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1.A.8.8.1
Aquaporin 1 (CO2-, O2- and nitrous oxide-permeable and water-selective) (Zwiazek et al. 2017). Aquaporin-1 tunes pain perception by interacting with Na(v)1.8 Na+ channels in dorsal root ganglion neurons (Zhang and Verkman, 2010). It is upregulated in skeletal muscle in muscular dystrophy (Au et al. 2008). AQP1 has been reported to first insert as a four-helical intermediate, where helices 2 and 4 are not inserted into the membrane. In a second step this intermediate is folded into a six-helical topology. During this process, the orientation of the third helix is inverted, and it can shift out the membrane core (Virkki et al. 2014).  Its synthesis is regluated by Kruppel-like factor 2 (KLF2; Q9Y5W3) which also interacts directly with Aqp1 (Fontijn et al. 2015). A nanoscale ion pump has been derived artificially from Aqp1 (Decker et al. 2017).

Accession Number:P29972
Protein Name:AQP1 or CHIP28
Length:269
Molecular Weight:28526.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate carbon dioxide

Cross database links:

Genevestigator: P29972
eggNOG: prNOG13886
DIP: DIP-29607N
RefSeq: NP_932766.1   
Entrez Gene ID: 358   
Pfam: PF00230   
Drugbank: Drugbank Link   
OMIM: 107776  gene
110450  phenotype
KEGG: hsa:358   

Gene Ontology

GO:0016324 C:apical plasma membrane
GO:0009925 C:basal plasma membrane
GO:0031526 C:brush border membrane
GO:0005737 C:cytoplasm
GO:0005887 C:integral to plasma membrane
GO:0031965 C:nuclear membrane
GO:0042383 C:sarcolemma
GO:0051739 F:ammonia transmembrane transporter activity
GO:0035379 F:carbon dioxide transmembrane transporter ac...
GO:0015168 F:glycerol transmembrane transporter activity
GO:0005223 F:intracellular cGMP activated cation channel...
GO:0030184 F:nitric oxide transmembrane transporter acti...
GO:0005267 F:potassium channel activity
GO:0015079 F:potassium ion transmembrane transporter act...
GO:0005515 F:protein binding
GO:0015250 F:water channel activity
GO:0015696 P:ammonium transport
GO:0035378 P:carbon dioxide transmembrane transport
GO:0006884 P:cell volume homeostasis
GO:0071474 P:cellular hyperosmotic response
GO:0071320 P:cellular response to cAMP
GO:0071280 P:cellular response to copper ion
GO:0071549 P:cellular response to dexamethasone stimulus
GO:0070301 P:cellular response to hydrogen peroxide
GO:0071456 P:cellular response to hypoxia
GO:0071260 P:cellular response to mechanical stimulus
GO:0071288 P:cellular response to mercury ion
GO:0071300 P:cellular response to retinoic acid
GO:0071472 P:cellular response to salt stress
GO:0034644 P:cellular response to UV
GO:0033326 P:cerebrospinal fluid secretion
GO:0006182 P:cGMP biosynthetic process
GO:0030950 P:establishment or maintenance of actin cytos...
GO:0015793 P:glycerol transport
GO:0021670 P:lateral ventricle development
GO:0050891 P:multicellular organismal water homeostasis
GO:0043066 P:negative regulation of apoptosis
GO:0030185 P:nitric oxide transport
GO:0042476 P:odontogenesis
GO:0030157 P:pancreatic juice secretion
GO:0045766 P:positive regulation of angiogenesis
GO:0048146 P:positive regulation of fibroblast prolifera...
GO:0046878 P:positive regulation of saliva secretion
GO:0006813 P:potassium ion transport
GO:0003097 P:renal water transport
GO:0042493 P:response to drug
GO:0035377 P:transepithelial water transport

References (19)

[1] “Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family.”  Preston G.M.et.al.   1722319
[2] “The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization.”  Moon C.et.al.   8340403
[3] “Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human retinal pigment epithelium.”  Ruiz A.C.et.al.   8703970
[4] “The water channel gene in human uterus.”  Li X.et.al.   7517253
[5] “Human protein factory for converting the transcriptome into an in vitro-expressed proteome.”  Goshima N.et.al.   19054851
[6] “The DNA sequence of human chromosome 7.”  Hillier L.W.et.al.   12853948
[7] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[8] “Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins.”  Smith B.L.et.al.   2007592
[9] “Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.”  Preston G.M.et.al.   1373524
[10] “The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel.”  Preston G.M.et.al.   7677994
[11] “Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis.”  Preston G.M.et.al.   7507481
[12] “Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.”  Daub H.et.al.   18691976
[13] “The three-dimensional structure of human erythrocyte aquaporin CHIP.”  Walz T.et.al.   7518771
[14] “The three-dimensional structure of aquaporin-1.”  Walz T.et.al.   9177353
[15] “Structural determinants of water permeation through aquaporin-1.”  Murata K.et.al.   11034202
[16] “A refined structure of human aquaporin-1.”  de Groot B.L.et.al.   11532455
[17] “Visualization of a water-selective pore by electron crystallography in vitreous ice.”  Ren G.et.al.   11171962
[18] “Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens.”  Smith B.L.et.al.   7521882
[19] “Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels.”  Preston G.M.et.al.   7521540
Structure:
1FQY   1H6I   1IH5   4CSK     

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FASTA formatted sequence
1:	MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI 
61:	ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT 
121:	GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH 
181:	LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD 
241:	RVKVWTSGQV EEYDLDADDI NSRVEMKPK