AQP3_HUMAN
ID AQP3_HUMAN Reviewed; 292 AA.
AC Q92482; A8K843; B2RE16; D3DRL3; O00108; Q6FGT2; Q6FGW6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Aquaporin-3;
DE Short=AQP-3;
DE AltName: Full=Aquaglyceroporin-3;
GN Name=AQP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=7558005; DOI=10.1006/geno.1995.1055;
RA Ishibashi K., Sasaki S., Saito F., Ikeuchi T., Marumo F.;
RT "Structure and chromosomal localization of a human water channel (AQP3)
RT gene.";
RL Genomics 27:352-354(1995).
RN [2]
RP SEQUENCE REVISION TO 91; 96 AND 186.
RA Ishibashi K.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP GIL BLOOD GROUP SYSTEM.
RC TISSUE=Blood;
RX PubMed=12239222; DOI=10.1074/jbc.m208999200;
RA Roudier N., Ripoche P., Gane P., Le Pennec P.Y., Daniels G., Cartron J.-P.,
RA Bailly P.;
RT "AQP3 deficiency in humans and the molecular basis of a novel blood group
RT system, GIL.";
RL J. Biol. Chem. 277:45854-45859(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Esophagus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-43.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [11]
RP INDUCTION.
RX PubMed=18495115; DOI=10.1016/j.ejphar.2008.03.063;
RA Okahira M., Kubota M., Iguchi K., Usui S., Hirano K.;
RT "Regulation of aquaporin 3 expression by magnesium ion.";
RL Eur. J. Pharmacol. 588:26-32(2008).
RN [12]
RP FUNCTION.
RX PubMed=30420639; DOI=10.1038/s41467-018-07176-z;
RA Gotfryd K., Mosca A.F., Missel J.W., Truelsen S.F., Wang K., Spulber M.,
RA Krabbe S., Helix-Nielsen C., Laforenza U., Soveral G., Pedersen P.A.,
RA Gourdon P.;
RT "Human adipose glycerol flux is regulated by a pH gate in AQP10.";
RL Nat. Commun. 9:4749-4749(2018).
CC -!- FUNCTION: Water channel required to promote glycerol permeability and
CC water transport across cell membranes (PubMed:12239222,
CC PubMed:30420639). Acts as a glycerol transporter in skin and plays an
CC important role in regulating SC (stratum corneum) and epidermal
CC glycerol content. Involved in skin hydration, wound healing, and
CC tumorigenesis. Provides kidney medullary collecting duct with high
CC permeability to water, thereby permitting water to move in the
CC direction of an osmotic gradient. Slightly permeable to urea and may
CC 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 (By
CC similarity). {ECO:0000250|UniProtKB:Q8R2N1,
CC ECO:0000269|PubMed:12239222, ECO:0000269|PubMed:30420639}.
CC -!- INTERACTION:
CC Q92482; Q92482: AQP3; NbExp=3; IntAct=EBI-2808854, EBI-2808854;
CC Q92482; P11912: CD79A; NbExp=3; IntAct=EBI-2808854, EBI-7797864;
CC Q92482; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-2808854, EBI-711490;
CC Q92482; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2808854, EBI-781551;
CC Q92482; P34910-2: EVI2B; NbExp=3; IntAct=EBI-2808854, EBI-17640610;
CC Q92482; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2808854, EBI-18304435;
CC Q92482; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-2808854, EBI-6166686;
CC Q92482; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2808854, EBI-13345167;
CC Q92482; Q8TED1: GPX8; NbExp=3; IntAct=EBI-2808854, EBI-11721746;
CC Q92482; P31937: HIBADH; NbExp=3; IntAct=EBI-2808854, EBI-11427100;
CC Q92482; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-2808854, EBI-17490413;
CC Q92482; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-2808854, EBI-11956541;
CC Q92482; O14880: MGST3; NbExp=3; IntAct=EBI-2808854, EBI-724754;
CC Q92482; Q6IN84: MRM1; NbExp=3; IntAct=EBI-2808854, EBI-5454865;
CC Q92482; P15941-11: MUC1; NbExp=3; IntAct=EBI-2808854, EBI-17263240;
CC Q92482; Q8N912: NRAC; NbExp=3; IntAct=EBI-2808854, EBI-12051377;
