|PubMed:9501178};
GN Name=aha-1 {ECO:0000312|WormBase:C25A1.11a}; ORFNames=C25A1.11;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB99999.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND INTERACTION
RP WITH AHR-1.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:9501178};
RX PubMed=9501178; DOI=10.1073/pnas.95.6.2844;
RA Powell-Coffman J.A., Bradfield C.A., Wood W.B.;
RT "Caenorhabditis elegans orthologs of the aryl hydrocarbon receptor and its
RT heterodimerization partner the aryl hydrocarbon receptor nuclear
RT translocator.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2844-2849(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB02764.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH HIF-1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:11427734};
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 [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:14757639};
RX PubMed=14757639; DOI=10.1242/dev.00959;
RA Huang X., Powell-Coffman J.A., Jin Y.;
RT "The AHR-1 aryl hydrocarbon receptor and its co-factor the AHA-1 aryl
RT hydrocarbon receptor nuclear translocator specify GABAergic neuron cell
RT fate in C. elegans.";
RL Development 131:819-828(2004).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:15136141};
RX PubMed=15136141; DOI=10.1016/j.ydbio.2004.02.004;
RA Qin H., Powell-Coffman J.A.;
RT "The Caenorhabditis elegans aryl hydrocarbon receptor, AHR-1, regulates
RT neuronal development.";
RL Dev. Biol. 270:64-75(2004).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:16919260};
RX PubMed=16919260; DOI=10.1016/j.ydbio.2006.07.017;
RA Qin H., Zhai Z., Powell-Coffman J.A.;
RT "The Caenorhabditis elegans AHR-1 transcription complex controls expression
RT of soluble guanylate cyclase genes in the URX neurons and regulates
RT aggregation behavior.";
RL Dev. Biol. 298:606-615(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH CKY-1.
RX PubMed=17628356; DOI=10.1016/j.gene.2007.06.005;
RA Ooe N., Saito K., Oeda K., Nakatuka I., Kaneko H.;
RT "Characterization of Drosophila and Caenorhabditis elegans NXF-like-
RT factors, putative homologs of mammalian NXF.";
RL Gene 400:122-130(2007).
CC -!- FUNCTION: Transcription factor (PubMed:17628356). Efficient DNA binding
CC requires dimerization with another bHLH protein, such as cky-1 or ahr-1
CC (PubMed:17628356, PubMed:9501178). Regulates transcription of target
CC genes, probably acting in complex with cky-1 (PubMed:17628356). Has a
CC role in cellular differentiation (PubMed:9501178, PubMed:15136141).
CC Required for pharyngeal development (PubMed:14757639). In collaboration
CC with ahr-1 it is involved in RMEL/R and SDQR neuron cell migration
CC (PubMed:14757639). Acts in the cellular response to hypoxia
CC (PubMed:11427734). Involved in aggregation behavior by regulating
CC soluble guanylate cyclase gene expression in the URX neurons
CC (PubMed:16919260). {ECO:0000269|PubMed:11427734,
CC ECO:0000269|PubMed:14757639, ECO:0000269|PubMed:15136141,
CC ECO:0000269|PubMed:16919260, ECO:0000269|PubMed:17628356,
CC ECO:0000269|PubMed:9501178}.
CC -!- SUBUNIT: Interacts with hif-1 (PubMed:11427734). Heterodimer; efficient
CC DNA binding requires dimerization with another bHLH protein
CC (PubMed:17628356, PubMed:9501178). Forms a heterodimer with ahr-1;
CC binds DNA as heterodimer (PubMed:9501178). Forms a heterodimer with PAS
CC domain-containing protein cky-1; binds DNA as heterodimer
CC (PubMed:17628356). {ECO:0000269|PubMed:11427734,
CC ECO:0000269|PubMed:17628356, ECO:0000269|PubMed:9501178}.
CC -!- INTERACTION:
CC O02219; O44712: ahr-1; NbExp=3; IntAct=EBI-2408984, EBI-2409183;
CC O02219; G5EGD2: hif-1; NbExp=3; IntAct=EBI-2408984, EBI-319821;
CC O02219; G5EFA5; NbExp=3; IntAct=EBI-2408984, EBI-313013;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:11427734}. Note=Nuclear location dependent on hif-1
CC expression in intestinal tissue but not in neuronal cells.
CC {ECO:0000269|PubMed:11427734}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:9501178, ECO:0000269|PubMed:9851916};
CC IsoId=O02219-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=O02219-2; Sequence=VSP_042476;
CC -!- TISSUE SPECIFICITY: Expressed in many cell types throughout
CC development, including hypodermal cells, intestinal cells, pharyngeal
CC cells, and neurons. Expressed in every cell during embryo.
