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AQP1 Membrane Protein Introduction

Introduction of AQP1

AQP1 is also known as Aquaporin-1, Aquaporin-CHIP, Urine water channel, Water channel protein for red blood cells and kidney proximal tubule. It belongs to the Aquaporins (AQPs) family which is a class of channel protein and is expressed in the plasma membrane of bacteria, plant, and animal cells. AQP1 is identified from human red blood cell membranes by Gheorghe Benga's research group in 1986 for the first time. AQP1 has six membrane-spanning domains and two domains that partially insert into the membrane (M1–M8), forming an amino acid-lined pore down the center of the protein.

Basic Information of AQP1
Protein Name Aquaporin-1
Gene Name AQP1
Aliases Aquaporin-1, Aquaporin-CHIP, Urine water channel
Organism Homo sapiens (Human)
UniProt ID P29972
Transmembrane Times 8
Length (aa) 269
Sequence MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK

Function of AQP1 Membrane Protein

AQP1 channels in the major intrinsic protein (MIP) family mediate water movement across membranes by a transmembrane osmotic gradient in the brain, kidney, vascular system, and other tissues. So, AQP1 is also known as water channels. AQP1 knockout mice have impaired urine concentration, reduced water movement across the peritoneum and lung microvessels. In the brain, AQP1 participates in the generation of cerebrospinal fluid. Besides, the site of AQP1 expression may be an important determinant of its role in myocardial water balance in health and disease. For example, if AQP1 is expressed in cardiomyocytes, it may facilitate water accumulation and clearance from these cells. If it is found in endothelial cells, it may mediate water flux between the vasculature and the interstitium. In addition, the increased activity of AQP1 in the presence of PKC may contribute to the stimulation of physiological processes that are modulated by AQP1 such as endothelial permeability, angiogenesis, and urea concentration.

Structure of AQP1 membrane protein. Fig.1 Structure of AQP1 membrane protein.

Application of AQP1 Membrane Protein in Literature

  1. Benga G. The first discovered water channel protein, later called aquaporin 1: Molecular characteristics, functions and medical implications. Molecular Aspects of Medicine. 2012, 33(5):518-534. PubMed ID: 22705445

    This article reviews the role of AQP1, the genetics of AQP1 and mutations in cell migration and angiogenesis in relation with cancer. Meanwhile, the role of AQP1 in red blood cells is discussed based on the comparative studies of water permeability in over 30 species.

  2. Conner M.T., et al.Rapid Aquaporin Translocation Regulates Cellular Water Flow: mechanism of hypotonicity-induced subcellular localization of aquaporin 1 water channel. The Journal of Biological Chemistry. 2012, 287(14):11516-11525. PubMed ID: 22334691

    This article describes a novel pathway in mammalian cells whereby a hypotonic stimulus directly induces intracellular calcium elevations through transient receptor potential channels, which trigger AQP1 translocation.

  3. Jiang Y., et al. Endothelial Aquaporin-1 (AQP1) Expression Is Regulated by Transcription Factor Mef2c. Molecules and Cells. 2016, 39(4):292-298. PubMed ID: 26923194

    The data of this article demonstrate that AQP1 is a direct target of Mef2c in regulating angiogenesis and vasculogenesis of endothelial cells.

  4. Agbani E.O., et al. Aquaporin-1 regulates platelet procoagulant membrane dynamics and in vivo thrombosis. JCI Insight. 2018, 3(10):e99062. PubMed ID: 29769447

    This article concludes that AQP1 is a major regulator of the platelet procoagulant response, able to modulate coagulation after injury or pathologic stimuli without affecting other platelet functional responses or normal hemostasis.

  5. Li J., et al. The potential role of aquaporin 1 on aristolochic acid I induced epithelial mesenchymal transition on HK-2 cells. Journal of Cellular Physiology. 2017, 233(6):4919-4925. PubMed ID: 29215709

    This article suggests that AQP1 could be adjusted by Erk1/2 signaling. Moreover, the inhibitory effect of AA-I on AQP1 was stronger than that of TGF-β1, suggests that AQP1 may be an important target on AAN clinical therapy.

AQP1 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-AQP1 antibody development services.


Creative Biolabs is a forward-looking research institute, as well as a leading customer service provider in the field of membrane protein,we, have built up a custom-service-centered business model to help our worldwide customers to accomplish numerous challenging functional membrane proteins projects. Please feel free to contact us for more information.

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