Recombinant Human Zinc transporter ZIP5 (SLC39A5) Protein

Function

Uniporter that transports zinc(2+) into polarized cells of enterocytes, pancreatic acinar and endoderm cells across the basolateral membrane and participates, notably, in zinc excretion from the intestine by the uptake of zinc from the blood into the intestine (By similarity). The transport mechanism is temperature- and concentration-dependent and saturable (By similarity). In addition, is also a high affinity copper transporter in vitro (PubMed:36454509). Also may regulate glucose-stimulated insulin secretion (GSIS) in islets primarily through the zinc-activated SIRT1-PPARGC1A axis (By similarity). Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (PubMed:24891338). Plays a role in eye development (PubMed:24891338)

Subcellular Location

Basolateral cell membrane (Multi-pass membrane protein)

Disease Association

Myopia 24, autosomal dominant (MYP24) : A refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far. [The disease is caused by variants affecting the gene represented in this entry]

Tissue Specificity

Expressed in liver, kidney, pancreas, small intestine, colon, spleen, fetal liver and fetal kidney

Subunit

Homodimer

• Ota T. et al. Complete sequencing and characterization of 21,243 full-length human cDNAs. — Nat. Genet. (2004)
• Scherer S.E. et al. The finished DNA sequence of human chromosome 12. — Nature (2006)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Wang F. et al. The mammalian Zip5 protein is a zinc transporter that localizes to the basolateral surface of polarized cells. — J. Biol. Chem. (2004)
• Guo H. et al. SLC39A5 mutations interfering with the BMP/TGF-beta pathway in non-syndromic high myopia. — J. Med. Genet. (2014)
• Polesel M. et al. Functional characterization of SLC39 family members ZIP5 and ZIP10 in overexpressing HEK293 cells reveals selective copper transport activity. — BioMetals (2023)
• Davydova E. et al. The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes. — Nat. Commun. (2021)
• Wang X. et al. Molecular basis for METTL9-mediated N1-histidine methylation. — Cell Discov. (2023)