SLC39A7

From Wikipedia, the free encyclopedia

Solute carrier family 39 (zinc transporter), member 7

Identifiers

SLC39A7; RING5; D6S115E; D6S2244E; H2-KE4; HKE4; KE4; ZIP7

External IDs

OMIM: 601416 MGI: 95909 HomoloGene: 5072

Gene ontology
Molecular Function:	• zinc ion binding • metal ion transmembrane transporter activity
Cellular Component:	• membrane fraction • membrane • integral to membrane
Biological Process:	• ion transport • zinc ion transport • metal ion transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001077516 (mRNA)
NP_001070984 (protein)

NM_001077709 (mRNA)
NP_001071177 (protein)

Location

Chr 6: 33.28 - 33.28 Mb

Chr 17: 33.64 - 33.64 Mb

Pubmed search

[1]

[2]

Solute carrier family 39 (zinc transporter), member 7, also known as SLC39A7, is a human gene.^[1]

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.[supplied by OMIM]^[1]

[edit] See also

Solute carrier family

[edit] References

^ ^a ^b Entrez Gene: SLC39A7 solute carrier family 39 (zinc transporter), member 7.

[edit] Further reading

Hanson IM, Trowsdale J (1991). "Colinearity of novel genes in the class II regions of the MHC in mouse and human.". Immunogenetics 34 (1): 5–11. PMID 1855816.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Ando A, Kikuti YY, Shigenari A, et al. (1996). "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. doi:10.1006/geno.1996.0405. PMID 8812499.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Taylor KM, Morgan HE, Johnson A, et al. (2003). "Structure-function analysis of LIV-1, the breast cancer-associated protein that belongs to a new subfamily of zinc transporters.". Biochem. J. 375 (Pt 1): 51–9. doi:10.1042/BJ20030478. PMID 12839489.
Taylor KM, Morgan HE, Johnson A, Nicholson RI (2004). "Structure-function analysis of HKE4, a member of the new LIV-1 subfamily of zinc transporters.". Biochem. J. 377 (Pt 1): 131–9. doi:10.1042/BJ20031183. PMID 14525538.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Huang L, Kirschke CP, Zhang Y, Yu YY (2005). "The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus.". J. Biol. Chem. 280 (15): 15456–63. doi:10.1074/jbc.M412188200. PMID 15705588.
Kim JE, Tannenbaum SR, White FM (2005). "Global phosphoproteome of HT-29 human colon adenocarcinoma cells.". J. Proteome Res. 4 (4): 1339–46. doi:10.1021/pr050048h. PMID 16083285.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.

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v • d • e Membrane proteins, carrier proteins: membrane transport proteins

ABC-transporter	A1, A2, A3, A4, A7, A8, A12, B1 B2-3, B2, B3, B4, B5, B6, B7, B9, B11 C1, C2, C3, C4, C5, C6, C8, C8-9, C10, C13, C11 D1, D2, D3, D4, E1, F1, F2 G1, G2, G4, Sterolin (G5, G8)

Solute carrier	1A1-7, 1A1, 1A2, 1A3, 1A4, 1A5, 2A1, 2A2, 2A3, 2A4, 2A5, 2A6, 2A8, 2A9, 2A10, 2A12, 3A1, 3A2, 4A1, 4A2, 4A3, 4A4, 4A5, 4A7, 4A8, 4A11, 5A1-2, 5A1, 5A3, 5A5, 5A8, 6A1, 6A2, 6A3, 6A4, 6A5, 6A8, 6A9, 6A19, 7A1, 7A2, 7A3, 7A4, 7A5, 7A7, 7A8, 7A9, 7A11, 8A1-3, 9A1, 9A2, 9A3, 9A3R1, 9A3R2, 9A5, 9A6, 9A8, 10A1, 10A2, 10A3, 10A7, 11A1, 11A2, 11A3, 12A1-2, 12A3, 12A4, 12A5, 12A6, 12A7, 14A1, 13A3, 14A2, 15A1, 15A2, 16A1, 16A2, 16A3, 16A4, 17A1, 17A5, 17A6-8, 17A7, 18A1, 18A2, 18A3, 19A1, 19A2, 19A3, 20A1, 20A2, 22A1, 22A2, 22A3, 22A4, 22A5, 22A6, 22A7, 22A9, 22A11, 22A12, 22A18, 23A1, 23A2, 24A1-2, 24A5, 25A1, 25A3, 25A4, 25A4-6, 25A8, 25A10, 25A11, 25A12, 25A13, 25A14, 25A15, 25A17, 25A19, 25A20, 25A27, 25A31, 25A37, 25A39, 26A2, 26A3, 26A4, 26A5, 26A6, 26A7, 26A8, 27A1, 27A2, 27A3, 27A4, 28A1, 28A2, 29A1, 29A2, 29A4, 30A4, 30A7, 30A8, 31A1, 31A2, 32A1, 34A1, 34A2, 34A3, 35A1, 35A2, 35B2, 35B4, 35C1, 36A1, 37A4, 38A2, 38A3, 39A1, 39A2, 39A3, 39A4, 39A6, 39A7, 40A1, 43A1 44A1, 44A2, 44A4, 45A2, O1A2, O1B1, O1B3, O2B1, O431, O4A1

Monosaccharide	GLUT1, GLUT2, GLUT3, GLUT4, GLUT5, GLUT6, GLUT8, GLUT9

Other	Amino acid (CD98) - Fatty acid (CD36) - Ion channels - Ion pumps - Mitochondrial membrane transport protein - Neurotransmitter transport proteins - Nuclear (Importin, Karyopherin)