Aquaporin-1


NameAquaporin-1
SynonymsAQP-1 Aquaporin-CHIP CHIP28 Urine water channel Water channel protein for red blood cells and kidney proximal tubule
Gene NameAQP1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0001754|Aquaporin-1
MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSI
ATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLT
GNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGH
LLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTD
RVKVWTSGQVEEYDLDADDINSRVEMKPK
Number of residues269
Molecular Weight28525.68
Theoretical pI7.5
GO Classification
Functions
    carbon dioxide transmembrane transporter activity
    transmembrane transporter activity
    potassium ion transmembrane transporter activity
    intracellular cGMP activated cation channel activity
    nitric oxide transmembrane transporter activity
    glycerol transmembrane transporter activity
    water transmembrane transporter activity
    glycerol channel activity
    potassium channel activity
    water channel activity
    ammonium transmembrane transporter activity
Processes
    potassium ion transmembrane transport
    cellular response to copper ion
    renal water homeostasis
    cerebrospinal fluid secretion
    water transport
    transmembrane transport
    cellular homeostasis
    cell volume homeostasis
    cellular response to UV
    cellular response to cAMP
    cellular response to mechanical stimulus
    positive regulation of saliva secretion
    multicellular organismal water homeostasis
    carbon dioxide transport
    cation transmembrane transport
    carbon dioxide transmembrane transport
    cellular response to retinoic acid
    positive regulation of fibroblast proliferation
    potassium ion transport
    pancreatic juice secretion
    cellular hyperosmotic response
    negative regulation of apoptotic process
    cellular response to salt stress
    cellular response to hypoxia
    response to drug
    cellular response to nitric oxide
    cellular response to inorganic substance
    negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
    positive regulation of angiogenesis
    cellular response to mercury ion
    cGMP biosynthetic process
    cellular response to stress
    renal water transport
    nitric oxide transport
    establishment or maintenance of actin cytoskeleton polarity
    cellular water homeostasis
    bicarbonate transport
    small molecule metabolic process
    ammonium transmembrane transport
    maintenance of symbiont-containing vacuole by host
    glycerol transport
    cellular response to dexamethasone stimulus
    ammonium transport
    odontogenesis
    transepithelial water transport
    lateral ventricle development
    cellular response to hydrogen peroxide
Components
    symbiont-containing vacuole
    nuclear membrane
    brush border
    integral component of plasma membrane
    cytoplasm
    nucleus
    sarcolemma
    basolateral plasma membrane
    apical part of cell
    plasma membrane
    apical plasma membrane
    brush border membrane
    extracellular exosome
    basal plasma membrane
General FunctionWater transmembrane transporter activity
Specific FunctionForms 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.
Transmembrane Regions8-36 49-66 95-115 137-155 167-183 208-228
GenBank Protein ID180501
UniProtKB IDP29972
UniProtKB Entry NameAQP1_HUMAN
Cellular LocationCell membrane
Gene sequence
>lcl|BSEQ0021277|Aquaporin-1 (AQP1)
ATGCCTGGGGCTCGCCCCTTGCCTCTGGTCTTGGTACCCCAGAATACCCTGGCCTGGATG
CAGCTGGATGCAAAGGCCCCAGCTCACCCCAGGCCTCTCCAGCTTCTAGGCAGAGTGGGG
CCTGGGTCTAGGCAGCTGGCTGATGGTGTGAACTCGGGCCAGGGCCTGGGCATCGAGATC
ATCGGGACCCTCCAGCTGGTGCTATGCGTGCTGGCTACTACCGACCGGAGGCGCCGTGAC
CTTGGTGGCTCAGCCCCCCTTGCCATCGGCCTCTCTGTAGCCCTTGGACACCTCCTGGCT
ATTGACTACACTGGCTGTGGGATTAACCCTGCTCGGTCCTTTGGCTCCGCGGTGATCACA
CACAACTTCAGCAACCACTGGATTTTCTGGGTGGGGCCATTCATCGGGGGAGCCCTGGCT
GTACTCATCTACGACTTCATCCTGGCCCCACGCAGCAGTGACCTCACAGACCGCGTGAAG
GTGTGGACCAGCGGCCAGGTGGAGGAGTATGACCTGGATGCCGACGACATCAACTCCAGG
GTGGAGATGAAGCCCAAATAG
GenBank Gene IDM77829
GeneCard IDNone
GenAtlas IDAQP1
HGNC IDHGNC:633
Chromosome Location7
Locus7p14
References
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  4. 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.[11171962 ]
  5. 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.[9177353 ]
  6. 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.[11034202 ]
  7. 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.[1722319 ]
  8. 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.[8340403 ]
  9. 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.[8703970 ]
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  13. 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.[2007592 ]
  14. 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.[1373524 ]
  15. 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.[7677994 ]
  16. 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.[7507481 ]
  17. 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.[23219802 ]
  18. 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.[7518771 ]
  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.[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.[7521540 ]

Related FRC


FRCD ID Name Exact Mass Structure



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Mercurol




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Meralluride




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Thiomersal




404.811