Aquaporin 1: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
m (Bot: HTTP→HTTPS (v470))
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Aquaporin 1''' is a [[protein]] that in humans is encoded by the ''AQP1'' [[gene]].
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = no
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = AQP1.png
| image_source =
|Name = Aquaporin 1 (Colton blood group)
| HGNCid = 633
| Symbol = AQP1
| AltSymbols =; AQP-CHIP; CHIP28; CO; MGC26324
| OMIM = 107776
| ECnumber = 
| Homologene = 68051
| MGIid = 103201
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005372 |text = water transporter activity}} {{GNF_GO|id=GO:0015288 |text = porin activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0019867 |text = outer membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006833 |text = water transport}} {{GNF_GO|id=GO:0007588 |text = excretion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 358
    | Hs_Ensembl = ENSG00000106125
    | Hs_RefseqProtein = NP_932766
    | Hs_RefseqmRNA = NM_198098
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 30917993
    | Hs_GenLoc_end = 30931656
    | Hs_Uniprot = P29972
    | Mm_EntrezGene = 11826
    | Mm_Ensembl = ENSMUSG00000004655
    | Mm_RefseqmRNA = NM_007472
    | Mm_RefseqProtein = NP_031498
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 55266010
    | Mm_GenLoc_end = 55278133
    | Mm_Uniprot = Q3TLW5
  }}
}}
{{SI}}
{{CMG}}


AQP1 is a widely expressed [[Aquaporin|water channel]], whose physiological function has been most thoroughly characterized in the [[kidney]].  It is found in the [[Basolateral membrane|basolateral]] and apical plasma membranes of the [[Nephron#Renal tubule|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).


==Overview==
== Function ==
'''AQP1''' is a widely expressed water channel, whose physiological function has been most thoroughly characterized in the [[kidney]].
 
It is found in the [[Basolateral membrane|basolateral]] and apical plasma membranes of the [[Nephron#Renal tubule|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).
[[Aquaporin]]s are a family of small integral membrane proteins related to the major intrinsic protein ([[MIP (gene)|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.<ref>{{cite web | title = Entrez Gene: AQP1 aquaporin 1 (Colton blood group)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=358| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== See also ==
{{PBB_Summary
| section_title =
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: AQP1 aquaporin 1 (Colton blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=358| accessdate = }}</ref>
}}
 
==See also==
* [[Aquaporin]]
* [[Aquaporin]]
* [[Colton antigen system]]
* [[Colton antigen system]]


