AQY1_YEAST
ID AQY1_YEAST Reviewed; 305 AA.
AC P0CD91; D6W4J2; O74680; P53386;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Aquaporin-1;
GN Name=AQY1; Synonyms=AQY1-2; OrderedLocusNames=YPR192W; ORFNames=P9677.5;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF MET-121 AND THR-255.
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 [5]
RP FUNCTION.
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 [6]
RP FUNCTION.
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 [7]
RP TOPOLOGY.
RX PubMed=12524434; DOI=10.1074/jbc.m300163200;
RA Kim H., Melen K., von Heijne G.;
RT "Topology models for 37 Saccharomyces cerevisiae membrane proteins based on
RT C-terminal reporter fusions and predictions.";
RL J. Biol. Chem. 278:10208-10213(2003).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across membranes. Involved in sporulation, freeze tolerance and
CC osmotolerance (By similarity). Is non-functional in most laboratory
CC strains. {ECO:0000250, ECO:0000269|PubMed:10092523,
CC ECO:0000269|PubMed:10870101, ECO:0000269|PubMed:9765289}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass
CC membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expressed in spores.
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 strain S288c and many other laboratory strains, a
CC natural frameshift in position 294 results in a shortened C-terminus
CC when compared to wild-type alleles. It is however not the different C-
CC terminus, but rather 2 polymorphisms at positions 121 and 255 that lead
CC to loss of water transport activity.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; U25841; AAB64621.1; -; Genomic_DNA.
DR EMBL; AY558066; AAS56392.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11608.1; -; Genomic_DNA.
DR PIR; S58822; S58822.
DR RefSeq; NP_015518.1; NM_001184289.1.
DR AlphaFoldDB; P0CD91; -.
DR SMR; P0CD91; -.
DR BioGRID; 36364; 36.
DR STRING; 4932.YPR192W; -.
DR PaxDb; P0CD91; -.
DR PRIDE; P0CD91; -.
DR DNASU; 856322; -.
DR EnsemblFungi; YPR192W_mRNA; YPR192W; YPR192W.
DR GeneID; 856322; -.
DR KEGG; sce:YPR192W; -.
DR SGD; S000006396; AQY1.
DR VEuPathDB; FungiDB:YPR192W; -.
DR eggNOG; KOG0223; Eukaryota.
DR GeneTree; ENSGT00940000176123; -.
DR HOGENOM; CLU_020019_1_4_1; -.
DR InParanoid; P0CD91; -.
DR OMA; WTPGPLH; -.
DR BioCyc; YEAST:G3O-34314-MON; -.
DR PRO; PR:P0CD91; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P0CD91; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
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; IDA:SGD.
DR GO; GO:0015250; F:water channel activity; IMP:SGD.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IDA:SGD.
DR GO; GO:0006833; P:water transport; IMP:SGD.
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 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..305
FT /note="Aquaporin-1"
FT /id="PRO_0000064076"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..305
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"
FT MUTAGEN 121
FT /note="M->V: Restores water permeability; when associated
FT with P-255."
FT /evidence="ECO:0000269|PubMed:9765289"
FT MUTAGEN 255
FT /note="T->P: Restores water permeability; when associated
FT with V-121."
FT /evidence="ECO:0000269|PubMed:9765289"
SQ SEQUENCE 305 AA; 32713 MW; 2C02491CF93ADC7F CRC64;
MSSNDSNDTD KQHTRLDPTG VDDAYIPPEQ PETKHHRFKI SRDTLRDHFI AAVGEFCGTF
MFLWCAYVIC NVANHDVALV AAPDGSHPGQ LIMIAIGFGF SVMFSIWCFA GVSGGALNPA
MSLSLCLARA VSPTRCVVMW VSQIVAGMAA GGAASAMTPG EVLFANSLGL GCSRTRGLFL
EMFGTAILCL TVLMTAVEKR ETNFMAALPI GISLFIAHVA LTAYTGTGVN PARSLGAAVA
ARYFPHYHWI YWIGTLLGSI LAWSVWQLLQ ILDYTTYVTA EKAASTKEKA QKKGETSSSS
AVAEV
