AQY1_YEASX
ID AQY1_YEASX Reviewed; 327 AA.
AC P0CD92; O74680; P53386;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Aquaporin-1;
GN Name=AQY1; Synonyms=AQY1-1;
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 FUNCTION.
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 [2]
RP FUNCTION.
RC STRAIN=Sigma 1278B;
RX PubMed=10092523; DOI=10.1006/bbrc.1999.0425;
RA Laize V., Gobin R., Rousselet G., Badier C., Hohmann S., Ripoche P.,
RA Tacnet F.;
RT "Molecular and functional study of AQY1 from Saccharomyces cerevisiae: role
RT of the C-terminal domain.";
RL Biochem. Biophys. Res. Commun. 257:139-144(1999).
RN [3]
RP FUNCTION.
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 [4]
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 [5]
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=SK1;
RX PubMed=15583134; DOI=10.1073/pnas.0404337101;
RA Sidoux-Walter F., Pettersson N., Hohmann S.;
RT "The Saccharomyces cerevisiae aquaporin Aqy1 is involved in sporulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17422-17427(2004).
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 {ECO:0000269|PubMed:10092523, ECO:0000269|PubMed:10870101,
CC ECO:0000269|PubMed:12450819, ECO:0000269|PubMed:15184134,
CC ECO:0000269|PubMed:15583134, ECO:0000269|PubMed:9765289}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15583134}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15583134}. Cell membrane
CC {ECO:0000269|PubMed:15583134}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15583134}.
CC -!- DEVELOPMENTAL STAGE: Expressed in spores.
CC {ECO:0000269|PubMed:15583134}.
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; AF053981; AAC69713.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CD92; -.
DR SMR; P0CD92; -.
DR IntAct; P0CD92; 3.
DR MINT; P0CD92; -.
DR VEuPathDB; FungiDB:YPR192W; -.
DR PhylomeDB; P0CD92; -.
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_0000391661"
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; 35409 MW; 22B09817FAC8B3C6 CRC64;
MSSNDSNDTD KQHTRLDPTG VDDAYIPPEQ PETKHHRFKI SRDTLRNHFI AAVGEFCGTF
MFLWCAYVIC NVANHDVALV AAPDGSHPGQ LIMIAIGFGF SVMFSIWCFA GVSGGALNPA
VSLSLCLARA VSPTRCVVMW VSQIVAGMAA GGAASAMTPG EVLFANSLGL GCSRTRGLFL
EMFGTAILCL TVLMTAVEKR ETNFMAALPI GISLFIAHVA LTAYTGTGVN PARSLGAAVA
ARYFPHYHWI YWIGPLLGSI LAWSVWQLLQ ILDYTTYVTA EKAASTKEKA QKKVKPAVPL
LWLKSNFPLL FFISRSLALN VIIFGKN
