title: Primary structure of bovine endothelin ETB receptor and identification of signal peptidase and metal proteinase cleavage sites.
abstract: A cDNA clone corresponding to the entire coding region of the bovine ETB endothelin receptor mRNA was isolated from a lung cDNA library and sequenced. The cDNA encodes 441 amino acids: 26 constituting an NH2-terminal signal peptide and 415 constituting the mature receptor. The signal peptidase cleavage site was determined by direct amino acid sequencing of purified receptor. A comparison of the predicted amino acid sequence with the available bovine ETA and rat ETB endothelin receptor sequences revealed 63 and 85% homology, respectively. Endothelin receptors of various species are known to be very sensitive to a certain metal proteinase(s) and have been shown to be converted to a lower Mr form in the absence of EDTA. The metal proteinase cleavage site was also determined by direct protein sequencing of the proteolysis product. The amino acid sequence (Ala-Gly-X-Pro-Pro-Arg) surrounding the cleavage site (between Ala-79 and Gly-80) is conserved among the ETB endothelin receptors, explaining the above mentioned proteolytic conversion from the higher to lower Mr forms observed in various species.
authors.affiliation: Department of Biological Sciences, Tokyo Institute of Technology, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Saito
authors.forename: T
authors.initials: T
authors.lastname: Mizuno
authors.forename: M
authors.initials: M
authors.lastname: Itakura
authors.forename: Y
authors.initials: Y
authors.lastname: Suzuki
authors.forename: T
authors.initials: T
authors.lastname: Ito
authors.forename: H
authors.initials: H
authors.lastname: Hagiwara
authors.forename: S
authors.initials: S
authors.lastname: Hirose
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA; D010450:Endopeptidases / Q000378:metabolism*; D016232:Endothelins / Q000378:metabolism*; D008565:Membrane Proteins; D008666:Metalloendopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism; D017466:Receptors, Endothelin; D015183:Restriction Mapping; D016415:Sequence Alignment; D012697:Serine Endopeptidases
chemical_list: D016232:Endothelins; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; D017466:Receptors, Endothelin; D004247:DNA; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase; D008666:Metalloendopeptidases