The nucleotide sequence of Syrian hamster HMG-CoA reductase cDNA.
We have determined the nucleotide sequence of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase cDNA. Comparison of the deduced amino acid sequence with the homologous sequence from Chinese hamster reveals highly conserved domains which appear to have functional significance. The amino-terminal membrane domain of HMG-CoA reductase exhibits 100% homology. This region may span the endoplasmic reticulum seven times and is thought to be involved in the sterol-regulated degradation of HMG-CoA reductase (Gil et al., 1985; Liscum et al., 1985). The carboxyl terminus contains the active site of the enzyme and exhibits greater than 99% homology. A central region linking these two conserved domains exhibits greater divergence. In this region there is only 85% homology between the two hamster lines, suggesting that this linkage domain has a less stringent structural requirement.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D003001:Cloning, Molecular; D006224:Cricetinae / Q000235:genetics*; D003412:Cricetulus / Q000235:genetics; D004247:DNA / Q000235:genetics*; D006903:Hydroxymethylglutaryl CoA Reductases / Q000235:genetics*; D008647:Mesocricetus / Q000235:genetics*; D013045:Species Specificity
D004247:DNA; D006903:Hydroxymethylglutaryl CoA Reductases