Aquaporin-9

Protein-coding gene in the species Homo sapiens
AQP9
Identifiers
AliasesAQP9, AQP-9, HsT17287, SSC1, T17287, aquaporin 9
External IDsOMIM: 602914; MGI: 1891066; HomoloGene: 41405; GeneCards: AQP9; OMA:AQP9 - orthologs
Gene location (Human)
Chromosome 15 (human)
Chr.Chromosome 15 (human)[1]
Chromosome 15 (human)
Genomic location for AQP9
Genomic location for AQP9
Band15q21.3Start58,138,169 bp[1]
End58,185,911 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for AQP9
Genomic location for AQP9
Band9|9 DStart71,017,941 bp[2]
End71,075,964 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • blood

  • monocyte

  • right lobe of liver

  • periodontal fiber

  • granulocyte

  • caput epididymis

  • germinal epithelium

  • corpus epididymis

  • bone marrow

  • right lung
Top expressed in
  • left lobe of liver

  • spermatocyte

  • granulocyte

  • spermatid

  • zygote

  • secondary oocyte

  • seminiferous tubule

  • primary oocyte

  • blood

  • blastocyst
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • porin activity
  • carboxylic acid transmembrane transporter activity
  • polyol transmembrane transporter activity
  • water transmembrane transporter activity
  • purine nucleobase transmembrane transporter activity
  • pyrimidine nucleobase transmembrane transporter activity
  • amine transmembrane transporter activity
  • water channel activity
  • urea channel activity
  • glycerol channel activity
  • channel activity
  • urea transmembrane transporter activity
Cellular component
  • integral component of membrane
  • intracellular membrane-bounded organelle
  • membrane
  • plasma membrane
  • integral component of plasma membrane
  • basolateral plasma membrane
Biological process
  • canalicular bile acid transport
  • excretion
  • water transport
  • amine transport
  • response to organic substance
  • water homeostasis
  • response to osmotic stress
  • polyol transport
  • carboxylic acid transport
  • immune response
  • pyrimidine nucleobase transport
  • response to mercury ion
  • glycerol transport
  • cellular response to cAMP
  • purine nucleobase transport
  • carboxylic acid transmembrane transport
  • purine nucleobase transmembrane transport
  • pyrimidine-containing compound transmembrane transport
  • transmembrane transport
  • urea transmembrane transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

366

64008

Ensembl

ENSG00000103569

ENSMUSG00000032204

UniProt

O43315

Q9JJJ3

RefSeq (mRNA)

NM_020980
NM_001320635
NM_001320636

NM_001271843
NM_022026

RefSeq (protein)

NP_001307564
NP_001307565
NP_066190

NP_001258772
NP_071309

Location (UCSC)Chr 15: 58.14 – 58.19 MbChr 9: 71.02 – 71.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Aquaporin-9 (AQP-9) is a protein that in humans is encoded by the AQP9 gene.[5]

The aquaporins/major intrinsic protein are a family of water-selective membrane channels. Aquaporin-9 has greater sequence similarity with AQP3 and AQP7 and they may be a subfamily. Aquaporin-9 allows passage of a wide variety of noncharged solutes. AQP-9 stimulates urea transport and osmotic water permeability; there are contradicting reports about its role in providing glycerol permeability. Aquaporin-9 may also have some role in specialized leukocyte functions such as immunological response and bactericidal activity.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000103569 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032204 – 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. ^ a b "Entrez Gene: AQP9 aquaporin 9".

Further reading

  • Ishibashi K, Kuwahara M, Gu Y, et al. (1998). "Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol". Biochem. Biophys. Res. Commun. 244 (1): 268–74. doi:10.1006/bbrc.1998.8252. PMID 9514918.
  • Tsukaguchi H, Shayakul C, Berger UV, et al. (1998). "Molecular characterization of a broad selectivity neutral solute channel". J. Biol. Chem. 273 (38): 24737–43. doi:10.1074/jbc.273.38.24737. PMID 9733774.
  • Tsukaguchi H, Weremowicz S, Morton CC, Hediger MA (1999). "Functional and molecular characterization of the human neutral solute channel aquaporin-9". Am. J. Physiol. 277 (5 Pt 2): F685–96. doi:10.1152/ajprenal.1999.277.5.F685. PMID 10564231. S2CID 4516233.
  • Pastor-Soler N, Bagnis C, Sabolic I, et al. (2001). "Aquaporin 9 expression along the male reproductive tract". Biol. Reprod. 65 (2): 384–93. doi:10.1095/biolreprod65.2.384. PMID 11466204.
  • Damiano A, Zotta E, Goldstein J, et al. (2001). "Water channel proteins AQP3 and AQP9 are present in syncytiotrophoblast of human term placenta". Placenta. 22 (8–9): 776–81. doi:10.1053/plac.2001.0717. PMID 11597198.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Okada S, Misaka T, Matsumoto I, et al. (2003). "Aquaporin-9 is expressed in a mucus-secreting goblet cell subset in the small intestine". FEBS Lett. 540 (1–3): 157–62. doi:10.1016/S0014-5793(03)00256-4. PMID 12681500. S2CID 20184558.
  • Bhattacharjee H, Carbrey J, Rosen BP, Mukhopadhyay R (2004). "Drug uptake and pharmacological modulation of drug sensitivity in leukemia by AQP9". Biochem. Biophys. Res. Commun. 322 (3): 836–41. doi:10.1016/j.bbrc.2004.08.002. PMID 15336539.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Wang S, Chen J, Beall M, et al. (2005). "Expression of aquaporin 9 in human chorioamniotic membranes and placenta". Am. J. Obstet. Gynecol. 191 (6): 2160–7. doi:10.1016/j.ajog.2004.05.089. PMID 15592307.
  • Damiano AE, Zotta E, Ibarra C (2006). "Functional and molecular expression of AQP9 channel and UT-A transporter in normal and preeclamptic human placentas". Placenta. 27 (11–12): 1073–81. doi:10.1016/j.placenta.2005.11.014. PMID 16480766.
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
  • Loitto VM, Huang C, Sigal YJ, Jacobson K (2007). "Filopodia are induced by aquaporin-9 expression". Exp. Cell Res. 313 (7): 1295–306. doi:10.1016/j.yexcr.2007.01.023. PMID 17346701.
  • Warth A, Mittelbronn M, Hülper P, et al. (2007). "Expression of the water channel protein aquaporin-9 in malignant brain tumors". Appl. Immunohistochem. Mol. Morphol. 15 (2): 193–8. doi:10.1097/01.pai.0000213110.05108.e9. PMID 17525633. S2CID 24070875.

External links

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

  • v
  • t
  • e
Ligand-gated
Voltage-gated
Constitutively active
Proton-gated
Voltage-gated
Calcium-activated
Inward-rectifier
Tandem pore domain
Voltage-gated
Miscellaneous
Cl: Chloride channel
H+: Proton channel
M+: CNG cation channel
M+: TRP cation channel
H2O (+ solutes): Porin
Cytoplasm: Gap junction
By gating mechanism
Ion channel class
see also disorders