AHR_CAEEL
ID AHR_CAEEL Reviewed; 602 AA.
AC O44712; Q564W4; Q93369;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Aryl hydrocarbon receptor protein 1 {ECO:0000312|EMBL:AAC00000.1};
DE Flags: Precursor;
GN Name=ahr-1 {ECO:0000312|EMBL:AAC00000.1, ECO:0000312|WormBase:C41G7.5a};
GN ORFNames=C41G7.5;
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:AAC00000.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND INTERACTION WITH
RP DAF-21.
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:0000312|EMBL:CAB51463.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB51463.1};
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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 [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=18524955; DOI=10.1073/pnas.0707469105;
RA Hallem E.A., Sternberg P.W.;
RT "Acute carbon dioxide avoidance in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8038-8043(2008).
RN [7] {ECO:0000305}
RP INTERACTION WITH AHA-1.
RX PubMed=19632181; DOI=10.1016/j.cell.2009.04.058;
RA Grove C.A., De Masi F., Barrasa M.I., Newburger D.E., Alkema M.J.,
RA Bulyk M.L., Walhout A.J.M.;
RT "A multiparameter network reveals extensive divergence between C. elegans
RT bHLH transcription factors.";
RL Cell 138:314-327(2009).
CC -!- FUNCTION: Probable ligand-activated transcriptional activator. Acts as
CC a transcriptional regulator in GABAergic motor neuron cell fate
CC specification and development. Promotes cell-type-specific expression
CC of guanylate cyclase genes that have key roles in aggregation behavior
CC and hyperoxia avoidance. Has no role in carbon dioxide avoidance.
CC {ECO:0000269|PubMed:14757639, ECO:0000269|PubMed:15136141,
CC ECO:0000269|PubMed:16919260, ECO:0000269|PubMed:18524955,
CC ECO:0000269|PubMed:9501178}.
CC -!- SUBUNIT: Interacts with daf-21/hsp90. Interacts with aha-1.
CC {ECO:0000269|PubMed:19632181, ECO:0000269|PubMed:9501178}.
CC -!- INTERACTION:
CC O44712; O02219: aha-1; NbExp=3; IntAct=EBI-2409183, EBI-2408984;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:9501178};
CC IsoId=O44712-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=O44712-2; Sequence=VSP_053164;
CC -!- TISSUE SPECIFICITY: Expressed in many distinct neuronal cells including
CC RMED, RMEV, RMEL and RMER. Functions in URX neurons to promote
CC aggregation behavior. {ECO:0000269|PubMed:14757639,
CC ECO:0000269|PubMed:15136141, ECO:0000269|PubMed:16919260}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic and larval development.
CC {ECO:0000269|PubMed:15136141}.
CC -!- DISRUPTION PHENOTYPE: Defects in neuronal differentiation, axon
CC branching, aberrant cell migration and abnormal aggregation behavior on
CC lawns of bacterial food. {ECO:0000269|PubMed:14757639,
CC ECO:0000269|PubMed:15136141, ECO:0000269|PubMed:16919260}.
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DR EMBL; AF039570; AAC00000.1; -; mRNA.
DR EMBL; Z81048; CAB51463.1; -; Genomic_DNA.
DR EMBL; Z81048; CAI79126.1; -; Genomic_DNA.
DR PIR; T19898; T19898.
DR RefSeq; NP_001021036.1; NM_001025865.3. [O44712-1]
DR RefSeq; NP_001021037.1; NM_001025866.3. [O44712-2]
DR AlphaFoldDB; O44712; -.
DR SMR; O44712; -.
DR BioGRID; 38214; 1.
DR IntAct; O44712; 2.
DR STRING; 6239.C41G7.5a; -.
DR PaxDb; O44712; -.
DR PRIDE; O44712; -.
DR EnsemblMetazoa; C41G7.5a.1; C41G7.5a.1; WBGene00000096. [O44712-1]
DR EnsemblMetazoa; C41G7.5b.1; C41G7.5b.1; WBGene00000096. [O44712-2]
DR GeneID; 172788; -.
DR KEGG; cel:CELE_C41G7.5; -.
DR UCSC; C41G7.5a; c. elegans.
DR CTD; 172788; -.
DR WormBase; C41G7.5a; CE20561; WBGene00000096; ahr-1. [O44712-1]
DR WormBase; C41G7.5b; CE38293; WBGene00000096; ahr-1. [O44712-2]
DR eggNOG; KOG3560; Eukaryota.
DR GeneTree; ENSGT00940000154486; -.
DR InParanoid; O44712; -.
DR OMA; FLQCKAH; -.
DR OrthoDB; 554030at2759; -.
DR PhylomeDB; O44712; -.
DR PRO; PR:O44712; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000096; Expressed in anatomical system and 4 other tissues.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:WormBase.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; TAS:WormBase.
DR GO; GO:0040013; P:negative regulation of locomotion; IMP:WormBase.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:WormBase.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR039091; AHR/AHRR.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR PANTHER; PTHR10649; PTHR10649; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Behavior; DNA-binding; Neurogenesis;
KW Nucleus; Receptor; Reference proteome; Transcription;
KW Transcription regulation.
FT PROPEP 1..2
FT /evidence="ECO:0000250|UniProtKB:P30561, ECO:0000255"
FT /id="PRO_0000388706"
FT CHAIN 3..602
FT /note="Aryl hydrocarbon receptor protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000388707"
FT DOMAIN 18..71
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 126..196
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053164"
SQ SEQUENCE 602 AA; 68232 MW; 6A891C2950B3FD36 CRC64;
MYASKRRQRN FKRVRDPPKQ LTNTNPSKRH RERLNGELET VAMLLPYDSS TISRLDKLSV
LRLAVSFLQC KAHFQACLHN SQFLSAGFPM STHSYSYQPH PPIPFSNKVP TIFDLRIGTP
MLDPEESNFE EISLKSLGGF ILVLNDNGEI YYASENVENY LGFHQSDVLH QPVYDLIHSE
DRDDIRQQLD SNFHIPTSSA SNQFDVFAPQ NSKYLERNVN ARFRCLLDNT CGFLRIDMRG
KLMSLHGLPS SYVMGRTASG PVLGMICVCT PFVPPSTSDL ASEDMILKTK HQLDGALVSM
DQKVYEMLEI DETDLPMPLY NLVHVEDAVC MAEAHKEAIK NGSSGLLVYR LVSTKTRRTY
FVQSSCRMFY KNSKPESIGL THRLLNEVEG TMLLEKRSTL KAKLLSFDDS FLQSPRNLQS
TAALPLPSVL KDDQDCLEPS TSNSLFPSVP VPTPTTTKAN RRRKENSHEI VPTIPSIPIP
THFDMQMFDP SWNHGVHPPA WPHDVYHLTQ YPPTYPHPPG TVGYPDVQIA PVDYPGWHPN
DIHMTQLPHG FTPDAQKLVP PHPQMSHFTE YPTPSTHHDL HHHPLKQDNF HLISEVTNLL
GT
