ID   AQY1_YEAS8              Reviewed;         327 AA.
AC   C8ZJM1;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Aquaporin-1;
GN   Name=AQY1; ORFNames=EC1118_1P2_5391g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Water channel required to facilitate the transport of water
CC       across membranes. Involved in sporulation, freeze tolerance and
CC       osmotolerance. Is non-functional in most laboratory strains.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Cell membrane; Multi-pass membrane protein.
CC   -!- DEVELOPMENTAL STAGE: Expressed in spores.
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; FN394217; CAY87152.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8ZJM1; -.
DR   SMR; C8ZJM1; -.
DR   EnsemblFungi; CAY87152; CAY87152; EC1118_1P2_5391g.
DR   HOGENOM; CLU_020019_1_7_1; -.
DR   Proteomes; UP000000286; Chromosome XVI, Scaffold EC1118_1P2.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR19139; PTHR19139; 1.
DR   Pfam; PF00230; MIP; 1.
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; Endoplasmic reticulum; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..327
FT                   /note="Aquaporin-1"
FT                   /id="PRO_0000391663"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        49..69
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        92..112
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        137..157
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..176
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        177..197
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..203
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        204..224
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        249..269
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           118..120
FT                   /note="NPA 1"
FT   MOTIF           230..232
FT                   /note="NPA 2"
SQ   SEQUENCE   327 AA;  35343 MW;  8358131AF44EE3B5 CRC64;
     MSSNDSNDTD KQHTRLDPTG VDDAYIPPEQ PETKHHRFKI SKDTLRNHFI AAAGEFCGTF
     MFLWCAYVIC NVANHDVALV AAPDGSHPGQ LIMIAIGFGF SVMFSIWCFA GVSGGALNPA
     VSLSLCLARA VSPTRCVVMW VSQIVAGMAA GGAASAMTPG EVLFANSLGL GCSRTRGLFL
     EMFGTAILCL TVLMTAVEKR ETNFMAALPI GISLFIAHVA LTAYTGTGVN PARSLGAAVA
     ARYFPHYHWI YWIGPLLGSI LAWSVWQLLQ ILDYTTYVTA EKAASTKEKA QKKVKPAVPL
     LWLKSNFSLL FFISRSLALN VIIFGKN