Tandem sequence repeats in transmembrane channel proteins.
The flow of ions and small molecules out of and between cells is mediated by various classes of transmembrane proteins. One group of putative channel proteins, including the abundant lens protein MIP, is widely distributed from prokaryotes to vertebrates. This article suggests that these proteins contain a structural twofold repeat and may have arisen by gene duplication. Such a model has implications for the tertiary structures of these important proteins.
Wistow
G J
GJ
Laboratory of Molecular and Developmental Biology, National Eye Institute, NIH, Bethesda, MD 20892.
Pisano
M M
MM
Chepelinsky
A B
AB
D000595:Amino Acid Sequence; D020346:Aquaporins; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics; D029721:Drosophila Proteins; D029968:Escherichia coli Proteins; D005136:Eye Proteins / Q000235:genetics*; D007473:Ion Channels; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000235:genetics; D012091:Repetitive Sequences, Nucleic Acid / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
D020346:Aquaporins; D001425:Bacterial Outer Membrane Proteins; D029721:Drosophila Proteins; D029968:Escherichia coli Proteins; D005136:Eye Proteins; D007473:Ion Channels; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D010940:Plant Proteins; C030328:aquaporin 0; C070621:bib protein, Drosophila; C045625:nodulin; C078043:GlpF protein, E coli