Passive transport by Aquaporins (Homo sapiens)

From WikiPathways

Jump to: navigation, search
17, 24, 31, 32, 36...526, 46, 53, 57, 68...521-16, 18-23, 25...5, 6, 11, 19, 23...1-16, 18-23, 25...5, 6, 46, 53, 57...5, 6, 11, 19, 23...cytosoltransport vesicleCl- AQP7 Fl- UreaGlycerolAQP0,1,2,3,4,5,7,8,9,10,11,12AglycerolI- NO3- H2OAQP9 AQP9,10Anions transportedby Aquaporin-6MIP Cl- Anions transportedby Aquaporin-6I- AQP1 AQP6 AQP11 AQP3 AQP4 AQP10 AQP7 AQP10 AQP9 NO3- p-S256-AQP2 Fl- AQP8 Br- AQP12A H2OAQP3 AQP10 AQP3,7,9,10AQP9 UreaAQP5 AQP6 tetramerBr-


Description

Aquaporins (AQP's) are six-pass transmembrane proteins that form channels in membranes. Each monomer contains a central channel formed in part by two asparagine-proline-alanine motifs (NPA boxes) that confer selectivity for water and/or solutes. The monomers assemble into tetramers. During passive transport by Aquaporins most aquaporins (i.e. AQP0/MIP, AQP1, AQP2, AQP3, AQP4, AQP5, AQP7, AQP8, AQP9, AQP10) transport water into and out of cells according to the osmotic gradient across the membrane. Four aquaporins (the aquaglyceroporins AQP3, AQP7, AQP9, AQP10) conduct glycerol, three aquaporins (AQP7, AQP9, AQP10) conduct urea, and one aquaporin (AQP6) conducts anions, especially nitrate. AQP8 also conducts ammonia in addition to water.
AQP11 and AQP12, classified as group III aquaporins, were identified as a result of the genome sequencing project and are characterized by having variations in the first NPA box when compared to more traditional aquaporins. Additionally, a conserved cysteine residue is present about 9 amino acids downstream from the second NPA box and this cysteine is considered indicative of group III aquaporins. Purified AQP11 incorporated into liposomes showed water transport. Knockout mice lacking AQP11 had fatal cyst formation in the proximal tubule of the kidney. Exogenously expressed AQP12 showed intracellular localization. AQP12 is expressed exclusively in pancreatic acinar cells.
Aquaporins are important in fluid and solute transport in various tissues. During Transport of glycerol from adipocytes to the liver by Aquaporins, glycerol generated by triglyceride hydrolysis is exported from adipocytes by AQP7 and is imported into liver cells via AQP9. AQP1 plays a role in forming cerebrospinal fluid and AQP1, AQP4, and AQP9 appear to be important in maintaining fluid balance in the brain. AQP0, AQP1, AQP3, AQP4, AQP8, AQP9, and AQP11 play roles in the physiology of the hepatobiliary tract.
In the kidney, water and solutes are passed out of the bloodstream and into the proximal tubule via the slit-like structure formed by nephrin in the glomerulus. Water is reabsorbed from the filtrate during its transit through the proximal tubule, the descending loop of Henle, the distal convoluted tubule, and the collecting duct. Aquaporin-1 (AQP1) in the proximal tubule and the descending thin limb of Henle is responsible for about 90% of reabsorption (as estimated from mouse knockouts of AQP1). AQP1 is located on both the apical and basolateral surface of epithelial cells and thus transports water through the epithelium and back into the bloodstream. In the collecting duct epithelial cells have AQP2 on their apical surfaces and AQP3 and AQP4 on their basolateral surfaces to transport water across the epithelium. Vasopressin regulates renal water homeostasis via Aquaporins by regulating the permeability of the epithelium through activation of a signaling cascade leading to the phosphorylation of AQP2 and its translocation from intracellular vesicles to the apical membrane of collecting duct cells.
