Abstract
Cloned cDNAs corresponding to the mitochondrial uncoupling protein of rat brown adipose tissue have been sequenced and the complete amino acid sequence of this unique membranous component is given. The N-terminal sequence of this protein is almost identical to the 14-residue N-terminal sequence previously determined by others for the hamster uncoupling protein. The uncoupling protein has no N-terminal signal extension. We found a significant sequence homology between the uncoupling protein and the ADP/ATP carrier and propose that the nucleotide binding site of the uncoupling protein is localized at the C-terminal end.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adipose Tissue, Brown / metabolism*
-
Amino Acid Sequence
-
Animals
-
Binding Sites
-
Carrier Proteins*
-
Cricetinae
-
DNA / analysis
-
Intracellular Membranes / metabolism
-
Ion Channels
-
Membrane Proteins / analysis*
-
Mitochondria / metabolism
-
Mitochondrial ADP, ATP Translocases / genetics
-
Mitochondrial Proteins
-
RNA, Messenger / genetics
-
Rats
-
Recombinant Proteins / analysis
-
Sequence Homology, Nucleic Acid
-
Uncoupling Protein 1
Substances
-
Carrier Proteins
-
Ion Channels
-
Membrane Proteins
-
Mitochondrial Proteins
-
RNA, Messenger
-
Recombinant Proteins
-
Uncoupling Protein 1
-
DNA
-
Mitochondrial ADP, ATP Translocases