AQY2_YEASX
ID AQY2_YEASX Reviewed; 289 AA.
AC P0CD89; O93938; Q12258; Q12302; Q9C411;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Aquaporin-2;
GN Name=AQY2; Synonyms=AQY2-1;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POLYMORPHISM.
RC STRAIN=Sigma 1278B;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sigma 1278B;
RX PubMed=9765289; DOI=10.1074/jbc.273.42.27565;
RA Bonhivers M., Carbrey J.M., Gould S.J., Agre P.;
RT "Aquaporins in Saccharomyces. Genetic and functional distinctions between
RT laboratory and wild-type strains.";
RL J. Biol. Chem. 273:27565-27572(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-141, AND FUNCTION.
RC STRAIN=ATCC 10604 / CBS 405 / CECT 11837 / NBRC 0258 / NRRL Y-1546;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11168368; DOI=10.1046/j.1432-1033.2001.01882.x;
RA Meyrial V., Laize V., Gobin R., Ripoche P., Hohmann S., Tacnet F.;
RT "Existence of a tightly regulated water channel in Saccharomyces
RT cerevisiae.";
RL Eur. J. Biochem. 268:334-343(2001).
RN [5]
RP FUNCTION.
RX PubMed=12450819; DOI=10.1128/aem.68.12.5981-5989.2002;
RA Tanghe A., Van Dijck P., Dumortier F., Teunissen A., Hohmann S.,
RA Thevelein J.M.;
RT "Aquaporin expression correlates with freeze tolerance in baker's yeast,
RT and overexpression improves freeze tolerance in industrial strains.";
RL Appl. Environ. Microbiol. 68:5981-5989(2002).
RN [6]
RP FUNCTION.
RX PubMed=15184134; DOI=10.1128/aem.70.6.3377-3382.2004;
RA Tanghe A., Van Dijck P., Colavizza D., Thevelein J.M.;
RT "Aquaporin-mediated improvement of freeze tolerance of Saccharomyces
RT cerevisiae is restricted to rapid freezing conditions.";
RL Appl. Environ. Microbiol. 70:3377-3382(2004).
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. {ECO:0000269|PubMed:11158584, ECO:0000269|PubMed:11168368,
CC ECO:0000269|PubMed:12450819, ECO:0000269|PubMed:15184134}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11168368}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11168368}. Cell membrane
CC {ECO:0000269|PubMed:11168368}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11168368}.
CC -!- INDUCTION: During exponential phase in rich medium and repressed in
CC minimum medium, hyper-osmolar medium or in sporulating conditions.
CC {ECO:0000269|PubMed:11168368}.
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 -!- POLYMORPHISM: In many laboratory strains, a natural 11 bp deletion in
CC position 109 leads to a frameshift, which disrupts the gene coding for
CC this protein and produces two ORFs.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AF112860; AAD10058.1; -; Genomic_DNA.
DR EMBL; AF056193; AAD25168.1; -; Genomic_DNA.
DR EMBL; AF321111; AAG53971.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CD89; -.
DR SMR; P0CD89; -.
DR IntAct; P0CD89; 1.
DR MINT; P0CD89; -.
DR TCDB; 1.A.8.6.2; the major intrinsic protein (mip) family.
DR VEuPathDB; FungiDB:YPR192W; -.
DR PhylomeDB; P0CD89; -.
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..289
FT /note="Aquaporin-2"
FT /id="PRO_0000227681"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..90
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..111
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 136..156
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..175
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 176..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..247
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 248..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 117..119
FT /note="NPA 1"
FT MOTIF 229..231
FT /note="NPA 2"
FT VARIANT 141
FT /note="P -> S (in strain: Chevalieri / ATCC 10604)"
FT /evidence="ECO:0000269|PubMed:11158584"
SQ SEQUENCE 289 AA; 31284 MW; 2CA048D683B6D918 CRC64;
MSNESNDLEK NISHLDPTGV DNAYIPPEQP ETKHSRFNID RDTLRNHFIA AVGEFCGTFM
FLWCAYVICN VANHDVALTT EPEGSHPGQL IMIALGFGFS VMFSIWCFAG VSGGALNPAV
SLSLCLARAI SPARCVVMWF PQIIAGMAAG GAASAMTPGK VLFTNALGLG CSRSRGLFLE
MFGTAVLCLT VLMTAVEKRE TNFMAALPIG ISLFMAHMAL TGYTGTGVNP ARSLGAAVAA
RYFPHYHWIY WIGPLLGAFL AWSVWQLLQI LDYTTYVNAE KAAGQKKED