Here, three views of aquaporin-mediated transport have been annotated: a generic view of transport mediated by the various families of aquaporins independent of tissue type (Passive transport by Aquaporins), a view of the role of specific aquaporins in maintenance of renal water balance (Vasopressin regulates renal water homeostasis via Aquaporins), and a view of the role of specific aquaporins in glycerol transport from adipocytes to the liver (Transport of glycerol from adipocytes to the liver by Aquaporins). View original pathway at:Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 432047
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: May, Bruce

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Kamsteeg EJ, Heijnen I, van Os CH, Deen PM.; ''The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers.''; PubMed Europe PMC
  2. Huber VJ, Tsujita M, Yamazaki M, Sakimura K, Nakada T.; ''Identification of arylsulfonamides as Aquaporin 4 inhibitors.''; PubMed Europe PMC
  3. Bedford JJ, Leader JP, Walker RJ.; ''Aquaporin expression in normal human kidney and in renal disease.''; PubMed Europe PMC
  4. Fischer H, Stenling R, Rubio C, Lindblom A.; ''Differential expression of aquaporin 8 in human colonic epithelial cells and colorectal tumors.''; PubMed Europe PMC
  5. Cohly HH, Isokpehi R, Rajnarayanan RV.; ''Compartmentalization of aquaporins in the human intestine.''; PubMed Europe PMC
  6. Ishibashi K, Morinaga T, Kuwahara M, Sasaki S, Imai M.; ''Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin.''; PubMed Europe PMC
  7. Zeidel ML, Ambudkar SV, Smith BL, Agre P.; ''Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein.''; PubMed Europe PMC
  8. Liu K, Nagase H, Huang CG, Calamita G, Agre P.; ''Purification and functional characterization of aquaporin-8.''; PubMed Europe PMC
  9. Koyama N, Ishibashi K, Kuwahara M, Inase N, Ichioka M, Sasaki S, Marumo F.; ''Cloning and functional expression of human aquaporin8 cDNA and analysis of its gene.''; PubMed Europe PMC
  10. Varadaraj K, Kumari SS, Patil R, Wax MB, Mathias RT.; ''Functional characterization of a human aquaporin 0 mutation that leads to a congenital dominant lens cataract.''; PubMed Europe PMC
  11. Kida H, Miyoshi T, Manabe K, Takahashi N, Konno T, Ueda S, Chiba T, Shimizu T, Okada Y, Morishima S.; ''Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line.''; PubMed Europe PMC
  12. Sasaki S, Fushimi K, Saito H, Saito F, Uchida S, Ishibashi K, Kuwahara M, Ikeuchi T, Inui K, Nakajima K.; ''Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct.''; PubMed Europe PMC
  13. Tsunoda SP, Wiesner B, Lorenz D, Rosenthal W, Pohl P.; ''Aquaporin-1, nothing but a water channel.''; PubMed Europe PMC
  14. Oliva R, Calamita G, Thornton JM, Pellegrini-Calace M.; ''Electrostatics of aquaporin and aquaglyceroporin channels correlates with their transport selectivity.''; PubMed Europe PMC
  15. Buzhynskyy N, Girmens JF, Faigle W, Scheuring S.; ''Human cataract lens membrane at subnanometer resolution.''; PubMed Europe PMC
  16. Mobasheri A, Marples D.; ''Expression of the AQP-1 water channel in normal human tissues: a semiquantitative study using tissue microarray technology.''; PubMed Europe PMC
  17. Maeda N, Hibuse T, Funahashi T.; ''Role of aquaporin-7 and aquaporin-9 in glycerol metabolism; involvement in obesity.''; PubMed Europe PMC
  18. Larocca MC, Soria LR, Espelt MV, Lehmann GL, Marinelli RA.; ''Knockdown of hepatocyte aquaporin-8 by RNA interference induces defective bile canalicular water transport.''; PubMed Europe PMC
  19. Fain JN, Buehrer B, Bahouth SW, Tichansky DS, Madan AK.; ''Comparison of messenger RNA distribution for 60 proteins in fat cells vs the nonfat cells of human omental adipose tissue.''; PubMed Europe PMC
  20. Yakata K, Tani K, Fujiyoshi Y.; ''Water permeability and characterization of aquaporin-11.''; PubMed Europe PMC
  21. Hub JS, de Groot BL.; ''Mechanism of selectivity in aquaporins and aquaglyceroporins.''; PubMed Europe PMC
