AQY3_YEAST
ID AQY3_YEAST Reviewed; 646 AA.
AC P43549; D6VTH6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Aquaglycerol porin AQY3 {ECO:0000303|PubMed:12832087};
DE AltName: Full=Aquaporin-3 {ECO:0000303|PubMed:9765289};
GN Name=AQY3 {ECO:0000303|PubMed:9765289}; OrderedLocusNames=YFL054C;
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=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 IDENTIFICATION.
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, AND DISRUPTION PHENOTYPE.
RX PubMed=12832087; DOI=10.1016/s0005-2736(03)00138-x;
RA Oliveira R., Lages F., Silva-Graca M., Lucas C.;
RT "Fps1p channel is the mediator of the major part of glycerol passive
RT diffusion in Saccharomyces cerevisiae: artefacts and re-definitions.";
RL Biochim. Biophys. Acta 1613:57-71(2003).
RN [6]
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Channel protein that mediates glycerol entry under ethanol
CC stimulation (PubMed:12832087). Does not seem to mediate glycerol uptake
CC under standard conditions (PubMed:12832087).
CC {ECO:0000269|PubMed:12832087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675,
CC ChEBI:CHEBI:17754; Evidence={ECO:0000269|PubMed:12832087};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12832087};
CC Multi-pass membrane protein {ECO:0000255}.
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). {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Decreases the gylcerol uptake in presence of
CC ethanol. {ECO:0000269|PubMed:12832087}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D50617; BAA09187.1; -; Genomic_DNA.
DR EMBL; AY692603; AAT92622.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12386.1; -; Genomic_DNA.
DR PIR; S56201; S56201.
DR RefSeq; NP_116601.1; NM_001179913.1.
DR AlphaFoldDB; P43549; -.
DR SMR; P43549; -.
DR BioGRID; 31093; 140.
DR DIP; DIP-4535N; -.
DR IntAct; P43549; 1.
DR MINT; P43549; -.
DR STRING; 4932.YFL054C; -.
DR TCDB; 1.A.8.9.7; the major intrinsic protein (mip) family.
DR iPTMnet; P43549; -.
DR MaxQB; P43549; -.
DR PaxDb; P43549; -.
DR PRIDE; P43549; -.
DR EnsemblFungi; YFL054C_mRNA; YFL054C; YFL054C.
DR GeneID; 850490; -.
DR KEGG; sce:YFL054C; -.
DR SGD; S000001840; AQY3.
DR VEuPathDB; FungiDB:YFL054C; -.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000176604; -.
DR HOGENOM; CLU_020019_2_1_1; -.
DR InParanoid; P43549; -.
DR OMA; YPEDLHP; -.
DR BioCyc; YEAST:G3O-30412-MON; -.
DR Reactome; R-SCE-432030; Transport of glycerol from adipocytes to the liver by Aquaporins.
DR Reactome; R-SCE-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-SCE-432047; Passive transport by Aquaporins.
DR PRO; PR:P43549; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43549; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015254; F:glycerol channel activity; IMP:SGD.
DR GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR GO; GO:0015793; P:glycerol transmembrane transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR GO; GO:0006833; P:water transport; IBA:GO_Central.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
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; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..646
FT /note="Aquaglycerol porin AQY3"
FT /id="PRO_0000064099"
FT TOPO_DOM 1..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..383
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..481
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..569
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 408..410
FT /note="NPA 1"
FT MOTIF 538..540
FT /note="NPA 2"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 70507 MW; C6A4BC452168C1F9 CRC64;
MSYESGRSSS SSESTRPPTL KEEPNGKIAW EESVKKSREN NENDSTLLRR KLGETRKAIE
TGGSSRNKLS ALTPLKKVVD ERKDSVQPQV PSMGFTYSLP NLKTLNSFSD AEQARIMQDY
LSRGVNQGNS NNYVDPLYRQ LNPTMGSSRN RPVWSLNQPL PHVLDRGLAA KMIQKNMDAR
SRASSRRGST DISRGGSTTS VKDWKRLLRG AAPGKKLGDI EAQTQRDNTV GADVKPTKLE
PENPQKPSNT HIENVSRKKK RTSHNVNFSL GDESYASSIA DAESRKLKNM QTLDGSTPVY
TKLPEELIEE ENKSTSALDG NEIGASEDED ADIMTFPNFW AKIRYHMREP FAEFLGTLVL
VIFGVGGNLQ ATVTKGSGGS YESLSFAWGF GCMLGVYVAG GISGGHINPA VTISMAIFRK
FPWKKVPVYI VAQIIGAYFG GAMAYGYFWS SITEFEGGPH IRTTATGACL FTDPKSYVTW
RNAFFDEFIG ASILVGCLMA LLDDSNAPPG NGMTALIIGF LVAAIGMALG YQTSFTINPA
RDLGPRIFAS MIGYGPHAFH LTHWWWTWGA WGGPIAGGIA GALIYDIFIF TGCESPVNYP
DNGYIENRVG KLLHAEFHQN DGTVSDESGV NSNSNTGSKK SVPTSS
