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AQP8_NOTAL
ID   AQP8_NOTAL              Reviewed;         261 AA.
AC   Q5I4F8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Aquaporin-8;
DE            Short=AQP-8;
GN   Name=AQP8;
OS   Notomys alexis (Spinifex hopping mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Notomys.
OX   NCBI_TaxID=184396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bartolo R.C., Donald J.A.;
RT   "Cloning and expression of aquaporin 8 in the Spinifex hopping mouse,
RT   Notomys alexis.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms a water-specific channel; mercury-sensitive. Also
CC       permeable to urea but not to glycerol (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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; AY856057; AAW47639.1; -; mRNA.
DR   AlphaFoldDB; Q5I4F8; -.
DR   SMR; Q5I4F8; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR023277; Aquaporin_8.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR45665; PTHR45665; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR02020; AQUAPORIN8.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..261
FT                   /note="Aquaporin-8"
FT                   /id="PRO_0000257849"
FT   TOPO_DOM        1..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..156
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        205..228
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           92..94
FT                   /note="NPA 1"
FT   MOTIF           210..212
FT                   /note="NPA 2"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   261 AA;  27780 MW;  1F6485E71E14BC6B CRC64;
     MSGETPMCSI DLSEVKAKET RMAGRFRVSW YEQYIQPCVV ELLGSALFIF IGCLSVIENS
     PDTGLLQPAL AHGLALGLII ATLGNISGGH FNPAVSLAVT VIGGLKTMLL IPYWISQIFG
     GLIGAALAKV VSPEERFWNA SGAAFAIVQE QEQVTEALGV EIILTILLVL AVCMGAVNEK
     TMGPLAPFSI GFSVIVDILA GGGISGACMN PARAFGPAVV AGYWDFHWIY WLGPLLAGLF
     VGLLIRLFIG DEKTRLILKS R
 
 
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