ID   AQP6_RAT                Reviewed;         276 AA.
AC   Q9WTY0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Aquaporin-6;
DE            Short=AQP-6;
GN   Name=Aqp6;
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], AND CHARACTERIZATION.
RX   PubMed=10318966; DOI=10.1073/pnas.96.10.5808;
RA   Yasui M., Kwon T.H., Knepper M.A., Nielsen S., Agre P.;
RT   "Aquaporin-6: an intracellular vesicle water channel protein in renal
RT   epithelia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:5808-5813(1999).
CC   -!- FUNCTION: Forms a water-specific channel that participates in distinct
CC       physiological functions such as glomerular filtration, tubular
CC       endocytosis and acid-base metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Kidney.
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).
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000305}.
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DR   EMBL; AF083879; AAD29856.1; -; mRNA.
DR   RefSeq; NP_071517.1; NM_022181.1.
DR   AlphaFoldDB; Q9WTY0; -.
DR   SMR; Q9WTY0; -.
DR   STRING; 10116.ENSRNOP00000000323; -.
DR   GlyGen; Q9WTY0; 1 site.
DR   PaxDb; Q9WTY0; -.
DR   Ensembl; ENSRNOT00000098480; ENSRNOP00000092300; ENSRNOG00000063448.
DR   GeneID; 29170; -.
DR   KEGG; rno:29170; -.
DR   UCSC; RGD:71100; rat.
DR   CTD; 363; -.
DR   RGD; 71100; Aqp6.
DR   VEuPathDB; HostDB:ENSRNOG00000053181; -.
DR   eggNOG; KOG0223; Eukaryota.
DR   GeneTree; ENSGT00940000161949; -.
DR   HOGENOM; CLU_020019_3_3_1; -.
DR   InParanoid; Q9WTY0; -.
DR   OMA; MAIQVTW; -.
DR   OrthoDB; 1152704at2759; -.
DR   PhylomeDB; Q9WTY0; -.
DR   TreeFam; TF312940; -.
DR   PRO; PR:Q9WTY0; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000053181; Expressed in kidney and 2 other tissues.
DR   Genevisible; Q9WTY0; RN.
DR   GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0005253; F:anion channel activity; TAS:Reactome.
DR   GO; GO:0015112; F:nitrate transmembrane transporter activity; IMP:RGD.
DR   GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR   GO; GO:0015670; P:carbon dioxide transport; IBA:GO_Central.
DR   GO; GO:0015706; P:nitrate transmembrane transport; IMP:RGD.
DR   GO; GO:0042476; P:odontogenesis; ISO:RGD.
DR   GO; GO:0003097; P:renal water transport; ISS:UniProtKB.
DR   GO; GO:0006833; P:water transport; IBA:GO_Central.
DR   CDD; cd00333; MIP; 1.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR023254; Aquaporin_6.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR19139; PTHR19139; 1.
DR   PANTHER; PTHR19139:SF113; PTHR19139:SF113; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR02018; AQUAPORIN6.
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   Cytoplasmic vesicle; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..276
FT                   /note="Aquaporin-6"
FT                   /id="PRO_0000063957"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..51
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..96
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..138
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           79..81
FT                   /note="NPA 1"
FT   MOTIF           193..195
FT                   /note="NPA 2"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   276 AA;  28860 MW;  A0B724FF81A4C492 CRC64;
     MEPGLCNRAY LLVGGLWTAI SKALFAEFLA TGLYVFFGVG SVLPWPVALP SVLQVAITFN
     LATATAVQIS WKTSGAHANP AVTLAYLVGS HISLPRAVAY IAAQLAGATV GAALLYGVTP
     GGVRETLGVN VVHNSTSTGQ AVAVELVLTL QLVLCVFASM DSRQTLGSPA AMIGTSVALG
     HLIGIYFTGC SMNPARSFGP AVIVGKFAVH WIFWVGPLTG AVLASLIYNF ILFPDTKTVA
     QRLAILVGTT KVEKVVDLEP QKKESQTNSE DTEVSV