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   24-JAN-2024, entry version 154.
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   GlyCosmos; Q9WTY4; 1 site, No reported glycans.
DR   GlyGen; Q9WTY4; 1 site.
DR   iPTMnet; Q9WTY4; -.
DR   PhosphoSitePlus; Q9WTY4; -.
DR   MaxQB; Q9WTY4; -.
DR   PaxDb; 10090-ENSMUSP00000127611; -.
DR   ProteomicsDB; 273913; -.
DR   ABCD; Q9WTY4; 1 sequenced antibody.
DR   Antibodypedia; 26098; 394 antibodies from 33 providers.
DR   DNASU; 11830; -.
DR   Ensembl; ENSMUST00000088200.13; ENSMUSP00000085530.7; ENSMUSG00000044217.18.
DR   Ensembl; ENSMUST00000169082.3; ENSMUSP00000127611.2; ENSMUSG00000044217.18.
DR   GeneID; 11830; -.
DR   KEGG; mmu:11830; -.
DR   UCSC; uc007xpt.1; mouse.
DR   AGR; MGI:106215; -.
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; IYEFFFI; -.
DR   OrthoDB; 3236018at2759; -.
DR   PhylomeDB; Q9WTY4; -.
DR   TreeFam; TF312940; -.
DR   Reactome; R-MMU-432047; Passive transport by Aquaporins.
DR   BioGRID-ORCS; 11830; 2 hits in 78 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 78 other cell types or tissues.
DR   ExpressionAtlas; Q9WTY4; baseline and differential.
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: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; Glycerol uptake facilitator protein; 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   NCBIfam; TIGR00861; MIP; 1.
DR   PANTHER; PTHR19139; AQUAPORIN TRANSPORTER; 1.
DR   PANTHER; PTHR19139:SF38; AQUAPORIN-5; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR02017; AQUAPORIN5.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; Aquaporin-like; 1.
DR   PROSITE; PS00221; MIP; 1.
DR   Genevisible; Q9WTY4; MM.
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
//