PHO84_YEAST
ID PHO84_YEAST Reviewed; 587 AA.
AC P25297; D6W0G2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Inorganic phosphate transporter PHO84;
GN Name=PHO84; OrderedLocusNames=YML123C; ORFNames=YM7056.03C;
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=2038328; DOI=10.1128/mcb.11.6.3229-3238.1991;
RA Bun-Ya M., Nishimura M., Harashima S., Oshima Y.;
RT "The PHO84 gene of Saccharomyces cerevisiae encodes an inorganic phosphate
RT transporter.";
RL Mol. Cell. Biol. 11:3229-3238(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302; SER-303; SER-316;
RP THR-317; SER-321; SER-577; SER-579 AND SER-581, AND IDENTIFICATION BY MASS
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302; SER-303; SER-316;
RP THR-317; SER-321; SER-579 AND SER-581, AND IDENTIFICATION BY MASS
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: High-affinity transporter for external inorganic phosphate.
CC Is not an essential protein, since a constitutive, low affinity pI
CC transporter exists in yeast.
CC -!- SUBUNIT: May function as a monomer.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Under the control of phosphate. It is derepressed by
CC phosphate starvation.
CC -!- MISCELLANEOUS: Present with 335000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; D90346; BAA14358.1; -; Genomic_DNA.
DR EMBL; Z49218; CAA89157.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09776.1; -; Genomic_DNA.
DR PIR; S54061; S54061.
DR RefSeq; NP_013583.1; NM_001182486.1.
DR AlphaFoldDB; P25297; -.
DR SMR; P25297; -.
DR BioGRID; 35082; 224.
DR DIP; DIP-5072N; -.
DR IntAct; P25297; 11.
DR MINT; P25297; -.
DR STRING; 4932.YML123C; -.
DR TCDB; 2.A.1.9.1; the major facilitator superfamily (mfs).
DR iPTMnet; P25297; -.
DR MaxQB; P25297; -.
DR PaxDb; P25297; -.
DR PRIDE; P25297; -.
DR TopDownProteomics; P25297; -.
DR EnsemblFungi; YML123C_mRNA; YML123C; YML123C.
DR GeneID; 854916; -.
DR KEGG; sce:YML123C; -.
DR SGD; S000004592; PHO84.
DR VEuPathDB; FungiDB:YML123C; -.
DR eggNOG; KOG0252; Eukaryota.
DR GeneTree; ENSGT00940000174507; -.
DR HOGENOM; CLU_001265_46_14_1; -.
DR InParanoid; P25297; -.
DR OMA; IAQTCIG; -.
DR BioCyc; MetaCyc:G3O-32702-MON; -.
DR BioCyc; YEAST:G3O-32702-MON; -.
DR BRENDA; 7.3.2.1; 984.
DR PRO; PR:P25297; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P25297; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:SGD.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IMP:SGD.
DR GO; GO:0097079; F:selenite:proton symporter activity; IDA:SGD.
DR GO; GO:0006828; P:manganese ion transport; IMP:SGD.
DR GO; GO:0006817; P:phosphate ion transport; IDA:SGD.
DR GO; GO:0097080; P:plasma membrane selenite transport; IMP:SGD.
DR GO; GO:0006797; P:polyphosphate metabolic process; IMP:SGD.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004738; Phos_permease.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00887; 2A0109; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Membrane; Phosphate transport; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..587
FT /note="Inorganic phosphate transporter PHO84"
FT /id="PRO_0000050477"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..395
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..442
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 568..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT CONFLICT 162
FT /note="A -> AHSPAINFVA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="S -> Y (in Ref. 1; BAA14358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 64382 MW; E463954395E8A840 CRC64;
MSSVNKDTIH VAERSLHKEH LTEGGNMAFH NHLNDFAHIE DPLERRRLAL ESIDDEGFGW
QQVKTISIAG VGFLTDSYDI FAINLGITMM SYVYWHGSMP GPSQTLLKVS TSVGTVIGQF
GFGTLADIVG RKRIYGMELI IMIVCTILQT TVAHSPAINF VAVLTFYRIV MGIGIGGDYP
LSSIITSEFA TTKWRGAIMG AVFANQAWGQ ISGGIIALIL VAAYKGELEY ANSGAECDAR
CQKACDQMWR ILIGLGTVLG LACLYFRLTI PESPRYQLDV NAKLELAAAA QEQDGEKKIH
DTSDEDMAIN GLERASTAVE SLDNHPPKAS FKDFCRHFGQ WKYGKILLGT AGSWFTLDVA
FYGLSLNSAV ILQTIGYAGS KNVYKKLYDT AVGNLILICA GSLPGYWVSV FTVDIIGRKP
IQLAGFIILT ALFCVIGFAY HKLGDHGLLA LYVICQFFQN FGPNTTTFIV PGECFPTRYR
STAHGISAAS GKVGAIIAQT ALGTLIDHNC ARDGKPTNCW LPHVMEIFAL FMLLGIFTTL
LIPETKRKTL EEINELYHDE IDPATLNFRN KNNDIESSSP SQLQHEA
