GDNF family receptor alpha-1; GFR-alpha-1; glial derived neurotrophic factor [GDNF] receptor alpha-1; TGF-beta-related neurotrophic factor receptor 1; RET ligand 1 (GFRA1, GDNFRA, RETL1, TRNR1)

Function: - receptor for GDNF - mediates the GDNF-induced autophosphorylation & activation of the RET receptor - 2 molecules of GDNFR-alpha are thought to form a complex with the disulfide-linked GDNF dimer & with 2 molecules of RET Structure: - belongs to the GDNFR family - glycosylphosphatidylinositol-linked cell surface receptor Compartment: cell membrane; lipid-anchor, GPI-anchor Alternative splicing: named isoforms=2 Note: may be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay

Related

glial-derived neurotrophic factor; hGDNF; astrocyte-derived trophic factor; ATF (GDNF) proto-oncogene tyrosine-protein kinase receptor ret; C-ret; (RET, CDHF12)

Properties

SIZE: entity length = 465 aa MW = 51 kD COMPARTMENT: plasma membrane CELL-REGION: apical region CELL: epithelial cell MOTIF: signal sequence {1-24} consensus repeat {25-113} MOTIF: cysteine residue {C29} MODIFICATION: cysteine residue {C87} cysteine residue {C36} MODIFICATION: cysteine residue {C42} cysteine residue {C42} MODIFICATION: cysteine residue {C36} cysteine residue {C52} MODIFICATION: cysteine residue {C72} N-glycosylation site {N59} cysteine residue {C72} MODIFICATION: cysteine residue {C52} cysteine residue {C87} MODIFICATION: cysteine residue {C29} cysteine residue {C89} MODIFICATION: cysteine residue {C99} cysteine residue {C99} MODIFICATION: cysteine residue {C89} consensus repeat {150-238} MOTIF: cysteine residue {C154} MODIFICATION: cysteine residue {C214} cysteine residue {C161} MODIFICATION: cysteine residue {C167} cysteine residue {C167} MODIFICATION: cysteine residue {C161} cysteine residue {C178} MODIFICATION: cysteine residue {C192} cysteine residue {C187} MODIFICATION: cysteine residue {C233} cysteine residue {C192} MODIFICATION: cysteine residue {C178} cysteine residue {C214} MODIFICATION: cysteine residue {C154} cysteine residue {C216} MODIFICATION: cysteine residue {C221} cysteine residue {C221} MODIFICATION: cysteine residue {C216} cysteine residue {C233} MODIFICATION: cysteine residue {C187} consensus repeat {239-342} MOTIF: cysteine residue {C243} MODIFICATION: cysteine residue {C313} cysteine residue {C250} MODIFICATION: cysteine residue {C256} cysteine residue {C256} MODIFICATION: cysteine residue {C250} cysteine residue {C267} MODIFICATION: cysteine residue {C285} cysteine residue {C277} MODIFICATION: cysteine residue {C337} cysteine residue {C285} MODIFICATION: cysteine residue {C267} cysteine residue {C313} MODIFICATION: cysteine residue {C243} cysteine residue {C315} MODIFICATION: cysteine residue {C325} cysteine residue {C325} MODIFICATION: cysteine residue {C315} cysteine residue {C337} MODIFICATION: cysteine residue {C277} N-glycosylation site {N347} threonine-rich region {362-369} MOTIF: threonine residue (SEVERAL) N-glycosylation site {N406} glycosyl phosphatidylinositol [GPI] membrane anchor {N429}

Database Correlations

OMIM 601496 UniProt P56159 Pfam PF02351 Kegg hsa:2674

References

UniProt :accession P56159