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Aquaporin 1 (Colton blood group)
Available structures
1fqy, 1h6i, 1ih5, 1j4n
Identifiers
Symbols AQP1; AQP-CHIP; CHIP28; CO; MGC26324
External IDs OMIM107776 MGI103201 HomoloGene68051 GeneCards: AQP1 Gene
RNA expression pattern
PBB GE AQP1 209047 at tn.png
PBB GE AQP1 207542 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 358 11826
Ensembl ENSG00000106125 ENSMUSG00000004655
UniProt P29972 Q3TLW5
RefSeq (mRNA) NM_198098 NM_007472
RefSeq (protein) NP_932766 NP_031498
Location (UCSC) Chr 7:
30.92 - 30.93 Mb
Chr 6:
55.27 - 55.28 Mb
PubMed search [1] [2]


AQP1 is a widely expressed water channel, whose physiological function has been most thoroughly characterized in the kidney.

It is found in the basolateral and apical plasma membranes of the proximal tubules, the descending limb of the loop of Henle, and in the descending portion of the vasa recta.

Additionally, it is found in red blood cells, vascular endothelium, the gastrointestinal tract, sweat glands, and lungs.

It is not regulated by vasopressin (ADH).

Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). This gene encodes an aquaporin which functions as a molecular water channel protein. It is a homotetramer with 6 bilayer spanning domains and N-glycosylation sites. The protein physically resembles channel proteins and is abundant in erythrocytes and renal tubes. The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement.[1]

Contents

See also

References

Further reading

  • Knepper MA (1994). "The aquaporin family of molecular water channels.". Proc. Natl. Acad. Sci. U.S.A. 91 (14): 6255–8. doi:10.1073/pnas.91.14.6255. PMID 7517546.  
  • Borgnia M, Nielsen S, Engel A, Agre P (2000). "Cellular and molecular biology of the aquaporin water channels.". Annu. Rev. Biochem. 68: 425–58. doi:10.1146/annurev.biochem.68.1.425. PMID 10872456.  
  • Horster M (2001). "Embryonic epithelial membrane transporters.". Am. J. Physiol. Renal Physiol. 279 (6): F982–96. PMID 11097616.  
  • Yool AJ, Weinstein AM (2002). "New roles for old holes: ion channel function in aquaporin-1.". News Physiol. Sci. 17: 68–72. PMID 11909995.  
  • Mitra AK, Ren G, Reddy VS, et al. (2002). "The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice.". Novartis Found. Symp. 245: 33–46; discussion 46–50; 165–8. doi:10.1002/0470868759.ch4. PMID 12027013.  
  • Ripoche P, Goossens D, Devuyst O, et al. (2006). "Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis.". Transfusion clinique et biologique : journal de la Société française de transfusion sanguine 13 (1-2): 117–22. doi:10.1016/j.tracli.2006.03.004. PMID 16574458.  
  • Preston GM, Carroll TP, Guggino WB, Agre P (1992). "Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.". Science 256 (5055): 385–7. doi:10.1126/science.256.5055.385. PMID 1373524.  
  • Preston GM, Agre P (1992). "Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family.". Proc. Natl. Acad. Sci. U.S.A. 88 (24): 11110–4. doi:10.1073/pnas.88.24.11110. PMID 1722319.  
  • Smith BL, Agre P (1991). "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins.". J. Biol. Chem. 266 (10): 6407–15. PMID 2007592.  
  • Denker BM, Smith BL, Kuhajda FP, Agre P (1988). "Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules.". J. Biol. Chem. 263 (30): 15634–42. PMID 3049610.  
  • Zelinski T, Kaita H, Lewis M, et al. (1988). "The Colton blood group locus. A linkage analysis.". Transfusion 28 (5): 435–8. doi:10.1046/j.1537-2995.1988.28588337331.x. PMID 3166547.  
  • Preston GM, Jung JS, Guggino WB, Agre P (1994). "Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis.". J. Biol. Chem. 269 (3): 1668–73. PMID 7507481.  
  • Skach WR, Shi LB, Calayag MC, et al. (1994). "Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum.". J. Cell Biol. 125 (4): 803–15. doi:10.1083/jcb.125.4.803. PMID 7514605.  
  • Li X, Yu H, Koide SS (1994). "The water channel gene in human uterus.". Biochem. Mol. Biol. Int. 32 (2): 371–7. PMID 7517253.  
  • Walz T, Smith BL, Agre P, Engel A (1994). "The three-dimensional structure of human erythrocyte aquaporin CHIP.". Embo J. 13 (13): 2985–93. PMID 7518771.  
  • Preston GM, Smith BL, Zeidel ML, et al. (1994). "Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels.". Science 265 (5178): 1585–7. doi:10.1126/science.7521540. PMID 7521540.  
  • Smith BL, Preston GM, Spring FA, et al. (1994). "Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens.". J. Clin. Invest. 94 (3): 1043–9. doi:10.1172/JCI117418. PMID 7521882.  
  • van Hoek AN, Wiener MC, Verbavatz JM, et al. (1995). "Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels.". Biochemistry 34 (7): 2212–9. doi:10.1021/bi00007a015. PMID 7532004.  
  • Keen TJ, Inglehearn CF, Patel RJ, et al. (1995). "Localization of the aquaporin 1 (AQP1) gene within a YAC contig containing the polymorphic markers D7S632 and D7S526.". Genomics 25 (2): 599–600. doi:10.1016/0888-7543(95)80070-3. PMID 7540589.  

External links

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

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