Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
A seven-transmembrane receptor that mediates avoidance response to dihydrocaffeic acid, a water-soluble repellent in Caenorhabditis elegans.
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DCAR-1 is a novel seven-transmembrane receptor for the water-soluble repellent dihydrocaffeic acid (DHCA), expressed in the ASH avoidance sensory neurons; dcar-1 mutants are defective in DHCA avoidance and ASH-specific expression rescues the defect.
"we identified a candidate dihydrocaffeic acid receptor (DCAR), DCAR-1. DCAR-1 is a novel seven-transmembrane protein that is expressed in the ASH avoidance sensory neurons of C. elegans."
Activation of a G protein-coupled receptor by its endogenous ligand triggers the innate immune response of Caenorhabditis elegans.
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DCAR-1 was the sole hit from an RNAi screen of 1,150 GPCR genes required for infection- and wounding-induced antimicrobial peptide expression, acting upstream of (or in parallel to) the Galpha protein GPA-12 in the epidermal p38 MAPK pathway.
"dcar-1 emerged alone as an innate immune receptor gene acting upstream of (or in parallel to) gpa-12"
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The tyrosine-derived metabolite HPLA is an endogenous damage-associated ligand for DCAR-1 that increases upon infection and cuticle damage and drives DCAR-1-dependent antimicrobial peptide expression in the epidermis.
"the tyrosine derivative 4-hydroxyphenyllactic acid (HPLA) as an endogenous ligand"
Deep research report (Edison/falcon) for C. elegans dcar-1