ID   AQY22_YEAS2             Reviewed;         149 AA.
AC   C7GNE3;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Aquaporin-like protein 2;
DE   AltName: Full=Truncated aquaporin-2;
GN   Name=AQY2-2; ORFNames=C1Q_01794;
OS   Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=574961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAY291;
RX   PubMed=19812109; DOI=10.1101/gr.091777.109;
RA   Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA   Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA   Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA   Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA   Pereira G.A.G.;
RT   "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT   bioethanol production.";
RL   Genome Res. 19:2258-2270(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 C1Q_01794 and C1Q_01798.
CC       A contiguous sequence for aquaporin-2 can be found in strain Sigma
CC       1278B (AC P0CD89). {ECO:0000305}.
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DR   EMBL; ACFL01000073; EEU07683.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7GNE3; -.
DR   SMR; C7GNE3; -.
DR   Proteomes; UP000008073; Unassembled WGS sequence.
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_0000391653"
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;  17024 MW;  197E5A42A2F7495E CRC64;
     MSNESNDLEK NISHLDPTGV DNAYIPPEQP ETKHSRFNID RDTLRNHFIA AVGEFCGTFM
     FLWCAYVICN VANHDVALTT EPEGSHPGQL IMIALGFGFS VMFSIWCFWW GFEPSRFSLF
     VFGQSHLTSQ MCSDVVSSDH CWDGCWWCR