アクア・リン1
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- AQP1
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/05/26 15:20:03」(JST)
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Aquaporin 1 (Colton blood group) |
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Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1FQY, 1H6I, 1IH5
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Identifiers |
Symbols |
AQP1 ; AQP-CHIP; CHIP28; CO |
External IDs |
OMIM: 107776 MGI: 103201 HomoloGene: 68051 IUPHAR: 688 GeneCards: AQP1 Gene |
Gene ontology |
Molecular function |
• intracellular cGMP activated cation channel activity
• potassium channel activity
• water transmembrane transporter activity
• protein binding
• ammonium transmembrane transporter activity
• potassium ion transmembrane transporter activity
• glycerol transmembrane transporter activity
• water channel activity
• transmembrane transporter activity
• nitric oxide transmembrane transporter activity
• carbon dioxide transmembrane transporter activity
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Cellular component |
• nucleus
• cytoplasm
• plasma membrane
• integral component of plasma membrane
• brush border
• basal plasma membrane
• basolateral plasma membrane
• apical plasma membrane
• symbiont-containing vacuole
• symbiont-containing vacuole membrane
• brush border membrane
• nuclear membrane
• sarcolemma
• apical part of cell
• extracellular vesicular exosome
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Biological process |
• renal water transport
• cGMP biosynthetic process
• potassium ion transport
• water transport
• cell volume homeostasis
• carbon dioxide transport
• ammonium transport
• bicarbonate transport
• glycerol transport
• cellular homeostasis
• lateral ventricle development
• pancreatic juice secretion
• nitric oxide transport
• establishment or maintenance of actin cytoskeleton polarity
• cerebrospinal fluid secretion
• cellular response to stress
• cellular response to UV
• transepithelial water transport
• carbon dioxide transmembrane transport
• odontogenesis
• response to drug
• negative regulation of apoptotic process
• negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
• small molecule metabolic process
• positive regulation of angiogenesis
• positive regulation of saliva secretion
• positive regulation of fibroblast proliferation
• multicellular organismal water homeostasis
• transmembrane transport
• cellular response to hydrogen peroxide
• cellular response to inorganic substance
• cellular response to mechanical stimulus
• cellular response to copper ion
• cellular response to mercury ion
• cellular response to retinoic acid
• cellular response to cAMP
• cellular response to hypoxia
• cellular response to salt stress
• cellular hyperosmotic response
• cellular response to dexamethasone stimulus
• cellular response to nitric oxide
• potassium ion transmembrane transport
• ammonium transmembrane transport
• maintenance of symbiont-containing vacuole by host
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
358 |
11826 |
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Ensembl |
ENSG00000240583 |
ENSMUSG00000004655 |
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UniProt |
P29972 |
Q02013 |
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RefSeq (mRNA) |
NM_000385 |
NM_007472 |
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RefSeq (protein) |
NP_001171989 |
NP_031498 |
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Location (UCSC) |
Chr 7:
30.89 – 30.97 Mb |
Chr 6:
55.34 – 55.35 Mb |
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PubMed search |
[1] |
[2] |
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Aquaporin 1 is a protein that in humans is encoded by the AQP1 gene.
AQP1 is a widely expressed water channel, whose physiological function has been most thoroughly characterized in the kidney. It is found in the basolateral and apical plasma membranes of the proximal tubules, the descending limb of the loop of Henle, and in the descending portion of the vasa recta. Additionally, it is found in red blood cells, vascular endothelium, the gastrointestinal tract, sweat glands, and lungs.
It is not regulated by vasopressin (ADH).
Contents
- 1 Function
- 2 See also
- 3 References
- 4 Further reading
- 5 External links
Function
Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). This gene encodes an aquaporin which functions as a molecular water channel protein. It is a homotetramer with 6 bilayer spanning domains and N-glycosylation sites. The protein physically resembles channel proteins and is abundant in erythrocytes and renal tubes. The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement.[1]
See also
- Aquaporin
- Colton antigen system
References
- ^ "Entrez Gene: AQP1 aquaporin 1 (Colton blood group)".
