Phylogenetic,Structural and Functional Characteristics of the Na-K-Cl Cotransporter Family |
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Authors: | JH Park MH Saier Jr |
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Institution: | (1) Department of Biology, University of California at San Diego, La Jolla, CA 92093-0116, US |
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Abstract: | Summary
Bumetanide-sensitive Na-K-Cl cotransporters and thiazide-sensitive Na-Cl cotransporters comprise a family of integral membrane
transport proteins, the Na-K-Cl cotransporter (NKCC) family. Each of the members of this family is over 1,000 amino acids
in length. We have multiply aligned the ten currently sequenced members of this family from human, rabbit, rodent, shark,
flounder, moth, worm and yeast sources. Phylogenetic analyses suggest the presence of at least six isoforms of these full
length proteins in eukaryotes. Average hydropathy and average similarity plots have been derived revealing that each of these
proteins possesses a central, well conserved, hydrophobic domain of almost invariant length, possibly consisting of twelve
transmembrane α-helical spanners, an N-terminal, poorly conserved, hydrophilic domain of variable length, and a C-terminal,
moderately conserved, hydrophilic domain of moderately constant length. A functionally uncharacterized homologue of this family
occurs in the cyanobacterium Synechococcus sp. Limited sequence similarity of these proteins with members of a family of basic amino acid transporters suggests that the
NKCC family may be distantly related to the previously characterized, ubiquitous, amino acid-polyamine-choline (APC) family
of facilitators. These observations suggest that the NKCC family is an old family that has its roots in the prokaryotic kingdom.
Received: 27 July 1995/Revised: 8 November 1995 |
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Keywords: | : Transport — Salt — Membrane proteins — Topology — Bumetanide — Thiazide — Phylogenies |
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