PHO91_YEAST
ID PHO91_YEAST Reviewed; 894 AA.
AC P27514; D6W1I8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Low-affinity phosphate transporter PHO91;
GN Name=PHO91; OrderedLocusNames=YNR013C; ORFNames=N2052;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7900425; DOI=10.1002/yea.320101013;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Twelve open reading frames revealed in the 23.6 kb segment flanking the
RT centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
RL Yeast 10:1355-1361(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 784-894.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=2169608; DOI=10.1093/nar/18.17.5279;
RA Kern L.;
RT "The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase.";
RL Nucleic Acids Res. 18:5279-5279(1990).
RN [5]
RP FUNCTION.
RX PubMed=11779791; DOI=10.1093/genetics/159.4.1491;
RA Wykoff D.D., O'Shea E.K.;
RT "Phosphate transport and sensing in Saccharomyces cerevisiae.";
RL Genetics 159:1491-1499(2001).
RN [6]
RP INDUCTION.
RX PubMed=12821119; DOI=10.1016/s0006-291x(03)01068-4;
RA Auesukaree C., Homma T., Kaneko Y., Harashima S.;
RT "Transcriptional regulation of phosphate-responsive genes in low-affinity
RT phosphate-transporter-defective mutants in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 306:843-850(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-311, 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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17804816; DOI=10.1091/mbc.e07-05-0457;
RA Hurlimann H.C., Stadler-Waibel M., Werner T.P., Freimoser F.M.;
RT "Pho91 is a vacuolar phosphate transporter that regulates phosphate and
RT polyphosphate metabolism in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 18:4438-4445(2007).
RN [10]
RP UBIQUITINATION BY RSP5.
RX PubMed=18165238; DOI=10.1074/jbc.m703630200;
RA Estrella L.A., Krishnamurthy S., Timme C.R., Hampsey M.;
RT "The Rsp5 E3 ligase mediates turnover of low affinity phosphate
RT transporters in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 283:5327-5334(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-312, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-311 AND SER-312, 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).
RN [13]
RP FUNCTION.
RX PubMed=20133652; DOI=10.1073/pnas.0906546107;
RA Popova Y., Thayumanavan P., Lonati E., Agrochao M., Thevelein J.M.;
RT "Transport and signaling through the phosphate-binding site of the yeast
RT Pho84 phosphate transceptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2890-2895(2010).
CC -!- FUNCTION: Vacuolar phosphate transporter that probably exports
CC phosphate from the vacuolar lumen to the cytosol.
CC {ECO:0000269|PubMed:11779791, ECO:0000269|PubMed:17804816,
CC ECO:0000269|PubMed:20133652}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17804816};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17804816}.
CC -!- INDUCTION: Expression is constitutive and independent of inorganic
CC phosphate concentration and PHO4 activity.
CC {ECO:0000269|PubMed:12821119}.
CC -!- PTM: Ubiquitinated by RSP5. RSP5-mediated ubiquitination initiates
CC internalization and degradation by the endocytic pathway.
CC {ECO:0000269|PubMed:18165238}.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CitM (TC 2.A.11) transporter family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37947.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X77395; CAA54581.1; -; Genomic_DNA.
DR EMBL; Z71628; CAA96290.1; -; Genomic_DNA.
DR EMBL; Z71629; CAA96292.1; -; Genomic_DNA.
DR EMBL; X53998; CAA37947.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006947; DAA10554.1; -; Genomic_DNA.
DR PIR; S45135; S45135.
DR RefSeq; NP_014410.3; NM_001183190.3.
DR AlphaFoldDB; P27514; -.
DR SMR; P27514; -.
DR BioGRID; 35838; 224.
DR DIP; DIP-4264N; -.
DR IntAct; P27514; 9.
DR MINT; P27514; -.
DR STRING; 4932.YNR013C; -.
DR TCDB; 2.A.47.2.2; the divalent anion:na(+) symporter (dass) family.
DR iPTMnet; P27514; -.
DR MaxQB; P27514; -.