  22. Kumari SS, Varadaraj K.; ''Intact AQP0 performs cell-to-cell adhesion.''; PubMed Europe PMC
  23. Silberstein C, Kierbel A, Amodeo G, Zotta E, Bigi F, Berkowski D, Ibarra C.; ''Functional characterization and localization of AQP3 in the human colon.''; PubMed Europe PMC
  24. Calamita G.; ''Aquaporins: highways for cells to recycle water with the outside world.''; PubMed Europe PMC
  25. Horsefield R, Nordén K, Fellert M, Backmark A, Törnroth-Horsefield S, Terwisscha van Scheltinga AC, Kvassman J, Kjellbom P, Johanson U, Neutze R.; ''High-resolution x-ray structure of human aquaporin 5.''; PubMed Europe PMC
  26. Burghardt B, Elkaer ML, Kwon TH, Rácz GZ, Varga G, Steward MC, Nielsen S.; ''Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas.''; PubMed Europe PMC
  27. Bachinsky DR, Sabolic I, Emmanouel DS, Jefferson DM, Carone FA, Brown D, Perrone RD.; ''Water channel expression in human ADPKD kidneys.''; PubMed Europe PMC
  28. Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P.; ''The human Aquaporin-5 gene. Molecular characterization and chromosomal localization.''; PubMed Europe PMC
  29. Nielsen S, Smith BL, Christensen EI, Knepper MA, Agre P.; ''CHIP28 water channels are localized in constitutively water-permeable segments of the nephron.''; PubMed Europe PMC
  30. Calvanese L, Pellegrini-Calace M, Oliva R.; ''In silico study of human aquaporin AQP11 and AQP12 channels.''; PubMed Europe PMC
  31. King LS, Kozono D, Agre P.; ''From structure to disease: the evolving tale of aquaporin biology.''; PubMed Europe PMC
  32. Nedvetsky PI, Tamma G, Beulshausen S, Valenti G, Rosenthal W, Klussmann E.; ''Regulation of aquaporin-2 trafficking.''; PubMed Europe PMC
  33. Mobasheri A, Wray S, Marples D.; ''Distribution of AQP2 and AQP3 water channels in human tissue microarrays.''; PubMed Europe PMC
  34. Wu B, Steinbronn C, Alsterfjord M, Zeuthen T, Beitz E.; ''Concerted action of two cation filters in the aquaporin water channel.''; PubMed Europe PMC
  35. Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, Heymann JB, Engel A, Fujiyoshi Y.; ''Structural determinants of water permeation through aquaporin-1.''; PubMed Europe PMC
  36. Nielsen S, Kwon TH, Frøkiaer J, Agre P.; ''Regulation and dysregulation of aquaporins in water balance disorders.''; PubMed Europe PMC
  37. Beitz E, Wu B, Holm LM, Schultz JE, Zeuthen T.; ''Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons.''; PubMed Europe PMC
  38. Nejsum LN.; ''The renal plumbing system: aquaporin water channels.''; PubMed Europe PMC
  39. Francis P, Chung JJ, Yasui M, Berry V, Moore A, Wyatt MK, Wistow G, Bhattacharya SS, Agre P.; ''Functional impairment of lens aquaporin in two families with dominantly inherited cataracts.''; PubMed Europe PMC
  40. Rojek A, Praetorius J, Frøkiaer J, Nielsen S, Fenton RA.; ''A current view of the mammalian aquaglyceroporins.''; PubMed Europe PMC
  41. Meinild AK, Klaerke DA, Zeuthen T.; ''Bidirectional water fluxes and specificity for small hydrophilic molecules in aquaporins 0-5.''; PubMed Europe PMC
  42. Kuwahara M, Gu Y, Ishibashi K, Marumo F, Sasaki S.; ''Mercury-sensitive residues and pore site in AQP3 water channel.''; PubMed Europe PMC
  43. Portincasa P, Palasciano G, Svelto M, Calamita G.; ''Aquaporins in the hepatobiliary tract. Which, where and what they do in health and disease.''; PubMed Europe PMC
  44. Mobasheri A, Marples D, Young IS, Floyd RV, Moskaluk CA, Frigeri A.; ''Distribution of the AQP4 water channel in normal human tissues: protein and tissue microarrays reveal expression in several new anatomical locations, including the prostate gland and seminal vesicles.''; PubMed Europe PMC
  45. Wang Y, Tajkhorshid E.; ''Molecular mechanisms of conduction and selectivity in aquaporin water channels.''; PubMed Europe PMC
  46. Ohgusu Y, Ohta KY, Ishii M, Katano T, Urano K, Watanabe J, Inoue K, Yuasa H.; ''Functional characterization of human aquaporin 9 as a facilitative glycerol carrier.''; PubMed Europe PMC
