ID   AQY22_YEAS8             Reviewed;         149 AA.
AC   C8ZCS3;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Aquaporin-like protein 2;
DE   AltName: Full=Truncated aquaporin-2;
GN   Name=AQY2-2; ORFNames=EC1118_1L10_0111g;
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 freeze tolerance, osmotolerance and cell
CC       flocculation in liquid cultures. Is non-functional in most laboratory
CC       strains (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass
CC       membrane protein.
CC   -!- INDUCTION: During exponential phase in rich medium and repressed in
CC       minimum medium, hyper-osmolar medium or in sporulating conditions.
CC       {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}.
CC   -!- CAUTION: This is a truncated version of aquaporin-2. A natural 11 bp
CC       deletion in position 109 leads to a frameshift, which disrupts the gene
CC       coding for this protein and produces two ORFs EC1118_1L10_0111g and
CC       EC1118_1L10_0100g. A contiguous sequence for aquaporin-2 can be found
CC       in strain Sigma 1278B (AC P0CD89). {ECO:0000305}.
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DR   EMBL; FN393078; CAY81189.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8ZCS3; -.
DR   SMR; C8ZCS3; -.
DR   EnsemblFungi; CAY81189; CAY81189; EC1118_1L10_0111g.
DR   HOGENOM; CLU_1750738_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome XII, Scaffold EC1118_1L10.
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   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   PANTHER; PTHR19139; PTHR19139; 1.
DR   SUPFAM; SSF81338; SSF81338; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Endoplasmic reticulum; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..149
FT                   /note="Aquaporin-like protein 2"
FT                   /id="PRO_0000391655"
FT   TOPO_DOM        1..47
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..89
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   149 AA;  16966 MW;  3FA77ED152CBBA91 CRC64;
     MSNESNDLEK NISHLDPTGV DNAYIPPEQP ETKHSRFNID RGTLRNHFIA AVGEFCGTFM
     FLWCAYVICN VANHDVALTT EPEGSHPGQL IMIALGFGFS VMFSIWCFWW GFEPSRFSLF
     VFGQSHLTSQ MCSDVVSSDH CWDGCWWCR