Aquaporin-1

Details

Name
Aquaporin-1
Synonyms
  • AQP-1
  • Aquaporin-CHIP
  • CHIP28
  • Urine water channel
  • Water channel protein for red blood cells and kidney proximal tubule
Gene Name
AQP1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0001754|Aquaporin-1
MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSI
ATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLT
GNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGH
LLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTD
RVKVWTSGQVEEYDLDADDINSRVEMKPK
Number of residues
269
Molecular Weight
28525.68
Theoretical pI
7.5
GO Classification
Functions
ammonium transmembrane transporter activity / carbon dioxide transmembrane transporter activity / glycerol channel activity / glycerol transmembrane transporter activity / intracellular cGMP activated cation channel activity / nitric oxide transmembrane transporter activity / potassium channel activity / potassium ion transmembrane transporter activity / transmembrane transporter activity / water channel activity / water transmembrane transporter activity
Processes
ammonium transmembrane transport / ammonium transport / bicarbonate transport / carbon dioxide transmembrane transport / carbon dioxide transport / cation transmembrane transport / cell volume homeostasis / cellular homeostasis / cellular hyperosmotic response / cellular response to cAMP / cellular response to copper ion / cellular response to dexamethasone stimulus / cellular response to hydrogen peroxide / cellular response to hypoxia / cellular response to inorganic substance / cellular response to mechanical stimulus / cellular response to mercury ion / cellular response to nitric oxide / cellular response to retinoic acid / cellular response to salt stress / cellular response to stress / cellular response to UV / cellular water homeostasis / cerebrospinal fluid secretion / cGMP biosynthetic process / establishment or maintenance of actin cytoskeleton polarity / glycerol transport / lateral ventricle development / maintenance of symbiont-containing vacuole by host / multicellular organismal water homeostasis / negative regulation of apoptotic process / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / nitric oxide transport / odontogenesis / pancreatic juice secretion / positive regulation of angiogenesis / positive regulation of fibroblast proliferation / positive regulation of saliva secretion / potassium ion transmembrane transport / potassium ion transport / renal water homeostasis / renal water transport / response to drug / small molecule metabolic process / transepithelial water transport / transmembrane transport / water transport
Components
apical part of cell / apical plasma membrane / basal plasma membrane / basolateral plasma membrane / brush border / brush border membrane / cytoplasm / extracellular exosome / integral component of plasma membrane / nuclear membrane / nucleus / plasma membrane / sarcolemma / symbiont-containing vacuole
General Function
Water transmembrane transporter activity
Specific Function
Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.
Pfam Domain Function
Transmembrane Regions
8-36 49-66 95-115 137-155 167-183 208-228
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0021277|Aquaporin-1 (AQP1)
ATGCCTGGGGCTCGCCCCTTGCCTCTGGTCTTGGTACCCCAGAATACCCTGGCCTGGATG
CAGCTGGATGCAAAGGCCCCAGCTCACCCCAGGCCTCTCCAGCTTCTAGGCAGAGTGGGG
CCTGGGTCTAGGCAGCTGGCTGATGGTGTGAACTCGGGCCAGGGCCTGGGCATCGAGATC
ATCGGGACCCTCCAGCTGGTGCTATGCGTGCTGGCTACTACCGACCGGAGGCGCCGTGAC
CTTGGTGGCTCAGCCCCCCTTGCCATCGGCCTCTCTGTAGCCCTTGGACACCTCCTGGCT
ATTGACTACACTGGCTGTGGGATTAACCCTGCTCGGTCCTTTGGCTCCGCGGTGATCACA
CACAACTTCAGCAACCACTGGATTTTCTGGGTGGGGCCATTCATCGGGGGAGCCCTGGCT
GTACTCATCTACGACTTCATCCTGGCCCCACGCAGCAGTGACCTCACAGACCGCGTGAAG
GTGTGGACCAGCGGCCAGGTGGAGGAGTATGACCTGGATGCCGACGACATCAACTCCAGG
GTGGAGATGAAGCCCAAATAG
Chromosome Location
7
Locus
7p14
External Identifiers
ResourceLink
UniProtKB IDP29972
UniProtKB Entry NameAQP1_HUMAN
GenBank Protein ID180501
GenBank Gene IDM77829
GenAtlas IDAQP1
HGNC IDHGNC:633
General References
  1. Preston GM, Agre P: 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. 1991 Dec 15;88(24):11110-4. [PubMed:1722319]
  2. Moon C, Preston GM, Griffin CA, Jabs EW, Agre P: The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization. J Biol Chem. 1993 Jul 25;268(21):15772-8. [PubMed:8340403]
  3. Ruiz A, Bok D: Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human retinal pigment epithelium. Biochim Biophys Acta. 1996 Jul 25;1282(2):174-8. [PubMed:8703970]
  4. Li X, Yu H, Koide SS: The water channel gene in human uterus. Biochem Mol Biol Int. 1994 Feb;32(2):371-7. [PubMed:7517253]
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  9. Smith BL, Agre P: Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J Biol Chem. 1991 Apr 5;266(10):6407-15. [PubMed:2007592]
  10. Preston GM, Carroll TP, Guggino WB, Agre P: Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 1992 Apr 17;256(5055):385-7. [PubMed:1373524]
  11. Preston GM, Jung JS, Guggino WB, Agre P: The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. J Biol Chem. 1993 Jan 5;268(1):17-20. [PubMed:7677994]
  12. Preston GM, Jung JS, Guggino WB, Agre P: Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis. J Biol Chem. 1994 Jan 21;269(3):1668-73. [PubMed:7507481]
  13. Rungaldier S, Oberwagner W, Salzer U, Csaszar E, Prohaska R: Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochim Biophys Acta. 2013 Mar;1828(3):956-66. doi: 10.1016/j.bbamem.2012.11.030. Epub 2012 Dec 3. [PubMed:23219802]
  14. Walz T, Smith BL, Agre P, Engel A: The three-dimensional structure of human erythrocyte aquaporin CHIP. EMBO J. 1994 Jul 1;13(13):2985-93. [PubMed:7518771]
  15. Walz T, Hirai T, Murata K, Heymann JB, Mitsuoka K, Fujiyoshi Y, Smith BL, Agre P, Engel A: The three-dimensional structure of aquaporin-1. Nature. 1997 Jun 5;387(6633):624-7. [PubMed:9177353]
  16. Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, Heymann JB, Engel A, Fujiyoshi Y: Structural determinants of water permeation through aquaporin-1. Nature. 2000 Oct 5;407(6804):599-605. [PubMed:11034202]
  17. de Groot BL, Engel A, Grubmuller H: A refined structure of human aquaporin-1. FEBS Lett. 2001 Aug 31;504(3):206-11. [PubMed:11532455]
  18. Ren G, Reddy VS, Cheng A, Melnyk P, Mitra AK: Visualization of a water-selective pore by electron crystallography in vitreous ice. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1398-403. Epub 2001 Jan 30. [PubMed:11171962]
  19. Smith BL, Preston GM, Spring FA, Anstee DJ, Agre P: Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens. J Clin Invest. 1994 Sep;94(3):1043-9. [PubMed:7521882]
  20. Preston GM, Smith BL, Zeidel ML, Moulds JJ, Agre P: Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels. Science. 1994 Sep 9;265(5178):1585-7. [PubMed:7521540]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00819Acetazolamideapproved, vet_approvedunknowninhibitorDetails
DB02451B-nonylglucosideexperimentalunknownDetails
DB09338MersalylexperimentalunknownDetails