==References==
== References ==
{{reflist|2}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Knepper MA | title = The aquaporin family of molecular water channels. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 91 | issue = 14 | pages = 6255–8 | year = 1994 | pmid = 7517546 | pmc = 44179 | doi = 10.1073/pnas.91.14.6255 }}
| citations =
* {{cite journal | vauthors = Borgnia M, Nielsen S, Engel A, Agre P | title = Cellular and molecular biology of the aquaporin water channels. | journal = Annu. Rev. Biochem. | volume = 68 | issue =  | pages = 425–58 | year = 2000 | pmid = 10872456 | doi = 10.1146/annurev.biochem.68.1.425 }}
*{{cite journal | author=Knepper MA |title=The aquaporin family of molecular water channels. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6255-8 |year= 1994 |pmid= 7517546 |doi= }}
* {{cite journal | vauthors = Horster M | title = Embryonic epithelial membrane transporters. | journal = Am. J. Physiol. Renal Physiol. | volume = 279 | issue = 6 | pages = F982–96 | year = 2001 | pmid = 11097616 | doi =  }}
*{{cite journal | author=Borgnia M, Nielsen S, Engel A, Agre P |title=Cellular and molecular biology of the aquaporin water channels. |journal=Annu. Rev. Biochem. |volume=68 |issue=  |pages= 425-58 |year= 2000 |pmid= 10872456 |doi= 10.1146/annurev.biochem.68.1.425 }}
* {{cite journal | vauthors = Yool AJ, Weinstein AM | title = New roles for old holes: ion channel function in aquaporin-1. | journal = News Physiol. Sci. | volume = 17 | issue =  | pages = 68–72 | year = 2002 | pmid = 11909995 | doi =  }}
*{{cite journal | author=Horster M |title=Embryonic epithelial membrane transporters. |journal=Am. J. Physiol. Renal Physiol. |volume=279 |issue= 6 |pages= F982-96 |year= 2001 |pmid= 11097616 |doi=  }}
* {{cite journal | vauthors = Mitra AK, Ren G, Reddy VS, Cheng A, Froger A | title = The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice | journal = Novartis Found. Symp. | volume = 245 | issue =  | pages = 33–46; discussion 46–50; 165–8 | year = 2002 | pmid = 12027013 | doi = 10.1002/0470868759.ch4 | isbn = 978-0-470-86875-1 | series = Novartis Foundation Symposia }}
*{{cite journal | author=Yool AJ, Weinstein AM |title=New roles for old holes: ion channel function in aquaporin-1. |journal=News Physiol. Sci. |volume=17 |issue=  |pages= 68-72 |year= 2002 |pmid= 11909995 |doi=  }}
* {{cite journal | vauthors = Ripoche P, Goossens D, Devuyst O, Gane P, Colin Y, Verkman AS, Cartron JP | title = Role of RhAG and AQP1 in NH<sub>3</sub> and CO<sub>2</sub> gas transport in red cell ghosts: a stopped-flow analysis | journal = Transfusion clinique et biologique : journal de la Société française de transfusion sanguine | volume = 13 | issue = 1–2 | pages = 117–22 | year = 2006 | pmid = 16574458 | doi = 10.1016/j.tracli.2006.03.004 }}
*{{cite journal | author=Mitra AK, Ren G, Reddy VS, ''et al.'' |title=The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice. |journal=Novartis Found. Symp. |volume=245 |issue=  |pages= 33-46; discussion 46-50; 165-8 |year= 2002 |pmid= 12027013 |doi= }}
* {{cite journal | vauthors = Preston GM, Carroll TP, Guggino WB, Agre P | title = Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein | journal = Science | volume = 256 | issue = 5055 | pages = 385–7 | year = 1992 | pmid = 1373524 | doi = 10.1126/science.256.5055.385 }}
*{{cite journal | author=Ripoche P, Goossens D, Devuyst O, ''et al.'' |title=Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis. |journal=Transfusion clinique et biologique : journal de la Société française de transfusion sanguine |volume=13 |issue= 1-2 |pages= 117-22 |year= 2006 |pmid= 16574458 |doi= 10.1016/j.tracli.2006.03.004 }}
* {{cite journal | vauthors = Preston GM, Agre P | title = Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 88 | issue = 24 | pages = 11110–4 | year = 1992 | pmid = 1722319 | pmc = 53083 | doi = 10.1073/pnas.88.24.11110 }}
*{{cite journal | author=Preston GM, Carroll TP, Guggino WB, Agre P |title=Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. |journal=Science |volume=256 |issue= 5055 |pages= 385-7 |year= 1992 |pmid= 1373524 |doi= }}
* {{cite journal | vauthors = Smith BL, Agre P | title = Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins | journal = J. Biol. Chem. | volume = 266 | issue = 10 | pages = 6407–15 | year = 1991 | pmid = 2007592 | doi =  }}
*{{cite journal | author=Preston GM, Agre P |title=Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 24 |pages= 11110-4 |year= 1992 |pmid= 1722319 |doi= }}
* {{cite journal | vauthors = Denker BM, Smith BL, Kuhajda FP, Agre P | title = Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules | journal = J. Biol. Chem. | volume = 263 | issue = 30 | pages = 15634–42 | year = 1988 | pmid = 3049610 | doi =  }}
*{{cite journal | author=Smith BL, Agre P |title=Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. |journal=J. Biol. Chem. |volume=266 |issue= 10 |pages= 6407-15 |year= 1991 |pmid= 2007592 |doi=  }}
* {{cite journal | vauthors = Zelinski T, Kaita H, Lewis M, Coghlan G, Philipps S, Belcher E, McAlpine PJ, Coopland G, Wong P | title = The Colton blood group locus. A linkage analysis | journal = Transfusion | volume = 28 | issue = 5 | pages = 435–8 | year = 1988 | pmid = 3166547 | doi = 10.1046/j.1537-2995.1988.28588337331.x }}
