Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14.
作者： K.M. Taylor , H.E. Morgan , A. Johnson , R.I. Nicholson
DOI: 10.1016/J.FEBSLET.2004.12.006
关键词: Histidine 、 Zinc 、 Chinese hamster ovary cell 、 Metalloproteinase 、 Transmembrane domain 、 Transporter 、 Transmembrane protein 、 Biology 、 Biochemistry 、 Subfamily
摘要: Here, we report the first investigation of a novel member LZT (LIV-1 subfamily ZIP zinc Transporters) influx transporters. sequences all contain unique and highly conserved metalloprotease motif (HEXPHEXGD) in transmembrane domain V with both histidine residues essential for transport by (Zrt-, Irt-like Proteins) We investigate here whether ZIP14 (SLC39A14), lacking initial this motif, is still able to zinc. demonstrate that plasma membrane located glycosylated protein functions as transporter temperature-dependant manner.
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