Aquaporin Z

Details

Name
Aquaporin Z
Synonyms
  • Bacterial nodulin-like intrinsic protein
  • bniP
Gene Name
aqpZ
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0017235|Aquaporin Z
MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGG
HFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNG
YGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPV
TNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD
Number of residues
231
Molecular Weight
23702.58
Theoretical pI
7.63
GO Classification
Functions
identical protein binding / water channel activity
Processes
cellular water homeostasis / response to osmotic stress / water transport
Components
integral component of membrane / integral component of plasma membrane / plasma membrane
General Function
Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Specific Function
Identical protein binding
Pfam Domain Function
Transmembrane Regions
9-29 34-54 82-102 131-151 156-176 202-222
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0017236|Aquaporin Z (aqpZ)
ATGTTCAGAAAATTAGCAGCTGAATGTTTTGGTACTTTCTGGCTTGTTTTTGGTGGCTGT
GGTAGTGCTGTACTGGCCGCAGGCTTCCCGGAATTAGGCATTGGTTTTGCCGGCGTGGCG
TTGGCGTTCGGTCTGACCGTTCTGACGATGGCCTTTGCTGTTGGTCATATTTCTGGTGGT
CATTTTAACCCGGCGGTCACTATTGGTTTATGGGCTGGCGGACGTTTTCCGGCAAAAGAA
GTCGTTGGCTACGTAATTGCCCAGGTTGTCGGCGGTATTGTTGCAGCGGCGCTGCTGTAT
TTAATTGCCAGTGGTAAAACGGGTTTTGACGCGGCAGCCAGCGGTTTTGCTTCTAACGGT
TATGGCGAGCATTCACCAGGCGGTTATTCCATGCTTTCCGCGCTGGTAGTTGAACTGGTA
TTGAGTGCAGGTTTCCTGTTGGTGATCCACGGCGCAACCGACAAATTCGCGCCGGCAGGT
TTTGCGCCGATCGCTATTGGTCTGGCCTTAACCCTGATTCACTTAATTAGTATTCCGGTG
ACTAACACTTCTGTTAACCCGGCGCGCAGCACCGCGGTTGCTATCTTCCAGGGCGGCTGG
GCATTAGAACAACTGTGGTTCTTCTGGGTGGTGCCAATTGTCGGCGGCATTATCGGTGGT
CTGATTTACCGGACCCTGCTGGAAAAGCGTGATTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP60844
UniProtKB Entry NameAQPZ_ECOLI
GenBank Protein ID1051283
GenBank Gene IDU38664
General References
  1. Calamita G, Bishai WR, Preston GM, Guggino WB, Agre P: Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli. J Biol Chem. 1995 Dec 8;270(49):29063-6. [Article]
  2. Fushimi K, Bai L, Marumo F, Sasaki S: Isolation of a gene encoding nodulin-like intrinsic protein of Escherichia coli. Biochem Mol Biol Int. 1997 Apr;41(5):995-1003. [Article]
  3. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Delamarche C, Thomas D, Rolland JP, Froger A, Gouranton J, Svelto M, Agre P, Calamita G: Visualization of AqpZ-mediated water permeability in Escherichia coli by cryoelectron microscopy. J Bacteriol. 1999 Jul;181(14):4193-7. [Article]
  7. Borgnia MJ, Kozono D, Calamita G, Maloney PC, Agre P: Functional reconstitution and characterization of AqpZ, the E. coli water channel protein. J Mol Biol. 1999 Sep 3;291(5):1169-79. [Article]
  8. Pohl P, Saparov SM, Borgnia MJ, Agre P: Highly selective water channel activity measured by voltage clamp: analysis of planar lipid bilayers reconstituted with purified AqpZ. Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9624-9. Epub 2001 Aug 7. [Article]
  9. Ringler P, Borgnia MJ, Stahlberg H, Maloney PC, Agre P, Engel A: Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography. J Mol Biol. 1999 Sep 3;291(5):1181-90. [Article]
  10. Scheuring S, Ringler P, Borgnia M, Stahlberg H, Muller DJ, Agre P, Engel A: High resolution AFM topographs of the Escherichia coli water channel aquaporin Z. EMBO J. 1999 Sep 15;18(18):4981-7. [Article]
  11. Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G: Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005 May 27;308(5726):1321-3. [Article]
  12. Savage DF, Egea PF, Robles-Colmenares Y, O'Connell JD 3rd, Stroud RM: Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z. PLoS Biol. 2003 Dec;1(3):E72. Epub 2003 Dec 22. [Article]
  13. Calamita G: The Escherichia coli aquaporin-Z water channel. Mol Microbiol. 2000 Jul;37(2):254-62. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB07349(1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATEexperimentalunknownDetails
DB03152B-2-OctylglucosideexperimentalunknownDetails
DB07923octyl alpha-L-altropyranosideexperimentalunknownDetails
DB07924octyl beta-D-galactopyranosideexperimentalunknownDetails