title: Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
abstract: 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.
authors.affiliation: Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021.
authors.forename: R W
authors.initials: RW
authors.lastname: Wozniak
authors.forename: E
authors.initials: E
authors.lastname: Bartnik
authors.forename: G
authors.initials: G
authors.lastname: Blobel
mesh_terms: 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
chemical_list: D008562:Membrane Glycoproteins; D004247:DNA; D006596:Hexosaminidases