Aquaporin 1

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

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
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7p14.3 Start 30,911,694 bp[1] End 30,925,517 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6 B3|6 27.38 cM Start 55,336,432 bp[2] End 55,348,555 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transporter activity • GO:0051739 ammonium transmembrane transporter activity • nitric oxide transmembrane transporter activity • intracellular cGMP activated cation channel activity • potassium channel activity • GO:0022891 transmembrane transporter activity • carbon dioxide transmembrane transporter activity • GO:0001948 protein binding • water transmembrane transporter activity • GO:0015388 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 • cell nucleus • apical plasma membrane • integral component of membrane • cell 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 • ammonium transport • 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 • response to drug • 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 • nociception • 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 • maintenance of symbiont-containing vacuole by host • 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: 55.34 – 55.35 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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 both a molecular water channel protein and as a non-selective cation channel gated by cyclic guanosine monophosphate (cGMP).[5] It is a homotetramer with six bilayer spanning domains and N-glycosylation sites. The AQP1 monomer consists of six transmembrane alpha helices that are connected by five loops (A to E).[6] 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.[7]

See also

• Aquaporin
• Colton antigen system

References

1. GRCh38: Ensembl release 89: ENSG00000240583 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000004655 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Boassa, Daniela; Yool, Andrea J (15 October 2003). "Single amino acids in the carboxyl terminal domain of aquaporin-1 contribute to cGMP-dependent ion channel activation". BMC Physiology. 3: 12. doi:10.1186/1472-6793-3-12. PMC 269983. PMID 14561230.
6. Kong, Yifei; Ma, Jianpeng (4 December 2001). "Dynamic mechanisms of the membrane water channel aquaporin-1 (AQP1)". Proceedings of the National Academy of Sciences of the United States of America. 98 (25): 14345–14349. Bibcode:2001PNAS...9814345K. doi:10.1073/pnas.251507998. PMC 64684. PMID 11717407.
7. "Entrez Gene: AQP1 aquaporin 1 (Colton blood group)".

Further reading

• Knepper MA (1994). "The aquaporin family of molecular water channels". Proc. Natl. Acad. Sci. U.S.A. 91 (14): 6255–8. Bibcode:1994PNAS...91.6255K. 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. doi:10.1152/ajprenal.2000.279.6.F982. PMID 11097616.
• Yool AJ, Weinstein AM (2002). "New roles for old holes: ion channel function in aquaporin-1". News Physiol. Sci. 17 (2): 68–72. doi:10.1152/nips.01372.2001. PMID 11909995.
• Mitra, Alok K.; Ren, Gang; Reddy, Vijay S.; Cheng, Anchi; Froger, Alexandrine (2008). "The Architecture of a Water-Selective Pore in the Lipid Bilayer Visualized by Electron Crystallography in Vitreous Ice". Ion Channels: From Atomic Resolution Physiology to Functional Genomics. Novartis Foundation Symposia. pp. 33–50. doi:10.1002/0470868759.ch4. ISBN 978-0-470-84375-8.
• 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. Bibcode:1992Sci...256..385P. 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. doi:10.1002/j.1460-2075.1994.tb06597.x. 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. Bibcode:1994Sci...265.1585P. 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 US 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.