Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
The complete primary structure of an integral membrane glycoprotein of the nuclear pore was deduced from the cDNA sequence. The cDNA encodes a polypeptide of 204,205 D containing a 25-residue-long signal sequence, two hydrophobic segments that could function as transmembrane segments, and 13 potential N-linked oligosaccharide addition sites. Endoglycosidase H reduces the molecular mass by approximately 9 kD suggesting that not all of these 13 sites are used. We discuss possible models for the topology of this protein in the pore membrane as well as a possible role in the formation of pores and pore complexes.
Wozniak
R W
RW
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021.
Bartnik
E
E
Blobel
G
G
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D006596:Hexosaminidases / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000235:genetics / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009685:Nuclear Envelope / Q000032:analysis* / Q000648:ultrastructure; D051381:Rats; D012995:Solubility
D008562:Membrane Glycoproteins; D004247:DNA; D006596:Hexosaminidases