Aquaporin-1

AQP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4CSK, 1FQY, 1H6I, 1IH5
Identifiers
Aliases	AQP1, AQP-CHIP, CHIP28, CO, aquaporin 1 (Colton blood group)
External IDs	OMIM: 107776; MGI: 103201; HomoloGene: 68051; GeneCards: AQP1; OMA:AQP1 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7p14.3 Start 30,911,853 bp End 30,925,517 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6 B3|6 27.38 cM Start 55,313,417 bp End 55,325,540 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Descending thoracic aorta ascending aorta right lung tendon of biceps brachii upper lobe of left lung right coronary artery pericardium human kidney apex of heart lower lobe of lung Top expressed in right lung right lung lobe tibiofemoral joint ankle fourth ventricle choroid plexus of fourth ventricle left lung rib human kidney body of femur More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transporter activity ammonium transmembrane transporter activity nitric oxide transmembrane transporter activity intracellular cGMP-activated cation channel activity potassium channel activity transmembrane transporter activity carbon dioxide transmembrane transporter activity protein binding water transmembrane transporter activity potassium ion transmembrane transporter activity glycerol transmembrane transporter activity water channel activity ephrin receptor binding identical protein binding channel activity Cellular component cytoplasm nuclear membrane symbiont-containing vacuole membrane membrane nucleus apical plasma membrane integral component of membrane plasma membrane apical part of cell basal plasma membrane integral component of plasma membrane brush border membrane basolateral plasma membrane sarcolemma brush border symbiont-containing vacuole axon neuron projection axon terminus extracellular exosome Biological process cellular response to retinoic acid cellular response to mechanical stimulus cellular response to copper ion cellular response to nitric oxide cellular response to hypoxia cellular response to cAMP carbon dioxide transmembrane transport positive regulation of fibroblast proliferation cellular homeostasis pancreatic juice secretion cGMP biosynthetic process cellular response to stress cellular response to salt stress cellular response to inorganic substance cell volume homeostasis cellular response to UV establishment or maintenance of actin cytoskeleton polarity negative regulation of apoptotic process cellular response to dexamethasone stimulus positive regulation of angiogenesis odontogenesis renal water transport negative regulation of cysteine-type endopeptidase activity involved in apoptotic process cellular response to mercury ion nitric oxide transport cellular hyperosmotic response bicarbonate transport positive regulation of saliva secretion renal water homeostasis multicellular organismal water homeostasis transepithelial water transport carbon dioxide transport cellular response to hydrogen peroxide cerebrospinal fluid secretion potassium ion transmembrane transport ammonium transmembrane transport cation transmembrane transport glomerular filtration potassium ion transport water transport hyperosmotic response response to hormone positive regulation of lamellipodium assembly positive regulation of epithelial cell migration glycerol transport sensory perception of pain lateral ventricle development water homeostasis positive regulation of cell migration secretion by cell secretory granule organization wound healing hyperosmotic salinity response response to estrogen lipid digestion camera-type eye morphogenesis corticotropin secretion renal water absorption metanephric descending thin limb development metanephric proximal straight tubule development metanephric proximal convoluted tubule segment 2 development metanephric glomerulus vasculature development transport cGMP-mediated signaling ion transmembrane transport transmembrane transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 358 11826 Ensembl ENSG00000240583 ENSMUSG00000004655 UniProt P29972 Q6JSD8 Q6JSD7 Q02013 RefSeq (mRNA) NM_198098 NM_000385 NM_001185060 NM_001185061 NM_001185062 NM_001329872 NM_007472 RefSeq (protein) NP_001316801 NP_932766 NP_031498 Location (UCSC) Chr 7: 30.91 – 30.93 Mb Chr 6: 55.31 – 55.33 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Aquaporin 1 is a protein that in humans is encoded by the AQP1 gene.

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).

Function

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.

See also

• Aquaporin
• Colton antigen system

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. PMC 44179. 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, Cheng A, Froger A (2002). "The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice". Novartis Found. Symp. Novartis Foundation Symposia. 245: 33–46, discussion 46–50, 165–8. doi:10.1002/0470868759.ch4. ISBN 978-0-470-86875-1. PMID 12027013.
• Ripoche P, Goossens D, Devuyst O, Gane P, Colin Y, Verkman AS, Cartron JP (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. PMC 53083. 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, Coghlan G, Philipps S, Belcher E, McAlpine PJ, Coopland G, Wong P (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, Frigeri A, Lingappa VR, Verkman AS (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. PMC 2120064. 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. PMC 395186. PMID 7518771.
• Preston GM, Smith BL, Zeidel ML, Moulds JJ, Agre P (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, Anstee DJ, Agre P (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. PMC 295159. PMID 7521882.
• van Hoek AN, Wiener MC, Verbavatz JM, Brown D, Lipniunas PH, Townsend RR, Verkman AS (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, Green ED, Peluso DC, Bhattacharya SS (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

• Aquaporin+1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Gallery of Aquaporin Simulations
• Human AQP1 genome location and AQP1 gene details page in the UCSC Genome Browser.

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