CC Q92482; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-2808854, EBI-2804156;
CC Q92482; Q04941: PLP2; NbExp=3; IntAct=EBI-2808854, EBI-608347;
CC Q92482; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-2808854, EBI-3920694;
CC Q92482; O95470: SGPL1; NbExp=3; IntAct=EBI-2808854, EBI-1046170;
CC Q92482; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-2808854, EBI-17280858;
CC Q92482; Q16623: STX1A; NbExp=3; IntAct=EBI-2808854, EBI-712466;
CC Q92482; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-2808854, EBI-12845616;
CC Q92482; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-2808854, EBI-12038591;
CC Q92482; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-2808854, EBI-12015604;
CC Q92482; P01375: TNF; NbExp=3; IntAct=EBI-2808854, EBI-359977;
CC Q92482; Q6EMK4: VASN; NbExp=3; IntAct=EBI-2808854, EBI-10249550;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12239222};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P47862}. Basolateral
CC cell membrane {ECO:0000250|UniProtKB:P47862}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P47862}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92482-1; Sequence=Displayed;
CC Name=2; Synonyms=delta5;
CC IsoId=Q92482-2; Sequence=VSP_003229, VSP_003230;
CC -!- TISSUE SPECIFICITY: Widely expressed in epithelial cells of kidney
CC (collecting ducts) and airways, in keratinocytes, immature dendritic
CC cells and erythrocytes. Isoform 2 is not detectable in erythrocytes at
CC the protein level.
CC -!- INDUCTION: Up-regulated by magnesium. {ECO:0000269|PubMed:18495115}.
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 -!- POLYMORPHISM: AQP3 is responsible for the GIL blood group system.
CC Isoform 2 is detected in GIL-negative individuals that lack functional
CC AQP3.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to a polymorphism at the 5'-splice
CC donor site of intron 5, leading to exon 5 skipping and premature
CC termination of translation. This is the molecular basis of the GIL
CC blood group. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=gil";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/aqp3/";
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DR EMBL; AB001325; BAA19237.1; -; mRNA.
DR EMBL; AJ493597; CAD38526.1; -; mRNA.
DR EMBL; CR541991; CAG46788.1; -; mRNA.
DR EMBL; CR542025; CAG46822.1; -; mRNA.
DR EMBL; BT007199; AAP35863.1; -; mRNA.
DR EMBL; AK292208; BAF84897.1; -; mRNA.
DR EMBL; AK315760; BAG38113.1; -; mRNA.
DR EMBL; DQ083949; AAY68214.1; -; Genomic_DNA.
DR EMBL; AL356218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58500.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58504.1; -; Genomic_DNA.
DR EMBL; BC013566; AAH13566.1; -; mRNA.
DR CCDS; CCDS6542.1; -. [Q92482-1]
DR PIR; A57119; A57119.
DR RefSeq; NP_001305073.1; NM_001318144.1.
DR RefSeq; NP_004916.1; NM_004925.4. [Q92482-1]
DR AlphaFoldDB; Q92482; -.
DR SMR; Q92482; -.
DR BioGRID; 106856; 284.
DR IntAct; Q92482; 27.
DR STRING; 9606.ENSP00000297991; -.
DR DrugBank; DB09020; Bisacodyl.
DR DrugBank; DB11365; Sennosides.
DR GuidetoPHARMACOLOGY; 690; -.
DR GlyGen; Q92482; 1 site.
DR iPTMnet; Q92482; -.
DR PhosphoSitePlus; Q92482; -.
DR BioMuta; AQP3; -.
DR DMDM; 2497938; -.
DR jPOST; Q92482; -.
DR MassIVE; Q92482; -.
DR PaxDb; Q92482; -.
DR PeptideAtlas; Q92482; -.
DR PRIDE; Q92482; -.
DR ProteomicsDB; 75263; -. [Q92482-1]
DR ProteomicsDB; 75264; -. [Q92482-2]
DR Antibodypedia; 55184; 358 antibodies from 31 providers.
DR DNASU; 360; -.
DR Ensembl; ENST00000297991.6; ENSP00000297991.4; ENSG00000165272.16. [Q92482-1]
DR GeneID; 360; -.