CC {ECO:0000269|PubMed:11427734}.
CC -!- DISRUPTION PHENOTYPE: Abnormal cell morphology of developing RMEL/R
CC neurons. Arrested development at larvae life stage due to its
CC requirement in the pharynx. Defects in SDQR neuron cell dorsal-ventral
CC migration. Aggregation behavior is diminished. Abolishes guanylate
CC cyclase gene expression in the URX neurons.
CC {ECO:0000269|PubMed:14757639, ECO:0000269|PubMed:15136141,
CC ECO:0000269|PubMed:16919260}.
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DR EMBL; AF039569; AAB99999.1; -; mRNA.
DR EMBL; Z81038; CAB02764.1; -; Genomic_DNA.
DR EMBL; Z81038; CBH29653.1; -; Genomic_DNA.
DR PIR; T19440; T19440.
DR PIR; T42397; T42397.
DR RefSeq; NP_001251326.1; NM_001264397.1.
DR RefSeq; NP_001251327.1; NM_001264398.1. [O02219-1]
DR AlphaFoldDB; O02219; -.
DR SMR; O02219; -.
DR BioGRID; 38307; 12.
DR ComplexPortal; CPX-4002; Hsp90-cdc-37-aha-1 complex.
DR IntAct; O02219; 11.
DR STRING; 6239.C25A1.11a; -.
DR EPD; O02219; -.
DR PaxDb; O02219; -.
DR PeptideAtlas; O02219; -.
DR EnsemblMetazoa; C25A1.11.1; C25A1.11.1; WBGene00000095. [O02219-1]
DR GeneID; 172889; -.
DR KEGG; cel:CELE_C25A1.11; -.
DR UCSC; C25A1.11; c. elegans. [O02219-1]
DR CTD; 172889; -.
DR WormBase; C25A1.11a; CE08377; WBGene00000095; aha-1. [O02219-1]
DR WormBase; C25A1.11b; CE44231; WBGene00000095; aha-1. [O02219-2]
DR eggNOG; KOG3561; Eukaryota.
DR GeneTree; ENSGT00940000169286; -.
DR HOGENOM; CLU_011864_0_0_1; -.
DR InParanoid; O02219; -.
DR OMA; EYVVATH; -.
DR OrthoDB; 331262at2759; -.
DR PhylomeDB; O02219; -.
DR Reactome; R-CEL-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR PRO; PR:O02219; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000095; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0101031; C:chaperone complex; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:WormBase.
DR GO; GO:0003677; F:DNA binding; IDA:WormBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:WormBase.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0001708; P:cell fate specification; IMP:UniProtKB.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; TAS:WormBase.
DR GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0022417; P:protein maturation by protein folding; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:WormBase.
DR GO; GO:0035176; P:social behavior; IMP:UniProtKB.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001067; Nuc_translocat.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00785; NCTRNSLOCATR.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Nucleus;
KW Receptor; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..453
FT /note="Aryl hydrocarbon receptor nuclear translocator
FT homolog"
FT /id="PRO_0000416049"
FT DOMAIN 44..97
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 115..193
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 277..347
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 348..392
FT /note="PAC"
FT /evidence="ECO:0000255"
FT REGION 410..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 274..275
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9501178,
FT ECO:0000303|PubMed:9851916"
FT /id="VSP_042476"
SQ SEQUENCE 453 AA; 51037 MW; B00FFE005C9B0BCB CRC64;
MAQDIFMDPW QSATSFAMED EDMGMPSGKY ARMEDEMGEN KERFARENHS EIERRRRNKM
THYINELAEM VPQCASLGRK PDKLTILRMA VSHMKGIRGH TAQDETSYKP SFLTDQELKH
LILEAANGFL FVVCCQTGKV LYVADSITPV LNLKQEDWLQ RNLNELIHPD DQDKIRDQLC
GSEVSVNKVL DLKSGSVKRE GASTRVHMSC RRGFICRMRV GALEPLHRLR NRRPLFQHAG
QNYVVMHCTG YIKNAPPQGI NAPASSCLVA IARLQVASMP VCADPTSTNQ FSVRVSEDGK
MTFIDARVSD LIGLSSDQLI GRYWWNLAHP ADEKTLQDSF VALLSDQPMR INIRVRTSTD
YIPCTVSAYK FMNPYSEQFE YVVATHQIAP QEDINNWVTA PTVPQPQASE FGELGGAPSA
VDYGQSSSGG WRPEAQGAPQ AQWQWDPMNG YNQ
