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 27-MAR-2024, entry version 171.
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; 113.
DR MINT; P39535; -.
DR STRING; 4932.YJL198W; -.
DR TCDB; 2.A.47.2.3; the divalent anion:na(+) symporter (dass) family.
DR GlyGen; P39535; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P39535; -.
DR MaxQB; P39535; -.
DR PaxDb; 4932-YJL198W; -.
DR PeptideAtlas; P39535; -.
DR EnsemblFungi; YJL198W_mRNA; YJL198W; YJL198W.
DR GeneID; 853241; -.
DR KEGG; sce:YJL198W; -.
DR AGR; SGD:S000003734; -.
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 OrthoDB; 5485124at2759; -.
DR BioCyc; YEAST:G3O-31629-MONOMER; -.
DR BRENDA; 7.3.2.1; 984.
DR BioGRID-ORCS; 853241; 2 hits in 10 CRISPR screens.
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:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; 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 CDD; cd01115; SLC13_permease; 1.
DR CDD; cd14478; SPX_PHO87_PHO90_like; 1.
DR InterPro; IPR004680; Cit_transptr-like_dom.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR10283:SF110; INORGANIC PHOSPHATE TRANSPORTER PHO87-RELATED; 1.
DR PANTHER; PTHR10283; SOLUTE CARRIER FAMILY 13 MEMBER; 1.
DR Pfam; PF03600; CitMHS; 1.
DR Pfam; PF03105; SPX; 1.
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
//
