Biology:SLC39A7

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A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Zinc transporter SLC39A7 (ZIP7) also known as solute carrier family 39 member 7 (SLC39A7) is a protein that in humans is encoded by the SLC39A7 gene.[1][2][3]

Function

Zinc is an essential cofactor for more than 50 classes of enzymes. It is involved in protein, nucleic acid, carbohydrate, and lipid metabolism, as well as in the control of gene transcription, growth, development, and differentiation. Zinc cannot passively diffuse across cell membranes and requires specific transporters, such as SLC39A7, to enter the cytosol from both the extracellular environment and from intracellular storage compartments.[3]

ZIP7 is a membrane transport protein of the endoplasmic reticulum.[4] Phosphorylation of ZIP7 by casein kinase 2 stimulates the release of zinc ions from the endoplasmic reticulum[5] This provides a signal transduction pathway by which activation of cell surface receptors such as the epidermal growth factor receptor can regulate the activity of downstream phosphatases and kinases.

See also

References

  1. "cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes at the centromeric end of the human MHC region". Genomics 35 (3): 600–2. Dec 1996. doi:10.1006/geno.1996.0405. PMID 8812499. 
  2. "Colinearity of novel genes in the class II regions of the MHC in mouse and human". Immunogenetics 34 (1): 5–11. Aug 1991. doi:10.1007/BF00212306. PMID 1855816. 
  3. 3.0 3.1 "Entrez Gene: SLC39A7 solute carrier family 39 (zinc transporter), member 7". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7922. 
  4. "Structure‒function analysis of HKE4, a member of the new LIV-1 subfamily of zinc transporters". Biochemical Journal 377 (Pt 1): 131–139. 2004. doi:10.1042/BJ20031183. PMID 14525538. 
  5. "Protein kinase CK2 opens the gate for zinc signaling". Cell Cycle 11 (10): 1863–1864. 2012. doi:10.4161/cc.20414. PMID 22580452. 

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.