AQP5_MOUSE
ID AQP5_MOUSE Reviewed; 265 AA.
AC Q9WTY4; Q545H1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Aquaporin-5;
DE Short=AQP-5;
GN Name=Aqp5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=FEBN; TISSUE=Lung;
RX PubMed=10337625; DOI=10.1007/s003359901030;
RA Krane C.M., Towne J.E., Menon A.G.;
RT "Cloning and characterization of murine Aqp5: evidence for a conserved
RT aquaporin gene cluster.";
RL Mamm. Genome 10:498-505(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10400615; DOI=10.1074/jbc.274.29.20071;
RA Ma T., Song Y., Gillespie A., Carlson E.J., Epstein C.J., Verkman A.S.;
RT "Defective secretion of saliva in transgenic mice lacking aquaporin-5 water
RT channels.";
RL J. Biol. Chem. 274:20071-20074(1999).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10619865; DOI=10.1172/jci8258;
RA Ma T., Fukuda N., Song Y., Matthay M.A., Verkman A.S.;
RT "Lung fluid transport in aquaporin-5 knockout mice.";
RL J. Clin. Invest. 105:93-100(2000).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=12042359; DOI=10.1113/jphysiol.2001.020180;
RA Song Y., Sonawane N., Verkman A.S.;
RT "Localization of aquaporin-5 in sweat glands and functional analysis using
RT knockout mice.";
RL J. Physiol. (Lond.) 541:561-568(2002).
RN [6]
RP FUNCTION, INTERACTION WITH TRPV4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16571723; DOI=10.1074/jbc.m600549200;
RA Liu X., Bandyopadhyay B.C., Bandyopadhyay B., Nakamoto T., Singh B.,
RA Liedtke W., Melvin J.E., Ambudkar I.;
RT "A role for AQP5 in activation of TRPV4 by hypotonicity: concerted
RT involvement of AQP5 and TRPV4 in regulation of cell volume recovery.";
RL J. Biol. Chem. 281:15485-15495(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18027168; DOI=10.1080/02713680701733076;
RA Sasaki Y., Tsubota K., Kawedia J.D., Menon A.G., Yasui M.;
RT "The difference of aquaporin 5 distribution in acinar and ductal cells in
RT lacrimal and parotid glands.";
RL Curr. Eye Res. 32:923-929(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23473857; DOI=10.1016/j.jdermsci.2013.01.013;
RA Inoue R., Sohara E., Rai T., Satoh T., Yokozeki H., Sasaki S., Uchida S.;
RT "Immunolocalization and translocation of aquaporin-5 water channel in sweat
RT glands.";
RL J. Dermatol. Sci. 70:26-33(2013).
CC -!- FUNCTION: Forms a water-specific channel (By similarity). Plays an
CC important role in fluid secretion in salivary glands (PubMed:10400615,
CC PubMed:16571723, PubMed:18027168). Required for TRPV4 activation by
CC hypotonicity. Together with TRPV4, controls regulatory volume decrease
CC in salivary epithelial cells (PubMed:16571723). Seems to play a
CC redundant role in water transport in the eye, lung and in sweat glands
CC (PubMed:10619865, PubMed:12042359, PubMed:18027168).
CC {ECO:0000250|UniProtKB:P55064, ECO:0000269|PubMed:10400615,
CC ECO:0000269|PubMed:10619865, ECO:0000269|PubMed:12042359,
CC ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:18027168}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with TRPV4; the
CC interaction is probably indirect and regulates TRPV4 activation by
CC hypotonicity (PubMed:16571723). {ECO:0000250|UniProtKB:P55064,
CC ECO:0000269|PubMed:16571723}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:10400615, ECO:0000269|PubMed:12042359,
CC ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:18027168,
CC ECO:0000269|PubMed:23473857}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55064}. Cell membrane
CC {ECO:0000250|UniProtKB:P55064}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55064}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:23473857}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P55064}. Note=Hypotonicity increases location at
CC the cell membrane. Phosphorylation decreases location at the cell
CC membrane. {ECO:0000250|UniProtKB:P55064}.
CC -!- TISSUE SPECIFICITY: Detected at the luminal membrane of secretory
CC epithelial cells in hindpaw sweat glands (PubMed:12042359,
CC PubMed:23473857). Detected in acinar cells in salivary glands, in duct
CC cells in lacrimal glands and in lung (at protein level)
CC (PubMed:10337625, PubMed:10400615, PubMed:10619865, PubMed:16571723,
CC PubMed:18027168). Detected in lung, parotid, submandibular, sublingual,
CC and lacrimal gland tissues (PubMed:10337625).