  47. Raina S, Preston GM, Guggino WB, Agre P.; ''Molecular cloning and characterization of an aquaporin cDNA from salivary, lacrimal, and respiratory tissues.''; PubMed Europe PMC
  48. Verkman AS.; ''Aquaporins: translating bench research to human disease.''; PubMed Europe PMC
  49. Takata K, Matsuzaki T, Tajika Y, Ablimit A, Hasegawa T.; ''Localization and trafficking of aquaporin 2 in the kidney.''; PubMed Europe PMC
  50. de Groot BL, Engel A, Grubmüller H.; ''A refined structure of human aquaporin-1.''; PubMed Europe PMC
  51. Moeller HB, MacAulay N, Knepper MA, Fenton RA.; ''Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating.''; PubMed Europe PMC
  52. Ma T, Yang B, Kuo WL, Verkman AS.; ''cDNA cloning and gene structure of a novel water channel expressed exclusively in human kidney: evidence for a gene cluster of aquaporins at chromosome locus 12q13.''; PubMed Europe PMC
  53. Tsukaguchi H, Weremowicz S, Morton CC, Hediger MA.; ''Functional and molecular characterization of the human neutral solute channel aquaporin-9.''; PubMed Europe PMC
  54. Ho JD, Yeh R, Sandstrom A, Chorny I, Harries WE, Robbins RA, Miercke LJ, Stroud RM.; ''Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance.''; PubMed Europe PMC
  55. Nielsen S, Frøkiaer J, Marples D, Kwon TH, Agre P, Knepper MA.; ''Aquaporins in the kidney: from molecules to medicine.''; PubMed Europe PMC
  56. Kuriyama H, Kawamoto S, Ishida N, Ohno I, Mita S, Matsuzawa Y, Matsubara K, Okubo K.; ''Molecular cloning and expression of a novel human aquaporin from adipose tissue with glycerol permeability.''; PubMed Europe PMC
  57. Elkjaer M, Vajda Z, Nejsum LN, Kwon T, Jensen UB, Amiry-Moghaddam M, Frøkiaer J, Nielsen S.; ''Immunolocalization of AQP9 in liver, epididymis, testis, spleen, and brain.''; PubMed Europe PMC
  58. Sorani MD, Zador Z, Zador Z, Hurowitz E, Yan D, Giacomini KM, Manley GT.; ''Novel variants in human Aquaporin-4 reduce cellular water permeability.''; PubMed Europe PMC
  59. Lu M, Lee MD, Smith BL, Jung JS, Agre P, Verdijk MA, Merkx G, Rijss JP, Deen PM.; ''The human AQP4 gene: definition of the locus encoding two water channel polypeptides in brain.''; PubMed Europe PMC
  60. Denker BM, Smith BL, Kuhajda FP, Agre P.; ''Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules.''; PubMed Europe PMC
  61. Kondo H, Shimomura I, Kishida K, Kuriyama H, Makino Y, Nishizawa H, Matsuda M, Maeda N, Nagaretani H, Kihara S, Kurachi Y, Nakamura T, Funahashi T, Matsuzawa Y.; ''Human aquaporin adipose (AQPap) gene. Genomic structure, promoter analysis and functional mutation.''; PubMed Europe PMC
  62. Preston GM, Carroll TP, Guggino WB, Agre P.; ''Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.''; PubMed Europe PMC
  63. Deen PM, Verdijk MA, Knoers NV, Wieringa B, Monnens LA, van Os CH, van Oost BA.; ''Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine.''; PubMed Europe PMC
  64. Wang JP, Hou XH.; ''Expression of aquaporin 8 in colonic epithelium with diarrhoea-predominant irritable bowel syndrome.''; PubMed Europe PMC
  65. Carbrey JM, Agre P.; ''Discovery of the aquaporins and development of the field.''; PubMed Europe PMC
  66. Marrades MP, Milagro FI, Martínez JA, Moreno-Aliaga MJ.; ''Differential expression of aquaporin 7 in adipose tissue of lean and obese high fat consumers.''; PubMed Europe PMC
  67. Frühbeck G, Catalán V, Gómez-Ambrosi J, Rodríguez A.; ''Aquaporin-7 and glycerol permeability as novel obesity drug-target pathways.''; PubMed Europe PMC
  68. Hatakeyama S, Yoshida Y, Tani T, Koyama Y, Nihei K, Ohshiro K, Kamiie JI, Yaoita E, Suda T, Hatakeyama K, Yamamoto T.; ''Cloning of a new aquaporin (AQP10) abundantly expressed in duodenum and jejunum.''; PubMed Europe PMC
  69. Padma S, Smeltz AM, Banks PM, Iannitti DA, McKillop IH.; ''Altered aquaporin 9 expression and localization in human hepatocellular carcinoma.''; PubMed Europe PMC

History

View all...
