Aqp8
entrez
11833
canonical
uniprot
P56404
canonical
ensembl
ENSMUSG00000030762
resolver
ensp
ENSMUSP00000033023
resolver
ensp
ENSMUSP00000095664
resolver
enst
ENSMUST00000033023
resolver
enst
ENSMUST00000098056
resolver
genesymbol
Aqp8
resolver
uniprot
A0A0X1KG59
resolver
uniprot
Q3UJ16
resolver
uniprot
Q91XC2
resolver
uniprot_entry
A0A0X1KG59_MOUSE
resolver
uniprot_entry
AQP8_MOUSE
resolver
uniprot_entry
Q3UJ16_MOUSE
resolver
uniprot_sec
Q91XC2
resolver
activity_regulation
ACTIVITY REGULATION: Reversibly gated by a two-step sulfenylation-persulfidation process in cells undergoing diverse stresses. {ECO:0000250|UniProtKB:O94778}.
uniprot
proteins
amino_acid_sequence
MSGEQTPMCSMDLPEVKVKTSMAGRCRVFWYEQYVQPCIVELVGSALFIFIGCLSVIENSPNTGLLQPALAHGLALGLIIATLGNISGGHFNPAVSLAVTVIGGLKTMLLIPYWISQLFGGLIGAALAKVVSPEERFWNASGAAFAIVQEQEQVAEALGIEIILTMLLVLAVCMGAVNEKTMGPLAPFSIGFSVIVDILAGGSISGACMNPARAFGPAVMAGYWDFHWIYWLGPLLAGLFVGLLIRLLIGDEKTRLILKSR
uniprot
proteins
function
FUNCTION: Channel that allows the facilitated permeation of water and uncharged molecules, such as hydrogen peroxide and the neutral form of ammonia (NH3), through cellular membranes such as plasma membrane, inner mitochondrial membrane and endoplasmic reticulum membrane of several tissues (PubMed:15647389, PubMed:15948717, PubMed:16624991, PubMed:21117174, PubMed:27256569, PubMed:9388476). The transport of ammonia neutral form induces a parallel transport of proton, at alkaline pH when the concentration of ammonia is high (By similarity). However, it is unclear whether the transport of proton takes place via the aquaporin or via an endogenous pathway (By similarity). Also, may transport ammonia analogs such as formamide and methylamine, a transport favourited at basic pH due to the increase of unprotonated (neutral) form, which is expected to favor diffusion (By similarity). In vitro, may be also permeable to urea but not to glycerol (PubMed:9388476). Does not transport urea or glycerol (By similarity). The water transport mechanism is mercury- and copper-sensitive and passive in response to osmotic driving forces (PubMed:9388476). At the canicular plasma membrane, mediates the osmotic transport of water toward the bile canaliculus and facilitates the cAMP-induced bile canalicular water secretion, a process involved in bile formation (By similarity). In addition, mediates the hydrogen peroxide release from hepatocyte mitochondria that modulates the SREBF2-mediated cholesterol synthesis and facilitates the mitochondrial ammonia uptake which is metabolized into urea, mainly under glucagon stimulation (By similarity). In B cells, transports the CYBB-generated hydrogen peroxide from the external leaflet of the plasma membrane to the cytosol to promote B cell activation and differentiation for signal amplification (PubMed:27256569). In the small intestine and colon system, mediates water transport through mitochondria and apical membrane of epithelial cells (By similarity). May play an important role in the adaptive response of proximal tubule cells to acidosis possibly facilitating mitochondrial ammonia transport (By similarity). {ECO:0000250|UniProtKB:O94778, ECO:0000250|UniProtKB:P56405, ECO:0000269|PubMed:15647389, ECO:0000269|PubMed:15948717, ECO:0000269|PubMed:16624991, ECO:0000269|PubMed:21117174, ECO:0000269|PubMed:27256569, ECO:0000269|PubMed:9388476}.
uniprot
proteins
mass_dalton
27797
uniprot
proteins
post_translational_modification
PTM: Sulfenylation at Cys-53(C53-SOH) when hydrogen peroxide flows through the AQP8 channel, making it susceptible to hydrogen sulfide produced by CBS. {ECO:0000250|UniProtKB:O94778}.; PTM: Persulfidation at Cys-53 is required to gate AQP8 channel; under stress condition, hydrogen peroxide accumulates in the cell leading to CBS activation that produces hydrogen sulfide inducing persulfidation of oxidized Cys-53 (C53-SOH). {ECO:0000250|UniProtKB:O94778}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P56405}.
uniprot
proteins
protein_family
MIP/aquaporin (TC 1.A.8) family
uniprot
proteins
pubmed
10449905
uniprot
proteins
pubmed
14512882
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15647389
uniprot
proteins
pubmed
15859952
uniprot
proteins
pubmed
15948717
uniprot
proteins
pubmed
16624991
uniprot
proteins
pubmed
21117174
uniprot
proteins
pubmed
21602842
uniprot
proteins
pubmed
27256569
uniprot
proteins
pubmed
9388476
uniprot
proteins
sequence_length
261
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14512882, ECO:0000269|PubMed:15647389, ECO:0000269|PubMed:15859952}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000269|PubMed:14512882, ECO:0000269|PubMed:15859952, ECO:0000305|PubMed:14512882, ECO:0000305|PubMed:15859952}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:15859952}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P56405}; Multi-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000269|PubMed:14512882}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at the hepatocyte canalicular plasma membrane (PubMed:14512882). Localized at the apical membrane of the gall-bladder epithelial cells lining both the neck and corpus regions (PubMed:15859952). Localized on the apical membranes of pancreatic acinar cells and mucosal epithelium of the colon and jejunum. Trafficking from intracellular vesicles to the hepatocyte canalicular plasma membrane is induced by glucagon or the second messenger 3',5'-cyclic AMP and the translocation is protein kinase A and microtubule-dependent. Localized at the brush border membranes of epithelial cells from jejunum (By similarity). Localized at the luminal membranes of crypts in ascending colon (PubMed:15647389). {ECO:0000250|UniProtKB:P56405, ECO:0000269|PubMed:14512882, ECO:0000269|PubMed:15647389, ECO:0000269|PubMed:15859952}.
uniprot
proteins
transmembrane_region
TRANSMEM 37..57; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 85..105; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 108..128; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 157..177; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 184..204; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 229..249; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins