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