Further reading
- Knepper MA (1994). "The aquaporin family of molecular water channels.". Proc. Natl. Acad. Sci. U.S.A. 91 (14): 6255–8. doi:10.1073/pnas.91.14.6255. PMC 44179. PMID 7517546.
- Borgnia M, Nielsen S, Engel A, Agre P (2000). "Cellular and molecular biology of the aquaporin water channels.". Annu. Rev. Biochem. 68: 425–58. doi:10.1146/annurev.biochem.68.1.425. PMID 10872456.
- Horster M (2001). "Embryonic epithelial membrane transporters.". Am. J. Physiol. Renal Physiol. 279 (6): F982–96. PMID 11097616.
- Yool AJ, Weinstein AM (2002). "New roles for old holes: ion channel function in aquaporin-1.". News Physiol. Sci. 17: 68–72. PMID 11909995.
- Mitra AK, Ren G, Reddy VS, Cheng A, Froger A (2002). "The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice". Novartis Found. Symp. Novartis Foundation Symposia 245: 33–46; discussion 46–50; 165–8. doi:10.1002/0470868759.ch4. ISBN 978-0-470-86875-1. PMID 12027013.
- Ripoche P, Goossens D, Devuyst O, Gane P, Colin Y, Verkman AS et al. (2006). "Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis". Transfusion clinique et biologique : journal de la Société française de transfusion sanguine 13 (1–2): 117–22. doi:10.1016/j.tracli.2006.03.004. PMID 16574458.
- Preston GM, Carroll TP, Guggino WB, Agre P (1992). "Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein". Science 256 (5055): 385–7. doi:10.1126/science.256.5055.385. PMID 1373524.
- Preston GM, Agre P (1992). "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. 88 (24): 11110–4. doi:10.1073/pnas.88.24.11110. PMC 53083. PMID 1722319.
- Smith BL, Agre P (1991). "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins". J. Biol. Chem. 266 (10): 6407–15. PMID 2007592.
- Denker BM, Smith BL, Kuhajda FP, Agre P (1988). "Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules". J. Biol. Chem. 263 (30): 15634–42. PMID 3049610.
- Zelinski T, Kaita H, Lewis M, Coghlan G, Philipps S, Belcher E et al. (1988). "The Colton blood group locus. A linkage analysis". Transfusion 28 (5): 435–8. doi:10.1046/j.1537-2995.1988.28588337331.x. PMID 3166547.
- Preston GM, Jung JS, Guggino WB, Agre P (1994). "Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis". J. Biol. Chem. 269 (3): 1668–73. PMID 7507481.
- Skach WR, Shi LB, Calayag MC, Frigeri A, Lingappa VR, Verkman AS (1994). "Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum". J. Cell Biol. 125 (4): 803–15. doi:10.1083/jcb.125.4.803. PMC 2120064. PMID 7514605.
- Li X, Yu H, Koide SS (1994). "The water channel gene in human uterus". Biochem. Mol. Biol. Int. 32 (2): 371–7. PMID 7517253.
- Walz T, Smith BL, Agre P, Engel A (1994). "The three-dimensional structure of human erythrocyte aquaporin CHIP". EMBO J. 13 (13): 2985–93. PMC 395186. PMID 7518771.
- Preston GM, Smith BL, Zeidel ML, Moulds JJ, Agre P (1994). "Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels". Science 265 (5178): 1585–7. doi:10.1126/science.7521540. PMID 7521540.
- Smith BL, Preston GM, Spring FA, Anstee DJ, Agre P (1994). "Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens". J. Clin. Invest. 94 (3): 1043–9. doi:10.1172/JCI117418. PMC 295159. PMID 7521882.
- van Hoek AN, Wiener MC, Verbavatz JM, Brown D, Lipniunas PH, Townsend RR et al. (1995). "Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels". Biochemistry 34 (7): 2212–9. doi:10.1021/bi00007a015. PMID 7532004.