CompareRevisionActionTimeUserComment
101641view11:50, 1 November 2018ReactomeTeamreactome version 66
101177view21:37, 31 October 2018ReactomeTeamreactome version 65
100703view20:10, 31 October 2018ReactomeTeamreactome version 64
100253view16:55, 31 October 2018ReactomeTeamreactome version 63
99806view15:20, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93844view13:40, 16 August 2017ReactomeTeamreactome version 61
93400view11:22, 9 August 2017ReactomeTeamreactome version 61
88086view09:15, 26 July 2016RyanmillerOntology Term : 'transport pathway' added !
88085view09:14, 26 July 2016RyanmillerOntology Term : 'water transport pathway' added !
88084view09:12, 26 July 2016RyanmillerOntology Term : 'regulatory pathway' added !
86485view09:19, 11 July 2016ReactomeTeamreactome version 56
83120view10:01, 18 November 2015ReactomeTeamVersion54
81770view10:17, 26 August 2015ReactomeTeamVersion53
77006view08:30, 17 July 2014ReactomeTeamFixed remaining interactions
76711view12:07, 16 July 2014ReactomeTeamFixed remaining interactions
76037view10:09, 11 June 2014ReactomeTeamRe-fixing comment source
75746view11:23, 10 June 2014ReactomeTeamReactome 48 Update
75096view14:04, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74743view08:49, 30 April 2014ReactomeTeamReactome46
42093view21:56, 4 March 2011MaintBotAutomatic update
39903view05:55, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
AQP0,1,2,3,4,5,7,8,9,10,11,12AComplexR-HSA-8862069 (Reactome)
AQP1 ProteinP29972 (Uniprot-TrEMBL)
AQP10 ProteinQ96PS8 (Uniprot-TrEMBL)
AQP11 ProteinQ8NBQ7 (Uniprot-TrEMBL)
AQP12A ProteinQ8IXF9 (Uniprot-TrEMBL)
AQP3 ProteinQ92482 (Uniprot-TrEMBL)
AQP3,7,9,10ComplexR-HSA-507882 (Reactome)
AQP4 ProteinP55087 (Uniprot-TrEMBL)
AQP5 ProteinP55064 (Uniprot-TrEMBL)
AQP6 ProteinQ13520 (Uniprot-TrEMBL)
AQP6 tetramerComplexR-HSA-432253 (Reactome) The formation of homotetramers by Aquaporin-6 (AQP6) is inferred from human AQP1, AQP2, AQP3, AQP4, and AQP5.
AQP7 ProteinO14520 (Uniprot-TrEMBL)
AQP8 ProteinO94778 (Uniprot-TrEMBL)
AQP9 ProteinO43315 (Uniprot-TrEMBL)
AQP9,10ComplexR-HSA-507881 (Reactome)
Anions transported by Aquaporin-6ComplexR-ALL-879865 (Reactome)
Anions transported by Aquaporin-6ComplexR-ALL-879874 (Reactome)
Br- MetaboliteCHEBI:15858 (ChEBI)
Cl- MetaboliteCHEBI:17996 (ChEBI)
Fl- MetaboliteCHEBI:17051 (ChEBI)
GlycerolMetaboliteCHEBI:17754 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
I- MetaboliteCHEBI:16382 (ChEBI)
MIP ProteinP30301 (Uniprot-TrEMBL)
NO3- MetaboliteCHEBI:17632 (ChEBI)
UreaMetaboliteCHEBI:16199 (ChEBI)
glycerolMetaboliteCHEBI:17754 (ChEBI)
p-S256-AQP2 ProteinP41181 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
AQP0,1,2,3,4,5,7,8,9,10,11,12Amim-catalysisR-HSA-507868 (Reactome)
AQP0,1,2,3,4,5,7,8,9,10,11,12Amim-catalysisR-HSA-507870 (Reactome)
AQP3,7,9,10mim-catalysisR-HSA-507869 (Reactome)
AQP3,7,9,10mim-catalysisR-HSA-507871 (Reactome)
AQP6 tetramermim-catalysisR-HSA-432034 (Reactome)
AQP6 tetramermim-catalysisR-HSA-432036 (Reactome)
AQP9,10mim-catalysisR-HSA-507873 (Reactome)
AQP9,10mim-catalysisR-HSA-507875 (Reactome)
Anions transported by Aquaporin-6ArrowR-HSA-432034 (Reactome)
Anions transported by Aquaporin-6ArrowR-HSA-432036 (Reactome)
Anions transported by Aquaporin-6R-HSA-432034 (Reactome)
Anions transported by Aquaporin-6R-HSA-432036 (Reactome)
GlycerolArrowR-HSA-507869 (Reactome)
