AQP3_RAT
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 03-AUG-2022, entry version 131.
DE RecName: Full=Aquaporin-3;
DE Short=AQP-3;
DE AltName: Full=31.4 kDa water channel protein;
DE AltName: Full=Aquaglyceroporin-3;
GN Name=Aqp3;
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, SUBCELLULAR LOCATION, AND TISSUE
RP 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, SUBCELLULAR LOCATION,
RP 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: Water channel required to promote glycerol permeability and
CC water transport across cell membranes (PubMed:7526388, PubMed:7517548).
CC Acts as a glycerol transporter in skin and plays an important role in
CC regulating SC (stratum corneum) and epidermal glycerol content.
CC Involved in skin hydration, wound healing, and tumorigenesis. Provides
CC kidney medullary collecting duct with high permeability to water,
CC thereby permitting water to move in the direction of an osmotic
CC gradient. Slightly permeable to urea and may function as a water and
CC urea exit mechanism in antidiuresis in collecting duct cells. It may
CC play an important role in gastrointestinal tract water transport and in
CC glycerol metabolism (By similarity). {ECO:0000250|UniProtKB:Q8R2N1,
CC ECO:0000269|PubMed:7517548, ECO:0000269|PubMed:7526388}.
CC -!- ACTIVITY REGULATION: Channel activity is inhibited by mercury ions.
CC {ECO:0000269|PubMed:7517548}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7517548,
CC ECO:0000269|PubMed:7526388}; Multi-pass membrane protein {ECO:0000305}.
CC Basolateral cell membrane {ECO:0000269|PubMed:7517548}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in kidney medulla and papilla, in
CC collecting duct cells (PubMed:7526388, PubMed:7517548). 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:Q96PS8}.
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};
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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_113891.1; NM_031703.1.
DR AlphaFoldDB; P47862; -.
DR SMR; P47862; -.
DR STRING; 10116.ENSRNOP00000013803; -.
DR TCDB; 1.A.8.9.1; the major intrinsic protein (mip) family.
DR GlyGen; P47862; 1 site.
DR PaxDb; P47862; -.
DR GeneID; 65133; -.
DR KEGG; rno:65133; -.
DR UCSC; RGD:68428; rat.
DR CTD; 360; -.
DR RGD; 68428; Aqp3.
DR eggNOG; KOG0224; Eukaryota.
DR InParanoid; P47862; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P47862; -.
DR TreeFam; TF313173; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:0090650; P:cellular response to oxygen-glucose deprivation; 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: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 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 2: Evidence at transcript 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_0000063945"
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 273
FT /note="P -> L (in Ref. 2; AAI27491)"
FT /evidence="ECO:0000305"
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
