DAF37_CAEEL
ID DAF37_CAEEL Reviewed; 482 AA.
AC Q18321;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=G-protein coupled receptor daf-37 {ECO:0000305};
DE AltName: Full=Abnormal dauer formation protein 37 {ECO:0000312|WormBase:C30B5.5};
GN Name=daf-37 {ECO:0000312|WormBase:C30B5.5};
GN ORFNames=C30B5.5 {ECO:0000312|WormBase:C30B5.5};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=23509272; DOI=10.1073/pnas.1214467110;
RA Ludewig A.H., Izrayelit Y., Park D., Malik R.U., Zimmermann A., Mahanti P.,
RA Fox B.W., Bethke A., Doering F., Riddle D.L., Schroeder F.C.;
RT "Pheromone sensing regulates Caenorhabditis elegans lifespan and stress
RT resistance via the deacetylase SIR-2.1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5522-5527(2013).
CC -!- FUNCTION: G-protein coupled receptor (GPCR) that forms a heterodimer
CC with daf-38 to control dauer formation and behavior (PubMed:22665789,
CC PubMed:23509272). Receptor for the ascaroside pheromone ascr#2
CC (PubMed:22665789). Required for the response to dauer inducing
CC pheromones, specifically the ascaroside ascr#2 (PubMed:22665789,
CC PubMed:23509272). May serve neuronal specific roles in response to
CC ascr#2 with expression in ASI neurons controlling dauer formation in
CC larvae, and expression in ASK neurons playing a role in longevity and
CC hermaphrodite repulsion (PubMed:22665789, PubMed:23509272). May
CC function upstream of the daf-11, daf-7 and daf-2 signaling pathways
CC (PubMed:22665789). {ECO:0000269|PubMed:22665789,
CC ECO:0000269|PubMed:23509272}.
CC -!- SUBUNIT: Homodimer. Heterodimer; with daf-38.
CC {ECO:0000269|PubMed:22665789}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22665789};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium
CC {ECO:0000269|PubMed:22665789}. Golgi apparatus
CC {ECO:0000269|PubMed:22665789}. Note=Localizes to the cell membrane in
CC the presence of daf-38, but localizes to the Golgi apparatus in the
CC absence of daf-38. {ECO:0000269|PubMed:22665789}.
CC -!- TISSUE SPECIFICITY: Expressed in the ASI and ASK chemosensory neurons,
CC in the IL-2 interneurons, and in the male specific CEM (cephalic
CC sensilla, male) neurons. {ECO:0000269|PubMed:22665789}.
CC -!- DEVELOPMENTAL STAGE: Expressed strongly during the L1 and L2 stages of
CC larval development, but expression is weaker during the subsequent L3
CC and L4 stages of larval development and during the adult stages of
CC development. {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; BX284602; CCD66137.2; -; Genomic_DNA.
DR PIR; T15709; T15709.
DR RefSeq; NP_001309490.1; NM_001322732.1.
DR AlphaFoldDB; Q18321; -.
DR SMR; Q18321; -.
DR ComplexPortal; CPX-4628; daf-37-daf-38 complex.
DR IntAct; Q18321; 1.
DR EnsemblMetazoa; C30B5.5.1; C30B5.5.1; WBGene00016246.
DR GeneID; 183041; -.
DR KEGG; cel:CELE_C30B5.5; -.
DR UCSC; C30B5.5; c. elegans.
DR CTD; 183041; -.
DR WormBase; C30B5.5; CE51245; WBGene00016246; daf-37.
DR HOGENOM; CLU_355342_0_0_1; -.
DR InParanoid; Q18321; -.
DR OrthoDB; 634775at2759; -.
DR PRO; PR:Q18321; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016246; Expressed in larva and 3 other tissues.
DR GO; GO:0038039; C:G protein-coupled receptor heterodimeric complex; IPI:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:1904067; F:ascr#2 binding; IDA:WormBase.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:WormBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:WormBase.
DR GO; GO:1904066; P:G protein-coupled receptor signaling pathway involved in dauer larval development; IMP:WormBase.
DR GO; GO:1904068; P:G protein-coupled receptor signaling pathway involved in social behavior; IMP:WormBase.
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; IPR019427; 7TM_GPCR_serpentine_rcpt_Srw.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF10324; 7TM_GPCR_Srw; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; G-protein coupled receptor; Glycoprotein;
KW Golgi apparatus; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..482
FT /note="G-protein coupled receptor daf-37"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436098"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..113
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 114..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..218
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..305
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..330
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 331..351
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 482 AA; 54261 MW; 7B55F720CF48F447 CRC64;
MDVIGNITDL SPTVSGIPDE CGLEPHDFLE VKFFLISVVG TLIGLFGLFG NATTALILTR
PSMRNPNNLF LTALAVFDSC LLITAFFIYA MEYIIEYTAA FDLYVAWLTY LRFAFALSHI
SQTGSVYITV AVTIERYLAV CHPKSSKNMC GPGGAAWTIL GVTTFAVVFN CTKFFELQVT
VNPSCPDGSN WQSYILLPSA MASNPIYQQV YSLWVTNFVM VFFPFLTLLL FNAIIAYTIR
QSLEKYDFHN QKSVVAALSA SVNLPRNIAG ISSRNELKEK SREATLVLVI IVFIFLGCNF
WGFVLTLLER IMGQETLMVE HHIFYTFSRE AINFLAIINS SINFVIYLLF GKDFRKELVV
VYGCGIRGIS LRLPVQDKFV IWRHWKRTKS RISMNTTNRT RHKISLPQTL VEHANLERLE
ETRFLAHHED GVQTQVSPIH ALRNGSTPKI DTLQDLTSNG RPCKTSIIDD NGTVVCTVTE
FP
