ID AQP3_RAT Reviewed; 292 AA. AC P47862; A0JPL5; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 02-SEP-2026, entry version 147. DE RecName: Full=Aquaporin-3 {ECO:0000305|PubMed:7517548}; DE Short=AQP-3; DE AltName: Full=31.4 kDa water channel protein; DE AltName: Full=Aquaglyceroporin-3; GN Name=Aqp3 {ECO:0000312|RGD:68428}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; TISSUE=Kidney; RX PubMed=7526388; DOI=10.1073/pnas.91.23.10997; RA Echevarria M., Windhager E.E., Tate S.S., Frindt G.; RT "Cloning and expression of AQP3, a water channel from the medullary RT collecting duct of rat kidney."; RL Proc. Natl. Acad. Sci. U.S.A. 91:10997-11001(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-292, FUNCTION, TRANSPORTER ACTIVITY, RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND TISSUE SPECIFICITY. RC TISSUE=Kidney; RX PubMed=7517548; DOI=10.1073/pnas.91.14.6269; RA Ishibashi K., Sasaki S., Fushimi K., Uchida S., Kuwahara M., Saito H., RA Furukawa T., Nakajima K., Yamaguchi Y., Gojobori T., Marumo F.; RT "Molecular cloning and expression of a member of the aquaporin family with RT permeability to glycerol and urea in addition to water expressed at the RT basolateral membrane of kidney collecting duct cells."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6269-6273(1994). CC -!- FUNCTION: Aquaglyceroporins form homotetrameric transmembrane channels, CC with each monomer independently mediating glycerol and water transport CC across the plasma membrane along their osmotic gradient CC (PubMed:7517548, PubMed:7526388). Could also be permeable to urea CC (PubMed:7517548, PubMed:7526388). Also participates in cell CC permeability to H2O2 and H2O2-mediated signaling (By similarity). In CC skin, transports glycerol to the epidermis and stratum corneum, where CC it maintains hydration, elasticity, and supports lipid biosynthesis for CC barrier repair. In kidney, contributes to the reabsorption of water, CC helping the body maintain proper fluid balance (By similarity). CC {ECO:0000250|UniProtKB:Q8R2N1, ECO:0000250|UniProtKB:Q92482, CC ECO:0000269|PubMed:7517548, ECO:0000269|PubMed:7526388}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675, CC ChEBI:CHEBI:17754; Evidence={ECO:0000269|PubMed:7517548}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377; CC Evidence={ECO:0000269|PubMed:7517548, ECO:0000269|PubMed:7526388}; CC -!- CATALYTIC ACTIVITY: CC Reaction=urea(in) = urea(out); Xref=Rhea:RHEA:32799, ChEBI:CHEBI:16199; CC Evidence={ECO:0000269|PubMed:7517548, ECO:0000269|PubMed:7526388}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O2(out) = H2O2(in); Xref=Rhea:RHEA:74375, ChEBI:CHEBI:16240; CC Evidence={ECO:0000250|UniProtKB:Q92482}; CC -!- ACTIVITY REGULATION: Channel activity is inhibited by mercury ions. CC {ECO:0000269|PubMed:7517548}. CC -!- SUBUNIT: Homotetramer; each monomer provides an independent CC glycerol/water pore (By similarity). Could also exist in other CC oligomeric states (By similarity). {ECO:0000250|UniProtKB:O14520, CC ECO:0000250|UniProtKB:Q92482}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7517548, CC ECO:0000269|PubMed:7526388}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:O14520}. Basolateral cell membrane CC {ECO:0000269|PubMed:7517548}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:O14520}. CC -!- TISSUE SPECIFICITY: Detected in kidney medulla and papilla, in CC collecting duct cells (PubMed:7517548, PubMed:7526388). Detected in CC colon (PubMed:7517548). {ECO:0000269|PubMed:7517548, CC ECO:0000269|PubMed:7526388}. 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:O14520}. CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA04559.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L35108; AAA53652.1; -; mRNA. DR EMBL; BC127490; AAI27491.1; -; mRNA. DR EMBL; D17695; BAA04559.1; ALT_INIT; mRNA. DR PIR; I59266; I59266. DR RefSeq; NP_113891.2; NM_031703.2. DR PDB; 8Y8N; EM; 3.12 A; A=1-292. DR PDB; 8Y8O; EM; 2.94 A; A=1-292. DR PDB; 8Y8P; EM; 2.90 A; A=1-292. DR PDB; 8Y8Q; EM; 2.67 A; A=1-292. DR PDB; 8Y8R; EM; 3.39 A; A=1-292. DR PDB; 8Y8S; EM; 3.03 A; A/B/C/D=1-292. DR AlphaFoldDB; P47862; -. DR EMDB; EMD-39052; -. DR EMDB; EMD-39053; -. DR EMDB; EMD-39054; -. DR EMDB; EMD-39055; -. DR EMDB; EMD-39056; -. DR EMDB; EMD-39057; -. DR SMR; P47862; -. DR FunCoup; P47862; 97. DR STRING; 10116.ENSRNOP00000013803; -. DR TCDB; 1.A.8.9.1; the major intrinsic protein (mip) family. DR GlyCosmos; P47862; 1 site, No reported glycans. DR GlyGen; P47862; 1 site. DR PhosphoSitePlus; P47862; -. DR PaxDb; 10116-ENSRNOP00000013803; -. DR Ensembl; ENSRNOT00055028604; ENSRNOP00055023042; ENSRNOG00055016831. DR Ensembl; ENSRNOT00060006225; ENSRNOP00060004631; ENSRNOG00060003749. DR Ensembl; ENSRNOT00065006920; ENSRNOP00065004733; ENSRNOG00065004787. DR GeneID; 65133; -. DR KEGG; rno:65133; -. DR UCSC; RGD:68428; rat. DR AGR; RGD:68428; -. DR CTD; 360; -. DR RGD; 68428; Aqp3. DR eggNOG; KOG0224; Eukaryota. DR InParanoid; P47862; -. DR OrthoDB; 3222at2759; -. DR PhylomeDB; P47862; -. DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-RNO-432047; Passive transport by Aquaporins. DR PRO; PR:P47862; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0015254; F:glycerol channel activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0015166; F:polyol transmembrane transporter activity; IDA:UniProtKB. 