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Family 2.A.5 - ZIP (ZRT IRT-like Protein Family)

Family ID: 52616
Members of the ZIP family consist of 220-430 amino acyl residues
with eight putative transmembrane spanners. They are derived from
animals, plants and yeast, bacteria and archaea. They comprise
a diverse family, with several paralogues in any one organism
(e.g., twelve in humans, at least five in Caenorhabditis elegans
and Arabidopsis thaliana, and two in Saccharomyces cervisiae).
The two S. cerevisiae proteins, Zrt1 and Zrt2, both probably transport
Zn2+ with high specificity, but Zrt1 transports Zn2+ with ten-fold
higher affinity than Zrt2. Some members of the ZIP family have
been shown to transport Zn2+ while others transport Fe2+, and
at least one transports a range of metal ions. One human protein
member of the ZIP family is designated "growth arrest inducible
gene product," but its presumed transport activity has not
been identified. The energy source for transport has not been
characterized, but these systems probably function as secondary
carriers. In one study, uptake of Zn2+ via the hZip2 permease
was energy independent, independent of Na+ and K+ gradients, but
stimulated by HCO3- (Gaither and Eide, 2000). The authors propose
a Zn2+:HCO3- symport mechanism. hZip1 is the major Zn2+ uptake
system in many human tissues (Gaither and Eide, 2001).
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Mäser
P, Thomine S, Schroeder JI, Ward JM, Hirschi K, Sze H, Talke
IN, Amtmann A, Maathuis FJM, Sanders D, Harper JH, Tchieu
J, Gribskov M, Persans MW, Salt DE, Kim SA, Guerinot ML (2001)
Phylogenetic relationships within cation-transporter families
of Arabidopsis thaliana. Plant Physiol 2001 Aug;126(4):1646-67
Eng BH, Guerinot ML, Eide D, Saier MH Jr.
Sequence analyses and phylogenetic characterization
of the ZIP family of metal ion transport proteins.
J Membr Biol. 1998 Nov 1;166(1):1-7. Review.
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