Neurturin and glial‐cell‐line‐derived neurotrophic factor (GDNF) promote the survival and maintenance of different types of neuronal cells and signal through a receptor complex composed of a ligand binding subunit, either GDNF family receptor α‐1 (GFRα‐1) or α‐2 (GFRα‐2), together with the cRET membrane‐bound protein tyrosine kinase. We have cloned GFRα‐3, a novel receptor belonging to the GFRα family, that is 35 % identical by amino acid sequence to both GFRα‐1 and GFRα‐2. GFRα‐3 is a protein composed of 400 amino acid residues with three potential N‐linked glycosylation sites together with the features characteristic of a glycosyl‐phosphatidylinositol‐anchored membrane protein. The heterologous expression of a FLAG‐tagged GFRα‐3 in human embryonic kidney cells showed that the protein is bound to the cell surface via a glycosyl‐PtdIns anchor and is glycosylated, with different glycoforms migrating on SDS/PAGE with apparent molecular masses ranging over 43−62 kDa. The gene for GFRα‐3 was mapped to human chromosome 5 in a region (q31.1−q31.3) where several disease loci, growth factor and growth factor receptor genes have been localized. Using northern blot analysis or reverse‐transcription PCR, GFRα‐3 was shown to be expressed within the nervous system predominantly in the cerebellum and the spinal cord while in peripheral tissues GFRα‐3 was found to be expressed mostly in the colon, small intestine, pancreas, heart, testis and prostate. Using a GFRα‐3‐specific [35S]cRNA[γS] probe, in situ hybridization histochemistry experiments confirmed the expression in the cerebellum.