ID   AQY2_YEAST              Reviewed;         149 AA.
AC   P0CD90; D6VXV6; O93938; Q12258; Q12302; Q9C411;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=Aquaporin-like protein 2;
DE   AltName: Full=Truncated aquaporin-2;
GN   Name=AQY2; Synonyms=AQY2-2; OrderedLocusNames=YLL052C; ORFNames=L0590;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   POLYMORPHISM.
RX   PubMed=10870101;
RX   DOI=10.1002/1097-0061(200007)16:10<897::aid-yea583>3.0.co;2-t;
RA   Laize V., Tacnet F., Ripoche P., Hohmann S.;
RT   "Polymorphism of Saccharomyces cerevisiae aquaporins.";
RL   Yeast 16:897-903(2000).
RN   [4]
RP   POLYMORPHISM.
RX   PubMed=11158584; DOI=10.1073/pnas.98.3.1000;
RA   Carbrey J.M., Bonhivers M., Boeke J.D., Agre P.;
RT   "Aquaporins in Saccharomyces: characterization of a second functional water
RT   channel protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:1000-1005(2001).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
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 (By similarity). Is non-functional in
CC       most laboratory strains. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14562095}. Cell membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:14562095}.
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. In strain S288c
CC       and many laboratory strains, a natural 11 bp deletion in position 109
CC       leads to a frameshift, which disrupts the gene coding for this protein
CC       and produces two ORFs YLL052C and YLL053C. A contiguous sequence for
CC       aquaporin-2 can be found in strain Sigma 1278B (AC P0CD89).
CC       {ECO:0000305}.
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DR   EMBL; Z73158; CAA97506.1; -; Genomic_DNA.
DR   EMBL; Z47973; CAA88005.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09272.1; -; Genomic_DNA.
DR   PIR; S50968; S50968.
DR   RefSeq; NP_013048.1; NM_001181872.1.
DR   AlphaFoldDB; P0CD90; -.
DR   SMR; P0CD90; -.
DR   BioGRID; 31263; 13.
DR   STRING; 4932.YLL052C; -.
DR   PaxDb; 4932-YLL052C; -.
DR   EnsemblFungi; YLL052C_mRNA; YLL052C; YLL052C.
DR   GeneID; 850674; -.
DR   KEGG; sce:YLL052C; -.
DR   AGR; SGD:S000003975; -.
DR   SGD; S000003975; AQY2.
DR   VEuPathDB; FungiDB:YLL052C; -.
DR   eggNOG; KOG0223; Eukaryota.
DR   GeneTree; ENSGT00940000176123; -.
DR   HOGENOM; CLU_1750738_0_0_1; -.
DR   InParanoid; P0CD90; -.
DR   OrthoDB; 3236018at2759; -.
DR   BioCyc; YEAST:G3O-32151-MONOMER; -.
DR   BioGRID-ORCS; 850674; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P0CD90; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P0CD90; Protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0015250; F:water channel activity; IDA:SGD.
DR   GO; GO:0055085; P:transmembrane transport; IDA:SGD.
DR   GO; GO:0006833; P:water transport; IDA:SGD.
DR   Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   SUPFAM; SSF81338; Aquaporin-like; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Endoplasmic reticulum; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..149
FT                   /note="Aquaporin-like protein 2"
FT                   /id="PRO_0000391651"
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
//