DR KEGG; hsa:360; -.
DR MANE-Select; ENST00000297991.6; ENSP00000297991.4; NM_004925.5; NP_004916.1.
DR UCSC; uc003zsx.4; human. [Q92482-1]
DR CTD; 360; -.
DR DisGeNET; 360; -.
DR GeneCards; AQP3; -.
DR HGNC; HGNC:636; AQP3.
DR HPA; ENSG00000165272; Tissue enhanced (esophagus, urinary bladder).
DR MIM; 600170; gene.
DR MIM; 607457; phenotype.
DR neXtProt; NX_Q92482; -.
DR OpenTargets; ENSG00000165272; -.
DR PharmGKB; PA24921; -.
DR VEuPathDB; HostDB:ENSG00000165272; -.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000157242; -.
DR HOGENOM; CLU_020019_9_1_1; -.
DR InParanoid; Q92482; -.
DR OMA; GDLPWAS; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q92482; -.
DR TreeFam; TF313173; -.
DR PathwayCommons; Q92482; -.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-432047; Passive transport by Aquaporins.
DR SignaLink; Q92482; -.
DR SIGNOR; Q92482; -.
DR BioGRID-ORCS; 360; 7 hits in 1079 CRISPR screens.
DR ChiTaRS; AQP3; human.
DR GeneWiki; Aquaporin_3; -.
DR GenomeRNAi; 360; -.
DR Pharos; Q92482; Tchem.
DR PRO; PR:Q92482; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q92482; protein.
DR Bgee; ENSG00000165272; Expressed in nasal cavity epithelium and 188 other tissues.
DR ExpressionAtlas; Q92482; baseline and differential.
DR Genevisible; Q92482; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IC:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015254; F:glycerol channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IEP:UniProtKB.
DR GO; GO:0002684; P:positive regulation of immune system process; IDA:BHF-UCL.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; TAS:BHF-UCL.
DR GO; GO:0070295; P:renal water absorption; IEA:Ensembl.
DR GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
DR GO; GO:0051592; P:response to calcium ion; TAS:BHF-UCL.
DR GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR GO; GO:0033280; P:response to vitamin D; TAS:BHF-UCL.
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 Alternative splicing; Blood group antigen; Cell membrane; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..292
FT /note="Aquaporin-3"
FT /id="PRO_0000063943"
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 VAR_SEQ 165..281
FT /note="FIGTASLIVCVLAIVDPYNNPVPRGLEAFTVGLVVLVIGTSMGFNSGYAVNP
FT ARDFGPRLFTALAGWGSAVFTTGQHWWWVPIVSPLLGSIAGVFVYQLMIGCHLEQPPPS
FT NEEENV -> DRPALVVGAHRVPTPGLHCGCLRVPADDRLPPGAAPTLQRGRECEAGPC
FT EAQGADLSGKGHLPLRCPGLEHPLTVQGHSQEAPLHDPPFQAKELPIYPHPTKTAPSGF
FT PLDLAQIAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12239222"
FT /id="VSP_003229"
FT VAR_SEQ 282..292
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12239222"
FT /id="VSP_003230"
FT VARIANT 43
FT /note="V -> M (in dbSNP:rs34942735)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_025089"
FT CONFLICT 23
FT /note="R -> G (in Ref. 6; BAF84897)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="V -> A (in Ref. 4; CAG46822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 31544 MW; A9555E9576EABA9C CRC64;
MGRQKELVSR CGEMLHIRYR LLRQALAECL GTLILVMFGC GSVAQVVLSR GTHGGFLTIN
LAFGFAVTLG ILIAGQVSGA HLNPAVTFAM CFLAREPWIK LPIYTLAQTL GAFLGAGIVF
GLYYDAIWHF ADNQLFVSGP NGTAGIFATY PSGHLDMING FFDQFIGTAS LIVCVLAIVD
PYNNPVPRGL EAFTVGLVVL VIGTSMGFNS GYAVNPARDF GPRLFTALAG WGSAVFTTGQ
HWWWVPIVSP LLGSIAGVFV YQLMIGCHLE QPPPSNEEEN VKLAHVKHKE QI