DR PaxDb; P27514; -.
DR PRIDE; P27514; -.
DR EnsemblFungi; YNR013C_mRNA; YNR013C; YNR013C.
DR GeneID; 855747; -.
DR KEGG; sce:YNR013C; -.
DR SGD; S000005296; PHO91.
DR VEuPathDB; FungiDB:YNR013C; -.
DR eggNOG; KOG1281; Eukaryota.
DR GeneTree; ENSGT01030000234550; -.
DR HOGENOM; CLU_005170_8_0_1; -.
DR InParanoid; P27514; -.
DR OMA; QLEHIFG; -.
DR BioCyc; YEAST:G3O-33329-MON; -.
DR BRENDA; 7.3.2.1; 984.
DR PRO; PR:P27514; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P27514; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0015169; F:glycerol-3-phosphate transmembrane transporter activity; IMP:SGD.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IMP:SGD.
DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central.
DR GO; GO:0015794; P:glycerol-3-phosphate transmembrane transport; IMP:SGD.
DR GO; GO:0006817; P:phosphate ion transport; IGI:SGD.
DR GO; GO:0006797; P:polyphosphate metabolic process; IMP:SGD.
DR GO; GO:2000185; P:regulation of phosphate transmembrane transport; IGI:SGD.
DR InterPro; IPR001898; SLC13A/DASS.
DR InterPro; IPR004331; SPX_dom.
DR Pfam; PF00939; Na_sulph_symp; 1.
DR Pfam; PF03105; SPX; 2.
DR PROSITE; PS51382; SPX; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphate transport; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation; Vacuole.
FT CHAIN 1..894
FT /note="Low-affinity phosphate transporter PHO91"
FT /id="PRO_0000172519"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 874..894
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..256
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT REGION 124..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 894 AA; 99490 MW; 21938C585EB05509 CRC64;
MKFSHSLQFN SVPEWSTKYL AYSQLKKLIY SLQKDKLYSN NKHHVVEPHD ANDENLPLLA
DASPDDQFYI SKFVAALNQE LKKIDKFYIS QETGLIANYN ELKDDVMELE NTNKATQLFN
QQQQHQLQSV ARNRKSKSQQ RQRRFSSVSS TDSNPSLTDM SIDSAPVIHT QVSNTTNNGN
SMQNLASASV SLSNSNPVYL SPFTQHRLSL KKRLISIYTQ LSELKDFIEL NQTGFSKICK
KFDKSLNTNL KQNYLNYIKF HSHVFNPATI NRIQHHITET ILTYASLNKG TRRPSNTFNL
DADRINNDEN SSGNEEDEDG NRQEVLDFQD AERELSSHLR DHVVWERNTV WKDMMNLERK
YQSAKTDNKK FSKLSSSQLR PNANITESMA MSSGGAGIIA PSTDSLTFRE LMHLPPKQWL
QFIMGQTSLL KFLLITSCFI ALLTFNLTPF TQDSLQKNCF AILIYASLLW ATETIPLFVT
SLMIPLLIVV FPVIKDPITS QPMSPRDSSQ FILSTMWSSV IMLLLGGFTL AAALSKYNIA
KVLSTHILAS AGTNPHFILL TNMFVALFVS MWVSNVAAPV LCYSIVQPLL RTLPRNCSYA
KALILGIALA SNIGGMSSPI ASPQNIFSIG IMDPSPSWAE WFMIALPVCF ICVMAIWVLL
IITFPPEPNV KILQLHPSRD PFTLKQWFVT LVCIITIVLW CLSNQISGIF GEMGIISIIP
IVVFFGTGLL TSDDFNNFMW TIVVLAMGGT TLGKAVSSSG LLSTMAQLIK AQVEHEPIFI
IVLIFGLVIL VMATFVSHTV AAMIIVPLMS EIGSNLPSGD HSRLLIVIAA LLCSSAMGLP
TSGFPNVTAI SMIDEVGDRY LTVGTFITRG VPASLLSYAA IVTVGYGILK VMGF
