AQP7

From Wikipedia, the free encyclopedia

Aquaporin 7

Identifiers

AQP7; AQP7L; AQP9; AQPap; MGC149555; MGC149556

External IDs

OMIM: 602974 MGI: 1314647 HomoloGene: 48000

Gene ontology
Molecular Function:	• transporter activity • water channel activity • glycerol channel activity • porin activity
Cellular Component:	• integral to plasma membrane • membrane • integral to membrane • outer membrane
Biological Process:	• generation of precursor metabolites and energy • transport • water transport • excretion • glycerol transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001170 (mRNA)
NP_001161 (protein)

XM_982564 (mRNA)
XP_987658 (protein)

Location

Chr 9: 33.37 - 33.39 Mb

Chr 4: 41.22 - 41.24 Mb

Pubmed search

[1]

[2]

Aquaporin 7, also known as AQP7, is a human gene.^[1]

Aquaporins/major intrinsic protein (MIP) are a family of water-selective membrane channels. Aquaporin 7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin 7 facilitates water, glycerol and urea transport. It may play an important role in sperm function.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Aquaporin

[edit] References

^ ^a ^b Entrez Gene: AQP7 aquaporin 7.

[edit] Further reading

Dibas AI, Mia AJ, Yorio T (1998). "Aquaporins (water channels): role in vasopressin-activated water transport.". Proc. Soc. Exp. Biol. Med. 219 (3): 183–99. PMID 9824541.
Ishibashi K, Kuwahara M, Gu Y, et al. (1997). "Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea.". J. Biol. Chem. 272 (33): 20782–6. PMID 9252401.
Kuriyama H, Kawamoto S, Ishida N, et al. (1998). "Molecular cloning and expression of a novel human aquaporin from adipose tissue with glycerol permeability.". Biochem. Biophys. Res. Commun. 241 (1): 53–8. doi:10.1006/bbrc.1997.7769. PMID 9405233.
Ishibashi K, Yamauchi K, Kageyama Y, et al. (1998). "Molecular characterization of human Aquaporin-7 gene and its chromosomal mapping.". Biochim. Biophys. Acta 1399 (1): 62–6. PMID 9714739.
Suzuki-Toyota F, Ishibashi K, Yuasa S (1999). "Immunohistochemical localization of a water channel, aquaporin 7 (AQP7), in the rat testis.". Cell Tissue Res. 295 (2): 279–85. PMID 9931374.
Kondo H, Shimomura I, Kishida K, et al. (2002). "Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation.". Eur. J. Biochem. 269 (7): 1814–26. PMID 11952783.
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.
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.
Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9.". Nature 429 (6990): 369–74. doi:10.1038/nature02465. PMID 15164053.
Fortna A, Kim Y, MacLaren E, et al. (2006). "Lineage-specific gene duplication and loss in human and great ape evolution.". PLoS Biol. 2 (7): E207. doi:10.1371/journal.pbio.0020207. PMID 15252450.
Marrades MP, Milagro FI, Martínez JA, Moreno-Aliaga MJ (2006). "Differential expression of aquaporin 7 in adipose tissue of lean and obese high fat consumers.". Biochem. Biophys. Res. Commun. 339 (3): 785–9. doi:10.1016/j.bbrc.2005.11.080. PMID 16325777.
Prudente S, Flex E, Morini E, et al. (2007). "A functional variant of the adipocyte glycerol channel aquaporin 7 gene is associated with obesity and related metabolic abnormalities.". Diabetes 56 (5): 1468–74. doi:10.2337/db06-1389. PMID 17351148.
Ceperuelo-Mallafré V, Miranda M, Chacón MR, et al. (2007). "Adipose tissue expression of the glycerol channel aquaporin-7 gene is altered in severe obesity but not in type 2 diabetes.". J. Clin. Endocrinol. Metab. 92 (9): 3640–5. doi:10.1210/jc.2007-0531. PMID 17566090.

[edit] External links

MeSH AQP7+protein,+human

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

v • d • e Membrane transport protein: ion channels

Ca²⁺: Calcium channel	Voltage-dependent calcium channel (L-type/Ca_vα(1.1, 1.2, 1.3, 1.4), N-type, P-type/Ca_vα(2.1), Q-type, R-type, T-type, α₂δ-subunits (1, 2), β-subunits (β1, β2, β3, β4), γ-subunits (γ1, γ2, γ3, γ4) Inositol triphosphate receptor • Ryanodine receptor • Cation channels of sperm • Two-pore channel

Na⁺: Sodium channel	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.9, 7A) • Na_vβ (1, 2, 3, 4) • Epithelial sodium channel

K⁺: Potassium channel	Voltage-gated (K_vα (1.1, 1.2, 1.3, 1.4, 1.5, 2.1, 3.1, 3.4, 4.1, 4.2, 4.3, 6.1, 7.1, 7.2, 7.3, 7.4, 7.5, 9.3, 10.1, 11.1/hERG) • K_vβ (1, 2), Shaker gene, KCNE1) Calcium-activated (BK channel: α1, β1, β2, β3, β4; SK channel: SK1, SK2, SK3, SK4) Inward-rectifier K_ir (1.1, 2.1, 2.2, 2.3, 2.4, GIRK, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 5.1, 6.1, 6.2, 7.1) Tandem pore domain K2P (1, 2, 3, 4, 6, 9, 15, 17)

Cl^-: Chloride channel	Cystic fibrosis transmembrane conductance regulator

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) • Voltage-dependent anion channel (1)

Cations: TRP	TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (Mucolipin-1) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)

Other/general	Voltage-gated ion channel • Ligand-gated ion channel • Cyclic nucleotide-gated ion channel (α1, α2, α3, β1, β3, H1, H2, H3, H4) • Stretch-activated ion channel