Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14.
Here, we report the first investigation of a novel member of the LZT (LIV-1 subfamily of ZIP zinc Transporters) subfamily of zinc influx transporters. LZT subfamily sequences all contain a unique and highly conserved metalloprotease motif (HEXPHEXGD) in transmembrane domain V with both histidine residues essential for zinc transport by ZIP (Zrt-, Irt-like Proteins) transporters. We investigate here whether ZIP14 (SLC39A14), lacking the initial histidine in this motif, is still able to transport zinc. We demonstrate that this plasma membrane located glycosylated protein functions as a zinc influx transporter in a temperature-dependant manner.
Taylor
K M
KM
Tenovus Cancer Research Centre, Welsh School of Pharmacy, Cardiff University, Redwood Building, King Edward VII avenue, Cardiff CF10 3XF, UK. Taylorkm@cardiff.ac.uk
Morgan
H E
HE
Johnson
A
A
Nicholson
R I
RI
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001693:Biological Transport, Active / Q000502:physiology; D016466:CHO Cells; D027682:Cation Transport Proteins / Q000032:analysis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry; D006224:Cricetinae; D003412:Cricetulus; D006031:Glycosylation; D006801:Humans; D017136:Ion Transport / Q000502:physiology; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D014018:Tissue Distribution; D015032:Zinc / Q000032:analysis / Q000378:metabolism*
D027682:Cation Transport Proteins; D009363:Neoplasm Proteins; D011994:Recombinant Proteins; C497524:SLC39A14 protein, human; C418627:SLC39A6 protein, human; D015032:Zinc