A hydrophobic transmembrane segment at the carboxyl terminus of thy-1.
The mode of integration of the glycoprotein thy-1 within the cell membrane has been controversial due to an apparent lack of a transmembrane hydrophobic segment. Rat and mouse complementary DNA and genomic clones encoding the thy-1 molecule have been isolated and sequenced. These studies have enabled us to determine the intron-exon organization of the thy-1 gene. Furthermore, they have revealed the existence of a sequence which would encode an extra segment (31 amino acids) at the carboxyl terminus of the thy-1 molecule. These extra amino acids include a 20-amino acid hydrophobic segment which may be responsible for integration of thy-1 within the plasma membrane.
Seki
T
T
Chang
H C
HC
Moriuchi
T
T
Denome
R
R
Ploegh
H
H
Silver
J
J
D000595:Amino Acid Sequence; D000818:Animals; D000954:Antigens, Surface / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D004274:DNA, Recombinant / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D051379:Mice; D008970:Molecular Weight; D009693:Nucleic Acid Hybridization; D051381:Rats; D018800:Thy-1 Antigens
D000954:Antigens, Surface; D004274:DNA, Recombinant; D008565:Membrane Proteins; D018800:Thy-1 Antigens