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; ISO:RGD. DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB. DR GO; GO:0042476; P:odontogenesis; ISO:RGD. DR GO; GO:0015791; P:polyol transmembrane transport; IDA:UniProtKB. DR GO; GO:0002684; P:positive regulation of immune system process; ISO:RGD. DR GO; GO:0070295; P:renal water absorption; ISO:RGD. DR GO; GO:0002931; P:response to ischemia; ISO:RGD. DR GO; GO:0032526; P:response to retinoic acid; ISO:RGD. DR GO; GO:0015840; P:urea transport; ISO:RGD. DR GO; GO:0006833; P:water transport; IDA:UniProtKB. DR CDD; cd00333; MIP; 1. DR FunFam; 1.20.1080.10:FF:000005; Aquaporin 3; 1. DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1. DR InterPro; IPR023271; Aquaporin-like. DR InterPro; IPR023275; Aquaporin_3. DR InterPro; IPR000425; MIP. DR InterPro; IPR050363; MIP/Aquaporin. DR InterPro; IPR022357; MIP_CS. DR NCBIfam; TIGR00861; MIP; 1. DR PANTHER; PTHR43829; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 1. DR PANTHER; PTHR43829:SF7; AQUAPORIN-3; 1. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR02015; AQUAPORIN3. DR PRINTS; PR00783; MINTRINSICP. DR SUPFAM; SSF81338; Aquaporin-like; 1. DR PROSITE; PS00221; MIP; 1. DR PDBsum; 8Y8N; -. DR PDBsum; 8Y8O; -. DR PDBsum; 8Y8P; -. DR PDBsum; 8Y8Q; -. DR PDBsum; 8Y8R; -. DR PDBsum; 8Y8S; -. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Glycoprotein; Membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..292 FT /note="Aquaporin-3" FT /id="PRO_0000063945" FT TOPO_DOM 1..24 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TRANSMEM 25..42 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TOPO_DOM 43..56 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TRANSMEM 57..74 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TOPO_DOM 75..78 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O14520" FT INTRAMEM 79..92 FT /note="Discontinuously helical" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TOPO_DOM 93..100 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TRANSMEM 101..121 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TOPO_DOM 122..159 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TRANSMEM 160..177 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TOPO_DOM 178..189 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TRANSMEM 190..206 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TOPO_DOM 207..210 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:O14520" FT INTRAMEM 211..224 FT /note="Discontinuously helical" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TOPO_DOM 225..242 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TRANSMEM 243..264 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:O14520" FT TOPO_DOM 265..292 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:O14520" FT MOTIF 83..85 FT /note="NPA 1" FT /evidence="ECO:0000250|UniProtKB:O14520" FT MOTIF 215..217 FT /note="NPA 2" FT /evidence="ECO:0000250|UniProtKB:O14520" FT SITE 63 FT /note="Selectivity filter" FT /evidence="ECO:0000250|UniProtKB:O14520" FT SITE 212 FT /note="Selectivity filter" FT /evidence="ECO:0000250|UniProtKB:O14520" FT SITE 218 FT /note="Selectivity filter" FT /evidence="ECO:0000250|UniProtKB:O14520" FT CARBOHYD 141 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 273 FT /note="P -> L (in Ref. 2; AAI27491)" FT /evidence="ECO:0000305" FT HELIX 5..15 FT /evidence="ECO:0007829|PDB:8Y8N" FT HELIX 20..48 FT /evidence="ECO:0007829|PDB:8Y8Q" FT TURN 49..52 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 56..78 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 84..92 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 100..122 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 124..128 FT /evidence="ECO:0007829|PDB:8Y8Q" FT TURN 129..131 FT /evidence="ECO:0007829|PDB:8Y8Q" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:8Y8Q" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 157..178 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 184..187 FT /evidence="ECO:0007829|PDB:8Y8O" FT HELIX 190..205 FT /evidence="ECO:0007829|PDB:8Y8Q" FT STRAND 206..209 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 216..226 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 227..231 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 234..241 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 245..264 FT /evidence="ECO:0007829|PDB:8Y8Q" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:8Y8Q" SQ SEQUENCE 292 AA; 31384 MW; 41D9D3119DBA55AD CRC64; MGRQKELMNR CGEMLHIRYR LLRQALAECL GTLILVMFGC GSVAQVVLSR GTHGGFLTIN LAFGFAVTLA ILVAGQVSGA HLNPAVTFAM CFLAREPWIK LPIYTLAQTL GAFLGAGIVF GLYYDAIWAF AGNELVVSGP NGTAGIFATY PSGHLDMVNG FFDQFIGTAA LIVCVLAIVD PYNNPVPRGL EAFTVGLVVL VIGTSMGFNS GYAVNPARDF GPRLFTALAG WGSEVFTTGQ NWWWVPIVSP LLGSIGGVFV YQLMIGCHLE QPPPSTEAEN VKLAHMKHKE QI //