FPS1_YEAST
ID FPS1_YEAST Reviewed; 669 AA.
AC P23900; D6VXW3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Glycerol uptake/efflux facilitator protein;
GN Name=FPS1; OrderedLocusNames=YLL043W;
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 [GENOMIC DNA].
RX PubMed=1648479;
RA van Aelst L., Hohmann S., Zimmermann F.K., Jans A.W.H., Thevelein J.M.;
RT "A yeast homologue of the bovine lens fibre MIP gene family complements the
RT growth defect of a Saccharomyces cerevisiae mutant on fermentable sugars
RT but not its defect in glucose-induced RAS-mediated cAMP signalling.";
RL EMBO J. 10:2095-2104(1991).
RN [2]
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 [3]
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 [4]
RP CHARACTERIZATION.
RX PubMed=7729414; DOI=10.1002/j.1460-2075.1995.tb07122.x;
RA Luyten K., Albertyn J., Skibbe W.F., Prior B.A., Ramos J., Thevelein J.M.,
RA Hohmann S.;
RT "Fps1, a yeast member of the MIP family of channel proteins, is a
RT facilitator for glycerol uptake and efflux and is inactive under osmotic
RT stress.";
RL EMBO J. 14:1360-1371(1995).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; THR-168 AND SER-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Channel protein for glycerol. Has a role in both glycerol
CC influx and efflux. Plays a role in osmoregulation: under osmotic stress
CC the channel is apparently closed to allow accumulation of glycerol in
CC the cell under hyperosmotic conditions.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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/Leu-Ala/Ser (NPA).
CC -!- MISCELLANEOUS: Present with 907 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; X54157; CAA38096.1; -; Genomic_DNA.
DR EMBL; Z73148; CAA97494.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09279.1; -; Genomic_DNA.
DR PIR; S64795; S64795.
DR RefSeq; NP_013057.1; NM_001181863.1.
DR AlphaFoldDB; P23900; -.
DR SMR; P23900; -.
DR BioGRID; 31270; 374.
DR DIP; DIP-3979N; -.
DR IntAct; P23900; 7.
DR MINT; P23900; -.
DR STRING; 4932.YLL043W; -.
DR TCDB; 1.A.8.5.1; the major intrinsic protein (mip) family.
DR iPTMnet; P23900; -.
DR MaxQB; P23900; -.
DR PaxDb; P23900; -.
DR PRIDE; P23900; -.
DR EnsemblFungi; YLL043W_mRNA; YLL043W; YLL043W.
DR GeneID; 850683; -.
DR KEGG; sce:YLL043W; -.
DR SGD; S000003966; FPS1.
DR VEuPathDB; FungiDB:YLL043W; -.
DR eggNOG; KOG0224; Eukaryota.
DR GeneTree; ENSGT00940000176604; -.
DR HOGENOM; CLU_027014_0_0_1; -.
DR InParanoid; P23900; -.
DR OMA; MGTMVMI; -.
DR BioCyc; MetaCyc:G3O-32144-MON; -.
DR BioCyc; YEAST:G3O-32144-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:P23900; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P23900; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015254; F:glycerol channel activity; IMP:SGD.
DR GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR GO; GO:0006846; P:acetate transport; IMP:SGD.
DR GO; GO:0015700; P:arsenite transport; IMP:SGD.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:SGD.
DR GO; GO:0015791; P:polyol 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 Glycerol metabolism; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..669
FT /note="Glycerol uptake/efflux facilitator protein"
FT /id="PRO_0000064098"
FT TOPO_DOM 1..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..369
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..506
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 352..354
FT /note="NPA 1"
FT MOTIF 480..482
FT /note="NPA 2"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 168
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 640
FT /note="A -> R (in Ref. 1; CAA38096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 73877 MW; BA9C78056A1251B9 CRC64;
MSNPQKALND FLSSESVHTH DSSRKQSNKQ SSDEGRSSSQ PSHHHSGGTN NNNNNNNNNN
NSNNNNNGND GGNDDDYDYE MQDYRPSPQS ARPTPTYVPQ YSVESGTAFP IQEVIPSAYI
NTQDINHKDN GPPSASSNRA FRPRGQTTVS ANVLNIEDFY KNADDAHTIP ESHLSRRRSR
SRATSNAGHS ANTGATNGRT TGAQTNMESN ESPRNVPIMV KPKTLYQNPQ TPTVLPSTYH
PINKWSSVKN TYLKEFLAEF MGTMVMIIFG SAVVCQVNVA GKIQQDNFNV ALDNLNVTGS
SAETIDAMKS LTSLVSSVAG GTFDDVALGW AAAVVMGYFC AGGSAISGAH LNPSITLANL
VYRGFPLKKV PYYFAGQLIG AFTGALILFI WYKRVLQEAY SDWWMNESVA GMFCVFPKPY
LSSGRQFFSE FLCGAMLQAG TFALTDPYTC LSSDVFPLMM FILIFIINAS MAYQTGTAMN
LARDLGPRLA LYAVGFDHKM LWVHHHHFFW VPMVGPFIGA LMGGLVYDVC IYQGHESPVN
WSLPVYKEMI MRAWFRRPGW KKRNRARRTS DLSDFSYNND DDEEFGERMA LQKTKTKSSI
SDNENEAGEK KVQFKSVQRG KRTFGGIPTI LEEEDSIETA SLGATTTDSI GLSDTSSEDS
HYGNAKKVT
