DAF38_CAEEL
ID DAF38_CAEEL Reviewed; 415 AA.
AC Q9U320;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=G-protein coupled receptor daf-38 {ECO:0000305};
DE AltName: Full=Abnormal dauer formation protein 38 {ECO:0000312|WormBase:Y105C5A.23};
GN Name=daf-38 {ECO:0000312|WormBase:Y105C5A.23};
GN ORFNames=Y105C5A.23 {ECO:0000312|WormBase:Y105C5A.23};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=22665789; DOI=10.1073/pnas.1202216109;
RA Park D., O'Doherty I., Somvanshi R.K., Bethke A., Schroeder F.C., Kumar U.,
RA Riddle D.L.;
RT "Interaction of structure-specific and promiscuous G-protein-coupled
RT receptors mediates small-molecule signaling in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:9917-9922(2012).
CC -!- FUNCTION: G-protein coupled receptor (GPCR) that forms a heterodimer
CC with daf-37 to control dauer formation and behavior. Required for the
CC response to dauer inducing pheromones such as the ascarosides ascr#2,
CC ascr#3 and ascr#5. {ECO:0000269|PubMed:22665789}.
CC -!- SUBUNIT: Heterodimer; with daf-37. {ECO:0000269|PubMed:22665789}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the ASI and ASK chemosensory neurons
CC and in the IL-2 interneurons, but weakly expressed in other head
CC neurons in hermaphrodites. {ECO:0000269|PubMed:22665789}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BX284604; CAB60305.1; -; Genomic_DNA.
DR RefSeq; NP_502887.1; NM_070486.3.
DR AlphaFoldDB; Q9U320; -.
DR SMR; Q9U320; -.
DR ComplexPortal; CPX-4628; daf-37-daf-38 complex.
DR IntAct; Q9U320; 1.
DR STRING; 6239.Y105C5A.23; -.
DR PaxDb; Q9U320; -.
DR PRIDE; Q9U320; -.
DR EnsemblMetazoa; Y105C5A.23.1; Y105C5A.23.1; WBGene00013642.
DR GeneID; 178443; -.
DR KEGG; cel:CELE_Y105C5A.23; -.
DR UCSC; Y105C5A.23; c. elegans.
DR CTD; 178443; -.
DR WormBase; Y105C5A.23; CE24056; WBGene00013642; daf-38.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244841; -.
DR HOGENOM; CLU_009579_15_7_1; -.
DR InParanoid; Q9U320; -.
DR OMA; IWEIARL; -.
DR OrthoDB; 858238at2759; -.
DR PhylomeDB; Q9U320; -.
DR Reactome; R-CEL-391906; Leukotriene receptors.
DR Reactome; R-CEL-416476; G alpha (q) signalling events.
DR PRO; PR:Q9U320; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00013642; Expressed in larva and 3 other tissues.
DR GO; GO:0038039; C:G protein-coupled receptor heterodimeric complex; IPI:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:WormBase.
DR GO; GO:1904066; P:G protein-coupled receptor signaling pathway involved in dauer larval development; IMP:WormBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0043949; P:regulation of cAMP-mediated signaling; IC:ComplexPortal.
DR GO; GO:1905909; P:regulation of dauer entry; IC:ComplexPortal.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..415
FT /note="G-protein coupled receptor daf-38"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436099"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..108
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..222
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..382
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 107..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 415 AA; 47440 MW; A5F5BD71095A5BDC CRC64;
MLLPSNLTTS TLMTSSSESY DADNPGLPPE PILSDYVEMF TLVLNFIVGA PLNLAAYTQL
SERPTSTRLD LLKRSLNYSD LLVLFIYVPS RACWLLTYDW RGGDALCKIV KMFHTFAFQS
SSNVIVCIAV DRLLSVLSPS HHSPNKALKR TKMMLIVAWI VALVISCPQL FIWKAYLALP
EYNWSQCLQI WEIARMEKFN KPQVVPEFDA EFWYSILHIS LVFWIPCIII MLSYIIVISW
VWINSRPSIR HTSSFSFHTG CDTVDTVLTR ASEWNPLKTF SRHVNIKEPE KPMTTPRIVV
SDETEVPLTQ RPSISPSEAS AVMRTGVHTS TSYNANLNRS RALRVSLLLV VAYIICWLPY
NLISLIQFLD RDFFSSYLKH VHFCQQLIIF NSVVNPWLYG FFGPRRPSTT GAGRH