- Keen TJ, Inglehearn CF, Patel RJ, Green ED, Peluso DC, Bhattacharya SS (1995). "Localization of the aquaporin 1 (AQP1) gene within a YAC contig containing the polymorphic markers D7S632 and D7S526". Genomics 25 (2): 599–600. doi:10.1016/0888-7543(95)80070-3. PMID 7540589.
External links
- Aquaporin 1 at the US National Library of Medicine Medical Subject Headings (MeSH)
- Gallery of Aquaporin Simulations
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
PDB gallery
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1fqy: STRUCTURE OF AQUAPORIN-1 AT 3.8 A RESOLUTION BY ELECTRON CRYSTALLOGRAPHY
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1h6i: A REFINED STRUCTURE OF HUMAN AQUAPORIN 1
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1ih5: CRYSTAL STRUCTURE OF AQUAPORIN-1
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1j4n: Crystal Structure of the AQP1 water channel
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UpToDate Contents
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English Journal
- A generic high-throughput assay to detect aquaporin functional mutants: Potential application to discovery of aquaporin inhibitors.
- To J1, Yeo CY1, Soon CH1, Torres J2.
- Biochimica et biophysica acta.Biochim Biophys Acta.2015 Sep;1850(9):1869-76. doi: 10.1016/j.bbagen.2015.05.019. Epub 2015 May 29.
- BACKGROUND: The discovery of stable, yet functional, protein mutants is a limiting factor in the development of biotechnological applications, structural studies or in drug discovery. Rapid detection of functional mutants is especially challenging for water channel aquaporins, as they do not have a
- PMID 26028295
- Water and solute transport across the peritoneal membrane.
- Morelle J1, Devuyst O.
- Current opinion in nephrology and hypertension.Curr Opin Nephrol Hypertens.2015 Sep;24(5):434-43. doi: 10.1097/MNH.0000000000000151.
- PURPOSE OF REVIEW: We review the molecular mechanisms of peritoneal transport and discuss how a better understanding of these mechanisms is relevant for dialysis therapy.RECENT FINDINGS: Peritoneal dialysis involves diffusion and osmosis through the highly vascularized peritoneal membrane. Computer
- PMID 26197201
- PBEF promotes the apoptosis of pulmonary microvascular endothelial cells and regulates the expression of inflammatory factors and AQP1 through the MAPK pathways.
- Ming GF1, Ma XH1, Xu DM1, Liu ZY1, Ai YH1, Liu HX2, Shi ZH3.
- International journal of molecular medicine.Int J Mol Med.2015 Sep;36(3):890-6. doi: 10.3892/ijmm.2015.2283. Epub 2015 Jul 13.
- Pre-B cell colony-enhancing factor (PBEF) has been shown to have a variety of biological functions. Studies have proven that PBEF plays a functional role in acute lung injury (ALI). Therefore, in this study, we aimed to confirm the importance of PBEF in ALI. The effects of PBEF overexpression on t
- PMID 26178576
Japanese Journal
- 抗MOG抗体が強陽性であったChronic relapsing inflammatory optic neuropathy(CRION)の1例
- Intractable Hiccups and Nausea as a Principal Symptom of Neuromyelitis Optica in a Patient with a Prior History of Miller-Fisher Syndrome
- フィンゴリモド投与中に帯状疱疹を発症した多発性硬化症の検討
Related Links
- Knepper MA (1994). "The aquaporin family of molecular water channels.". Proc. Natl. Acad. Sci. U.S.A. 91 (14): 6255-8. PMID 7517546. Borgnia M, Nielsen S, Engel A, Agre P (2000). "Cellular and molecular biology of the aquaporin ...
- Aquaporins Aquaporin-1 (AQP1) was first discovered in human red blood cell membranes by Gheorghe Benga's research group in 1986. [1] However, it was only known to be a novel protein and its function was unknown. Initially ...
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アクアポリン1 aquaporin 1