AQP3_MOUSE
ID AQP3_MOUSE Reviewed; 292 AA.
AC Q8R2N1; Q3TU75; Q9JJN8; Q9WTJ3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Aquaporin-3;
DE Short=AQP-3;
DE AltName: Full=Aquaglyceroporin-3;
GN Name=Aqp3;
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 [GENOMIC DNA / MRNA], FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=C57BL/6J;
RX PubMed=12771381; DOI=10.1073/pnas.1230416100;
RA Hara M., Verkman A.S.;
RT "Glycerol replacement corrects defective skin hydration, elasticity, and
RT barrier function in aquaporin-3-deficient mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7360-7365(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Extraembryonic tissue, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-292.
RC TISSUE=Kidney;
RX PubMed=10777495; DOI=10.1074/jbc.m001119200;
RA Kishida K., Kuriyama H., Funahashi T., Shimomura I., Kihara S., Ouchi N.,
RA Nishida M., Nishizawa H., Masuda M., Takahashi M., Hotta K., Nakamura T.,
RA Yamashita S., Tochino Y., Matsuzawa Y.;
RT "Aquaporin adipose, a putative glycerol channel in adipocytes.";
RL J. Biol. Chem. 275:20896-20902(2000).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16641094; DOI=10.1073/pnas.0602087103;
RA McDill B.W., Li S.Z., Kovach P.A., Ding L., Chen F.;
RT "Congenital progressive hydronephrosis (cph) is caused by an S256L mutation
RT in aquaporin-2 that affects its phosphorylation and apical membrane
RT accumulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6952-6957(2006).
RN [8]
RP FUNCTION.
RX PubMed=17429015; DOI=10.1095/biolreprod.106.059261;
RA Edashige K., Ohta S., Tanaka M., Kuwano T., Valdez D.M. Jr., Hara T.,
RA Jin B., Takahashi S., Seki S., Koshimoto C., Kasai M.;
RT "The role of aquaporin 3 in the movement of water and cryoprotectants in
RT mouse morulae.";
RL Biol. Reprod. 77:365-375(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Water channel required to promote glycerol permeability and
CC water transport across cell membranes. Acts as a glycerol transporter
CC in skin and plays an important role in regulating SC (stratum corneum)
CC and epidermal glycerol content. Involved in skin hydration, wound
CC healing, and tumorigenesis. Provides kidney medullary collecting duct
CC with high permeability to water, thereby permitting water to move in
CC the direction of an osmotic gradient. Slightly permeable to urea and
CC may function as a water and urea exit mechanism in antidiuresis in
CC collecting duct cells. It may play an important role in
CC gastrointestinal tract water transport and in glycerol metabolism.
CC {ECO:0000269|PubMed:12771381, ECO:0000269|PubMed:17429015}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P47862};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P47862}. Basolateral
CC cell membrane {ECO:0000269|PubMed:16641094}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P47862}.
CC -!- TISSUE SPECIFICITY: Detected in principal cells in collecting ducts in
CC kidney medulla (at protein level) (PubMed:16641094). Renal medulla and
CC colon. Predominantly in the inner medulla. Expressed in basal layer of
CC epidermal keratinocytes. {ECO:0000269|PubMed:16641094}.
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:Q96PS8}.
CC -!- DISRUPTION PHENOTYPE: Mice have dry skin with reduced SC (stratum
CC corneum) hydration, decreased elasticity and impaired biosynthesis. The
CC glycerol content of SC and epidermis is reduced, whereas that of dermis
CC and serum is normal. The dry, relatively inelastic skin is probably
CC related to the humectant properties of glycerol, and the impaired SC
CC repair to impaired epidermal biosynthetic function.
CC {ECO:0000269|PubMed:12771381}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB03270.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF104416; AAD20304.1; -; mRNA.
DR EMBL; AF104417; AAD20305.1; -; Genomic_DNA.
DR EMBL; AK145678; BAE26584.1; -; mRNA.
DR EMBL; AK160929; BAE36096.1; -; mRNA.
DR EMBL; AL837521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466538; EDL05416.1; -; Genomic_DNA.
DR EMBL; BC027400; AAH27400.1; -; mRNA.
DR EMBL; AB019039; BAB03270.1; ALT_INIT; mRNA.
DR CCDS; CCDS38714.1; -.
DR RefSeq; NP_057898.2; NM_016689.2.
DR AlphaFoldDB; Q8R2N1; -.
DR SMR; Q8R2N1; -.
DR BioGRID; 198172; 1.
DR STRING; 10090.ENSMUSP00000055110; -.
DR GlyGen; Q8R2N1; 1 site.
DR PhosphoSitePlus; Q8R2N1; -.
DR PaxDb; Q8R2N1; -.
DR PRIDE; Q8R2N1; -.
DR ProteomicsDB; 273909; -.
DR Antibodypedia; 55184; 358 antibodies from 31 providers.
DR DNASU; 11828; -.
DR Ensembl; ENSMUST00000055327; ENSMUSP00000055110; ENSMUSG00000028435.
DR GeneID; 11828; -.
DR KEGG; mmu:11828; -.
DR UCSC; uc008sih.1; mouse.
DR CTD; 360; -.
DR MGI; MGI:1333777; Aqp3.
DR VEuPathDB; HostDB:ENSMUSG00000028435; -.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000157242; -.
DR HOGENOM; CLU_020019_9_1_1; -.
DR InParanoid; Q8R2N1; -.
DR OMA; GDLPWAS; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q8R2N1; -.
DR TreeFam; TF313173; -.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-MMU-432047; Passive transport by Aquaporins.
DR BioGRID-ORCS; 11828; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Aqp3; mouse.
DR PRO; PR:Q8R2N1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8R2N1; protein.
DR Bgee; ENSMUSG00000028435; Expressed in lip and 130 other tissues.
DR Genevisible; Q8R2N1; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0015254; F:glycerol channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0015166; F:polyol transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0015791; P:polyol transmembrane transport; ISO:MGI.
DR GO; GO:0002684; P:positive regulation of immune system process; ISO:MGI.
DR GO; GO:0070295; P:renal water absorption; IMP:MGI.
DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
DR GO; GO:0015840; P:urea transport; IMP:MGI.
DR GO; GO:0006833; P:water transport; IDA:UniProtKB.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR023275; Aquaporin_3.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02015; AQUAPORIN3.
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; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..292
FT /note="Aquaporin-3"
FT /id="PRO_0000063944"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 48..53
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 75..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 79..92
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 93..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..123
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 124..157
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 179..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT INTRAMEM 209..227
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 228..244
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT TOPO_DOM 266..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 83..85
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT MOTIF 215..217
FT /note="NPA 2"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 170..173
FT /note="ALIV -> PLL (in Ref. 1; AAD20304/AAD20305)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="V -> A (in Ref. 6; BAB03270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 31568 MW; E9A7FFFB43DD98C5 CRC64;
MGRQKELMNR CGEMLHIRYR LLRQALAECL GTLILVMFGC GSVAQVVLSR GTHGGFLTIN
LAFGFAVTLG ILVAGQVSGA HLNPAVTFAM CFLAREPWIK LPIYALAQTL GAFLGAGIVF
GLYYDAIWAF ANNELFVSGP NGTAGIFATY PSGHLDMVNG FFDQFIGTAA LIVCVLAIVD
PYNNPVPRGL EAFTVGLVVL VIGTSMGFNS GYAVNPARDF GPRLFTALAG WGSEVFTTGR
HWWWVPIVSP LLGSIAGVFV YQLMIGCHLE QPPPSTEEEN VKLAHMKHKE QI
