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PMID: 6546784 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum.

Nature ·Vol. 308 ·No. 5960 ·1984-00-00 ·Pages 613-7

Chin DJ, Gil G, Russell DW, Liscum L, Luskey KL, Basu SK, Okayama H, Berg P, Goldstein JL, Brown MS

Abstract

The nucleotide sequence of a 4.8-kilobase mRNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase, the endoplasmic reticulum enzyme that controls cholesterol biosynthesis, shows that it is a protein of 887 amino acids (molecular weight 97,092) which contains three potential sites for asparagine-linked glycosylation. The reductase is a transmembrane glycoprotein, but in contrast to many other transmembrane glycoproteins, it lacks a cleavable or hydrophobic NH2-terminal signal sequence.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cell Line Cloning, Molecular Cricetinae Cricetulus DNA/metabolism Endoplasmic Reticulum/enzymology Female Glycoproteins/genetics Hydroxymethylglutaryl CoA Reductases/genetics Molecular Weight Ovary Plasmids RNA, Messenger/genetics
Chemicals
Glycoproteins RNA, Messenger DNA Hydroxymethylglutaryl CoA Reductases
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Chin D J
Gil G
Russell D W
Liscum L
Luskey K L
Basu S K
Okayama H
Berg P
Goldstein J L
Brown M S
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1984-00-00
Pages
613-7
Language
English
Region
England
NLM ID
0410462
Subset
IM
Databases
GENBANK
L00165, L00166, L00169, L00170, L00171, L00173, L00176, L00177, L00178, L00179, L00180, L00181, L00182, L00183, X00494
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