*{{cite journal | author=Denker BM, Smith BL, Kuhajda FP, Agre P |title=Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. |journal=J. Biol. Chem. |volume=263 |issue= 30 |pages= 15634-42 |year= 1988 |pmid= 3049610 |doi=  }}
* {{cite journal | vauthors = Preston GM, Jung JS, Guggino WB, Agre P | title = Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis | journal = J. Biol. Chem. | volume = 269 | issue = 3 | pages = 1668–73 | year = 1994 | pmid = 7507481 | doi =  }}
*{{cite journal | author=Zelinski T, Kaita H, Lewis M, ''et al.'' |title=The Colton blood group locus. A linkage analysis. |journal=Transfusion |volume=28 |issue= 5 |pages= 435-8 |year= 1988 |pmid= 3166547 |doi= }}
* {{cite journal | vauthors = Skach WR, Shi LB, Calayag MC, Frigeri A, Lingappa VR, Verkman AS | title = Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum | journal = J. Cell Biol. | volume = 125 | issue = 4 | pages = 803–15 | year = 1994 | pmid = 7514605 | pmc = 2120064 | doi = 10.1083/jcb.125.4.803 }}
*{{cite journal | author=Preston GM, Jung JS, Guggino WB, Agre P |title=Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis. |journal=J. Biol. Chem. |volume=269 |issue= 3 |pages= 1668-73 |year= 1994 |pmid= 7507481 |doi=  }}
* {{cite journal | vauthors = Li X, Yu H, Koide SS | title = The water channel gene in human uterus | journal = Biochem. Mol. Biol. Int. | volume = 32 | issue = 2 | pages = 371–7 | year = 1994 | pmid = 7517253 | doi =  }}
*{{cite journal | author=Skach WR, Shi LB, Calayag MC, ''et al.'' |title=Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum. |journal=J. Cell Biol. |volume=125 |issue= 4 |pages= 803-15 |year= 1994 |pmid= 7514605 |doi= }}
* {{cite journal | vauthors = Walz T, Smith BL, Agre P, Engel A | title = The three-dimensional structure of human erythrocyte aquaporin CHIP | journal = EMBO J. | volume = 13 | issue = 13 | pages = 2985–93 | year = 1994 | pmid = 7518771 | pmc = 395186 | doi =  }}
*{{cite journal | author=Li X, Yu H, Koide SS |title=The water channel gene in human uterus. |journal=Biochem. Mol. Biol. Int. |volume=32 |issue= 2 |pages= 371-7 |year= 1994 |pmid= 7517253 |doi=  }}
* {{cite journal | vauthors = Preston GM, Smith BL, Zeidel ML, Moulds JJ, Agre P | title = Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels | journal = Science | volume = 265 | issue = 5178 | pages = 1585–7 | year = 1994 | pmid = 7521540 | doi = 10.1126/science.7521540 }}
*{{cite journal | author=Walz T, Smith BL, Agre P, Engel A |title=The three-dimensional structure of human erythrocyte aquaporin CHIP. |journal=EMBO J. |volume=13 |issue= 13 |pages= 2985-93 |year= 1994 |pmid= 7518771 |doi=  }}
* {{cite journal | vauthors = Smith BL, Preston GM, Spring FA, Anstee DJ, Agre P | title = Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens | journal = J. Clin. Invest. | volume = 94 | issue = 3 | pages = 1043–9 | year = 1994 | pmid = 7521882 | pmc = 295159 | doi = 10.1172/JCI117418 }}
*{{cite journal | author=Preston GM, Smith BL, Zeidel ML, ''et al.'' |title=Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels. |journal=Science |volume=265 |issue= 5178 |pages= 1585-7 |year= 1994 |pmid= 7521540 |doi= }}
* {{cite journal | vauthors = van Hoek AN, Wiener MC, Verbavatz JM, Brown D, Lipniunas PH, Townsend RR, Verkman AS | title = Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels | journal = Biochemistry | volume = 34 | issue = 7 | pages = 2212–9 | year = 1995 | pmid = 7532004 | doi = 10.1021/bi00007a015 }}
*{{cite journal | author=Smith BL, Preston GM, Spring FA, ''et al.'' |title=Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens. |journal=J. Clin. Invest. |volume=94 |issue= 3 |pages= 1043-9 |year= 1994 |pmid= 7521882 |doi= }}
* {{cite journal | vauthors = Keen TJ, Inglehearn CF, Patel RJ, Green ED, Peluso DC, Bhattacharya SS | title = Localization of the aquaporin 1 (AQP1) gene within a YAC contig containing the polymorphic markers D7S632 and D7S526 | journal = Genomics | volume = 25 | issue = 2 | pages = 599–600 | year = 1995 | pmid = 7540589 | doi = 10.1016/0888-7543(95)80070-3 }}
*{{cite journal | author=van Hoek AN, Wiener MC, Verbavatz JM, ''et al.'' |title=Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels. |journal=Biochemistry |volume=34 |issue= 7 |pages= 2212-9 |year= 1995 |pmid= 7532004 |doi= }}
*{{cite journal | author=Keen TJ, Inglehearn CF, Patel RJ, ''et al.'' |title=Localization of the aquaporin 1 (AQP1) gene within a YAC contig containing the polymorphic markers D7S632 and D7S526. |journal=Genomics |volume=25 |issue= 2 |pages= 599-600 |year= 1995 |pmid= 7540589 |doi= }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|Aquaporin+1}}
* {{MeshName|Aquaporin+1}}
* [http://www3.mpibpc.mpg.de/groups/de_groot/gallery.html ''Gallery of Aquaporin Simulations'']
* {{UCSC gene info|AQP1}}


{{NLM content}}
{{NLM content}}
{{Ion channels}}
{{PDB Gallery|geneid=358}}
{{Ion channels|g4}}


[[Category:Integral membrane proteins]]
[[Category:Integral membrane proteins]]
[[pt:aquaporina 1]]
{{WH}}
{{WS}}

Latest revision as of 01:25, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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).

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

References

  1. ↑ "Entrez Gene: AQP1 aquaporin 1 (Colton blood group)".

Further reading

External links

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

Retrieved from "https://www.wikidoc.org/index.php?title=Aquaporin_1&oldid=1421522"