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PHO90_YEAST
ID   PHO90_YEAST             Reviewed;         881 AA.
AC   P39535;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Low-affinity phosphate transporter PHO90;
GN   Name=PHO90; OrderedLocusNames=YJL198W; ORFNames=J0336;
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 204508 / S288c;
RX   PubMed=7754713; DOI=10.1002/yea.320100912;
RA   Purnelle B., Coster F., Goffeau A.;
RT   "The sequence of a 36 kb segment on the left arm of yeast chromosome X
RT   identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6,
RT   CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two
RT   homologues to chromosome III genes.";
RL   Yeast 10:1235-1249(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   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   [5]
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   [6]
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   [7]
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: Low-affinity phosphate transporter involved in the control of
CC       cellular phosphate levels. {ECO:0000269|PubMed:11779791,
CC       ECO:0000269|PubMed:20133652}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Expression is constitutive and independent of inorganic
CC       phosphate concentration and PHO4 activity.
CC       {ECO:0000269|PubMed:12821119}.
CC   -!- MISCELLANEOUS: Present with 3430 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}.
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DR   EMBL; X77688; CAA54759.1; -; Genomic_DNA.
DR   EMBL; Z49473; CAA89493.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08610.1; -; Genomic_DNA.
DR   PIR; S46633; S46633.
DR   RefSeq; NP_012337.1; NM_001181631.1.
DR   AlphaFoldDB; P39535; -.
DR   SMR; P39535; -.
DR   BioGRID; 33566; 89.
DR   MINT; P39535; -.
DR   STRING; 4932.YJL198W; -.
DR   TCDB; 2.A.47.2.3; the divalent anion:na(+) symporter (dass) family.
DR   iPTMnet; P39535; -.
DR   MaxQB; P39535; -.
DR   PaxDb; P39535; -.
DR   PRIDE; P39535; -.
DR   EnsemblFungi; YJL198W_mRNA; YJL198W; YJL198W.
DR   GeneID; 853241; -.
DR   KEGG; sce:YJL198W; -.
DR   SGD; S000003734; PHO90.
DR   VEuPathDB; FungiDB:YJL198W; -.
DR   eggNOG; KOG1281; Eukaryota.
DR   GeneTree; ENSGT01030000234550; -.
DR   HOGENOM; CLU_005170_8_0_1; -.
DR   InParanoid; P39535; -.
DR   OMA; DINNFPW; -.
DR   BioCyc; YEAST:G3O-31629-MON; -.
DR   BRENDA; 7.3.2.1; 984.
DR   PRO; PR:P39535; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P39535; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA: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: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; IPR004680; Cit_transptr-like_dom.
DR   InterPro; IPR004331; SPX_dom.
DR   Pfam; PF03600; CitMHS; 1.
DR   Pfam; PF03105; SPX; 2.
DR   PROSITE; PS51382; SPX; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphate transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..881
FT                   /note="Low-affinity phosphate transporter PHO90"
FT                   /id="PRO_0000172518"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        539..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        581..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        663..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        691..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        718..738
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        758..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        805..825
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        854..874
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..288
FT                   /note="SPX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
SQ   SEQUENCE   881 AA;  97689 MW;  BB4466BC4D176714 CRC64;
     MRFSHFLKYN AVPEWQNHYM DYSELKNLIY TLQTDELQVG DNEEGFGAGK SSNITDRFKN
     KFSFKNAKED TSSGMNKDAG IVEETIELRE LPTAQTVAAK PSPFRRMKEK IFYKRRSSSA
     SSVSSTANEN LQLDTYDTFV GDLTAEKQKV DDFYKRTEAK FYDKFDALVK DLKKIGVIEY
     DIDDDTLFNE PIASTNDEVP PLDLDDDEDD DEFYDDQSNI EDNTALLHHS QYNIKSQKKS
     LLKKSIVNLY IDLCQLKSFI ELNRIGFAKI TKKSDKVLHL NTRTELIESE QFFKDTYAFQ
     AETIELLNSK ISQLVTFYAR ITDRPHNISH SKQELKSYLH DHIVWERSNT WKDMLGLLSQ
     ADELTPKETE YNANKLVGKL DLEYYRWPLP RPINLKFTSI NNVALPKLFF TKKAYKIYFI
     ILVTGLLLGI KTFNDAAQHR CMALVECVAF LWASEAIPLH ITAFLVPLLV VLFKVLKTSD
     GAIMSAASAS SEILAAMWSS TIMILLAGFT LGEVLAQYNI AKVLASWLLA FAGCKPRNVL
     LMAMCVVFFL SMWISNVAAP VLTYSLLSPL LDAMDADSPF AQALVLGVAL AANIGGMSSP
     ISSPQNIISM SYLKPYGIGW GQFFAVALPS GILAMLLVWI LLFTTFKMNK TKLEKFKPIK
     TKFTVKQYYI ITVTVATILL WCVESQIEGA FGSSGQIAII PIVLFFGTGL LSTQDLNAFP
     WSIVILAMGG IALGKAVSSS GLLSTIAKAL QKKIENDGVF AILCIFGILM LVVGTFVSHT
     VSAIIIIPLV QEVGDKLGNP KAAPILVFGC ALLSSCGMGL ASSGFPNVTA ISKVDRKGDR
     YLSVMTFLTR GVPASILAFL CVITLGYGIM ASVVKGNATS A
 
 
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