Molecular characteristics of the N-terminal region of the quail follitropin receptor.
We determined the primary structure of follitropin receptor (FSH-R) at its N-terminal extracellular domain, which is the key region of specific hormone binding in avian (quail) species. In this region, quail FSH-R showed about 70% homology with mammalian FSH-Rs at the level of predicted amino acid sequences. The leucine-rich repetitive motif which is conserved in all mammalian FSH-Rs was also detected in the quail FSH-R. However, some unique amino acid replacements were found at the positions of cystein residues and potential N-linked glycosylation sites. The sequence of the quail lutropin receptor (LH-R) previously defined by us showed a homology between FSH-R and LH-R of 47.4%. This value is close to those between mammalian FSH-Rs and LH-Rs, which in the corresponding region are human, 50.3%; rat, 50.9%.
Akazome
Y
Y
Department of Biological Sciences, Graduate School of Science, University of Tokyo, Japan.
Shimizu
F
F
Park
M K
MK
Mori
T
T
Kawashima
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003370:Coturnix / Q000378:metabolism*; D005260:Female; D006736:Horses / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D051381:Rats; D011962:Receptors, FSH / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D011962:Receptors, FSH