GlycerolR-HSA-507871 (Reactome)
H2OArrowR-HSA-507868 (Reactome)
H2OArrowR-HSA-507870 (Reactome)
H2OR-HSA-507868 (Reactome)
H2OR-HSA-507870 (Reactome)
R-HSA-432034 (Reactome) Aquaporin-6 (AQP6) passively transports anions across membranes. Rat AQP6 has been shown to transport anions, with the highest permeability for nitrate, the lowest permeability for fluoride, and low permeability for water. In rat AQP6 is expressed in the acid-secreting type-A intercalated cells of renal ducts where it co-localizes with the proton-ATPase in the membranes of intracellular vesicles. AQP6 is gated by low pH.
R-HSA-432036 (Reactome) Aquaporin-6 (AQP6) passively transports anions across membranes. Rat AQP6 has been shown to transport anions, with the highest permeability for nitrate, the lowest permeability for fluoride, and low permeability for water. In rat AQP6 is expressed in the acid-secreting type-A intercalated cells of renal ducts where it co-localizes with the proton-ATPase in the membranes of intracellular vesicles. AQP6 is gated by low pH.
R-HSA-507868 (Reactome) Aquaporin-0 (AQP0, also known as MIP), AQP1, AQP2, AQP3, AQP4, AQP5, AQP6, AQP7, AQP8, AQP9, AQP10 and AQP11 are 6-pass transmembrane proteins that passively transport water across the plasma membrane according to the concentration gradient. Each molecule contains a water channel and subunits assemble into homotetramers. In principle water can move in either direction through an aquaporin, however in vivo flow may occur in only one direction. Conductance of water by AQP0 and AQP11 are low relative to other aquaporins. AQP11 and AQP12 are not fully characterised and their ability to to allow transport of water is still debated .
R-HSA-507869 (Reactome) Aquaporin-3 (AQP3), AQP7, AQP9, and AQP10 are 6-pass transmembrane proteins that passively transport glycerol across the plasma membrane through a pore in each subunit of a homotetramer.
R-HSA-507870 (Reactome) Aquaporin-0 (AQP0, also known as MIP), AQP1, AQP2, AQP3, AQP4, AQP5, AQP6, AQP7, AQP8, AQP9, AQP10 and AQP11 are 6-pass transmembrane proteins that passively transport water across the plasma membrane according to the concentration gradient. Each molecule contains a water channel and subunits assemble into homotetramers. In principle water can move in either direction through an aquaporin, however in vivo flow may occur in only one direction. Conductance of water by AQP0 and AQP11 are low relative to other aquaporins. AQP11 and AQP12 are not fully characterised and their ability to to allow transport of water is still debated .
R-HSA-507871 (Reactome) Aquaporin-3 (AQP3), AQP7, AQP9, and AQP10 are 6-pass transmembrane proteins that passively transport glycerol across the plasma membrane through a pore in each subunit of a homotetramer.
R-HSA-507873 (Reactome) Aquaporin-9 (AQP9) and AQP10 are 6-pass transmembrane proteins that passively transport urea across the plasma membrane through a pore in each subunit of a homotetramer.
R-HSA-507875 (Reactome) Aquaporin-9 (AQP9) and AQP10 are 6-pass transmembrane proteins that passively transport urea across the plasma membrane through a pore in each subunit of a homotetramer.
UreaArrowR-HSA-507873 (Reactome)
UreaArrowR-HSA-507875 (Reactome)
UreaR-HSA-507873 (Reactome)
UreaR-HSA-507875 (Reactome)
glycerolArrowR-HSA-507871 (Reactome)
glycerolR-HSA-507869 (Reactome)
Personal tools