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J. Biol. Chem., Vol. 263, Issue 25, 12274-12277, Sep, 1988
LP Kozak, JH Britton, UC Kozak and JM Wells
The mitochondrial uncoupling protein, a protein essential for the
thermogenic properties of brown fat in mammals, is inserted in the inner
mitochondrial membrane by means of six alpha-helical hydrophobic
transmembrane domains. We have sequenced a complete cDNA and parts of the
gene to determine that the mitochondrial uncoupling protein gene is
composed of six exons, each of which encodes a transmembrane domain. We
also show that transcription of the uncoupling protein gene is from a
single start site; however, the use of alternative poly(A) addition signal
sequences results in two mRNAs, the major species of 1221 nucleotides, not
including the poly(A) tail, and a minor species of about 1600 nucleotides.
The 5'-untranslated region of the mRNA is composed of 231 nucleotides, and
the 3'-untranslated region contains 81 nucleotides prior to addition of the
poly(A) tail.
The mitochondrial uncoupling protein gene. Correlation of exon structure to transmembrane domains
Jackson Laboratory, Bar Harbor, Maine 04609.
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