CC {ECO:0000269|PubMed:10337625, ECO:0000269|PubMed:10400615,
CC ECO:0000269|PubMed:10619865, ECO:0000269|PubMed:12042359,
CC ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:18027168,
CC ECO:0000269|PubMed:23473857}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA). {ECO:0000250|UniProtKB:P55064}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mice are born at less than the
CC expected Mendelian rate, indicative of embryonic lethality
CC (PubMed:10400615, PubMed:10619865). After weaning, mice display
CC decreased pilocarbine-induced saliva secretion, and their saliva
CC displays increased osmolality and viscosity (PubMed:10400615,
CC PubMed:18027168). Mice display reduced Ca2+ entry and loss of
CC regulatory volume decrease in response to hypotonicity in acinar cells.
CC HTS-stimulated Ca2+ entry is significantly decreased in submandibular
CC gland acini and almost completely abolished in parotid acini
CC (PubMed:16571723). Lung airspace-capillary osmotic water permeability
CC is strongly decreased. In contrast, there is no change in alveolar
CC fluid clearance (PubMed:10619865). Paws of mutant mice display normal
CC sweat secretion (PubMed:12042359). Tear secretion is not changed in
CC mutant mice (PubMed:18027168). {ECO:0000269|PubMed:10400615,
CC ECO:0000269|PubMed:10619865, ECO:0000269|PubMed:12042359,
CC ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:18027168}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AF087654; AAD32491.1; -; mRNA.
DR EMBL; AK009302; BAB26203.1; -; mRNA.
DR CCDS; CCDS27823.1; -.
DR RefSeq; NP_033831.1; NM_009701.4.
DR AlphaFoldDB; Q9WTY4; -.
DR SMR; Q9WTY4; -.
DR STRING; 10090.ENSMUSP00000127611; -.
DR GlyGen; Q9WTY4; 1 site.
DR iPTMnet; Q9WTY4; -.
DR PhosphoSitePlus; Q9WTY4; -.
DR MaxQB; Q9WTY4; -.
DR PaxDb; Q9WTY4; -.
DR PRIDE; Q9WTY4; -.
DR ProteomicsDB; 273913; -.
DR ABCD; Q9WTY4; 1 sequenced antibody.
DR Antibodypedia; 26098; 326 antibodies from 33 providers.
DR DNASU; 11830; -.
DR Ensembl; ENSMUST00000088200; ENSMUSP00000085530; ENSMUSG00000044217.
DR Ensembl; ENSMUST00000169082; ENSMUSP00000127611; ENSMUSG00000044217.
DR GeneID; 11830; -.
DR KEGG; mmu:11830; -.
DR UCSC; uc007xpt.1; mouse.
DR CTD; 362; -.
DR MGI; MGI:106215; Aqp5.
DR VEuPathDB; HostDB:ENSMUSG00000044217; -.
DR eggNOG; KOG0223; Eukaryota.
DR GeneTree; ENSGT00940000161557; -.
DR HOGENOM; CLU_020019_3_3_1; -.
DR InParanoid; Q9WTY4; -.
DR OMA; KKEVCSA; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q9WTY4; -.
DR TreeFam; TF312940; -.
DR Reactome; R-MMU-432047; Passive transport by Aquaporins.
DR BioGRID-ORCS; 11830; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Aqp5; mouse.
DR PRO; PR:Q9WTY4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9WTY4; protein.
DR Bgee; ENSMUSG00000044217; Expressed in submandibular gland and 76 other tissues.
DR ExpressionAtlas; Q9WTY4; baseline and differential.
DR Genevisible; Q9WTY4; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0015670; P:carbon dioxide transport; ISO:MGI.
DR GO; GO:0071476; P:cellular hypotonic response; ISS:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0030157; P:pancreatic juice secretion; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0046541; P:saliva secretion; IMP:MGI.
DR GO; GO:0006833; P:water transport; IMP:MGI.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR023276; Aquaporin_5.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR PANTHER; PTHR19139:SF38; PTHR19139:SF38; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02017; AQUAPORIN5.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..265
FT /note="Aquaporin-5"
FT /id="PRO_0000063952"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 34..39
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 61..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 66..74
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 75..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 109..126
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 148..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 180
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 181..191
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 192..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT TOPO_DOM 225..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 69..71
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT MOTIF 185..187
FT /note="NPA 2"
FT /evidence="ECO:0000250|UniProtKB:P55064"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 265 AA; 28274 MW; 917DF4A0C0A4C620 CRC64;
MKKEVCSVAF FKAVFAEFLA TLIFVFFGLG SALKWPSALP TILQISIAFG LAIGTLAQAL
GPVSGGHINP AITLALLIGN QISLLRAIFY VAAQLVGAIA GAGILYWLAP GNARGNLAVN
ALSNNTTPGK AVVVELILTF QLALCIFSST DSRRTSPVGS PALSIGLSVT LGHLVGIYFT
GCSMNPARSF GPAVVMNRFS PSHWVFWVGP IVGAVLAAIL YFYLLFPSSL SLHDRVAVVK
GTYEPEEDWE DHREERKKTI ELTAH
