SLC39A1

From Wikipedia, the free encyclopedia

Solute carrier family 39 (zinc transporter), member 1

Identifiers

SLC39A1; ZIP1; ZIRTL

External IDs

OMIM: 604740 MGI: 1353474 HomoloGene: 40906

Gene ontology
Molecular Function:	• zinc ion binding • di-, tri-valent inorganic cation transmembrane transporter activity • metal ion transmembrane transporter activity
Cellular Component:	• membrane fraction • endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• ion transport • zinc ion transport • di-, tri-valent inorganic cation transport • metal ion transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_014437 (mRNA)
NP_055252 (protein)

XM_989797 (mRNA)
XP_994891 (protein)

Location

Chr 1: 152.2 - 152.21 Mb

n/a

Pubmed search

[1]

[2]

Solute carrier family 39 (zinc transporter), member 1, also known as SLC39A1, is a human gene.^[1]

[edit] See also

Solute carrier family

[edit] References

^ Entrez Gene: SLC39A1 solute carrier family 39 (zinc transporter), member 1.

[edit] Further reading

Lioumi M, Ferguson CA, Sharpe PT, et al. (2000). "Isolation and characterization of human and mouse ZIRTL, a member of the IRT1 family of transporters, mapping within the epidermal differentiation complex.". Genomics 62 (2): 272–80. doi:10.1006/geno.1999.5993. PMID 10610721.
Gaither LA, Eide DJ (2000). "Functional expression of the human hZIP2 zinc transporter.". J. Biol. Chem. 275 (8): 5560–4. PMID 10681536.
Lai CH, Chou CY, Ch'ang LY, et al. (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics.". Genome Res. 10 (5): 703–13. PMID 10810093.
Gaither LA, Eide DJ (2001). "The human ZIP1 transporter mediates zinc uptake in human K562 erythroleukemia cells.". J. Biol. Chem. 276 (25): 22258–64. doi:10.1074/jbc.M101772200. PMID 11301334.
Milon B, Dhermy D, Pountney D, et al. (2001). "Differential subcellular localization of hZip1 in adherent and non-adherent cells.". FEBS Lett. 507 (3): 241–6. PMID 11696349.
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.
Franklin RB, Ma J, Zou J, et al. (2003). "Human ZIP1 is a major zinc uptake transporter for the accumulation of zinc in prostate cells.". J. Inorg. Biochem. 96 (2-3): 435–42. PMID 12888280.
Dufner-Beattie J, Langmade SJ, Wang F, et al. (2004). "Structure, function, and regulation of a subfamily of mouse zinc transporter genes.". J. Biol. Chem. 278 (50): 50142–50. doi:10.1074/jbc.M304163200. PMID 14525987.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Franklin RB, Feng P, Milon B, et al. (2006). "hZIP1 zinc uptake transporter down regulation and zinc depletion in prostate cancer.". Mol. Cancer 4: 32. doi:10.1186/1476-4598-4-32. PMID 16153295.
Tang Z, Sahu SN, Khadeer MA, et al. (2006). "Overexpression of the ZIP1 zinc transporter induces an osteogenic phenotype in mesenchymal stem cells.". Bone 38 (2): 181–98. doi:10.1016/j.bone.2005.08.010. PMID 16203195.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Huang L, Kirschke CP (2007). "A di-leucine sorting signal in ZIP1 (SLC39A1) mediates endocytosis of the protein.". FEBS J. 274 (15): 3986–97. doi:10.1111/j.1742-4658.2007.05933.x. PMID 17635580.

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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)