PHO89_YEAST
ID PHO89_YEAST Reviewed; 574 AA.
AC P38361; D6VQU0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Phosphate permease PHO89;
DE AltName: Full=Na(+)/Pi cotransporter PHO89;
GN Name=PHO89; Synonyms=ITN1; OrderedLocusNames=YBR296C; ORFNames=YBR2113;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
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 [3]
RP FUNCTION, AND CHARACTERIZATION.
RX PubMed=9671031; DOI=10.1007/s004380050776;
RA Martinez P., Persson B.L.;
RT "Identification, cloning and characterization of a derepressible Na+-
RT coupled phosphate transporter in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 258:628-638(1998).
RN [4]
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 [5]
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: Sodium-phosphate symporter. Active in early growth phase.
CC {ECO:0000269|PubMed:9671031}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for phosphate;
CC pH dependence:
CC Optimum pH is 9.5.;
CC -!- INTERACTION:
CC P38361; P38361: PHO89; NbExp=4; IntAct=EBI-21068, EBI-21068;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: The gene for PHO89 is only transcribed under conditions of
CC phosphate limitation.
CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC
CC 2.A.20) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z36165; CAA85261.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07410.1; -; Genomic_DNA.
DR PIR; S46178; S46178.
DR RefSeq; NP_009855.1; NM_001178644.1.
DR AlphaFoldDB; P38361; -.
DR SMR; P38361; -.
DR BioGRID; 32989; 59.
DR DIP; DIP-4966N; -.
DR IntAct; P38361; 3.
DR MINT; P38361; -.
DR STRING; 4932.YBR296C; -.
DR TCDB; 2.A.20.2.2; the inorganic phosphate transporter (pit) family.
DR iPTMnet; P38361; -.
DR MaxQB; P38361; -.
DR PaxDb; P38361; -.
DR PRIDE; P38361; -.
DR EnsemblFungi; YBR296C_mRNA; YBR296C; YBR296C.
DR GeneID; 852599; -.
DR KEGG; sce:YBR296C; -.
DR SGD; S000000500; PHO89.
DR VEuPathDB; FungiDB:YBR296C; -.
DR eggNOG; KOG2493; Eukaryota.
DR GeneTree; ENSGT00390000014879; -.
DR HOGENOM; CLU_015355_3_0_1; -.
DR InParanoid; P38361; -.
DR OMA; ATIYAIW; -.
DR BioCyc; YEAST:G3O-29214-MON; -.
DR PRO; PR:P38361; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38361; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015319; F:sodium:inorganic phosphate symporter activity; IDA:SGD.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IDA:SGD.
DR GO; GO:0006817; P:phosphate ion transport; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR InterPro; IPR001204; Phos_transporter.
DR PANTHER; PTHR11101; PTHR11101; 1.
DR Pfam; PF01384; PHO4; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..574
FT /note="Phosphate permease PHO89"
FT /id="PRO_0000080781"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 301..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 62654 MW; 9794C1D9D75014D5 CRC64;
MALHQFDYIF AIAMLFAFLD AFNIGANDVA NSFASSISSR SLKYWQAMVL AGLCEFLGAV
LAGARVSGTI KNNIIDSSIF TNDPAVLMLT MTSALIGSSC WLTFATAIGM PVSTTHSIVG
GTIGAGIAAG GANGVVWGWS GVSQIIASWF IAPILAGAIA AIVFSISRFS VLEVKSLERS
IKNALLLVGV LVFATFSILT MLIVWKGSPN LHLDDLSETE TAVSIVLTGA IASIVYFIFF
YPFYRRKVLD QDWTLKLIDI FRGPSFYFKS TDDIPPMPEG HQLTIDYYEG RRNLGTTVSV
EDEENKAASN SNDSVKNKED IQEVDLVRTE TEPETKLSTK QYWWSLLKQG PKKWPLLFWL
VISHGWTQDV IHAQVNDRDM LSGDLKGMYE RSKFYDNRVE YIYSVLQAIT AATMSFAHGA
NDVANATGPL SAVYVIWKTN TIGAKSEVPV WVLAYGGVAL VIGCWTYGYN IIKNLGNKMI
LQSPSRGFSI ELAVAITTVM ATQLGIPTST TQIAVGGIVA VGLCNKDLKS VNWRMVAWCY
SGWFLTLPIA GLIAGIINGI ILNAPRFGVE YQMT
