PHO87_YEAST
ID PHO87_YEAST Reviewed; 923 AA.
AC P25360; D6VR47;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Inorganic phosphate transporter PHO87;
GN Name=PHO87; OrderedLocusNames=YCR037C; ORFNames=YCR37C, YCR524;
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=1964349; DOI=10.1002/yea.320060609;
RA Thierry A., Fairhead C., Dujon B.;
RT "The complete sequence of the 8.2 kb segment left of MAT on chromosome III
RT reveals five ORFs, including a gene for a yeast ribokinase.";
RL Yeast 6:521-534(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION TO 72.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP CHARACTERIZATION.
RX PubMed=8598055; DOI=10.1007/bf02208615;
RA Bun-Ya M., Shikata K., Nakade S., Yompakdee C., Harashima S., Oshima Y.;
RT "Two new genes, PHO86 and PHO87, involved in inorganic phosphate uptake in
RT Saccharomyces cerevisiae.";
RL Curr. Genet. 29:344-351(1996).
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY
RP 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 [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY
RP 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: Involved in the uptake of inorganic phosphate.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 504 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 ---------------------------------------------------------------------------
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; X56909; CAA40229.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42304.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07516.1; -; Genomic_DNA.
DR PIR; S12919; MMBY7C.
DR RefSeq; NP_009966.2; NM_001178751.1.
DR AlphaFoldDB; P25360; -.
DR SMR; P25360; -.
DR BioGRID; 31020; 84.
DR DIP; DIP-7842N; -.
DR IntAct; P25360; 6.
DR MINT; P25360; -.
DR STRING; 4932.YCR037C; -.
DR TCDB; 2.A.47.2.1; the divalent anion:na(+) symporter (dass) family.
DR iPTMnet; P25360; -.
DR MaxQB; P25360; -.
DR PaxDb; P25360; -.
DR PRIDE; P25360; -.
DR EnsemblFungi; YCR037C_mRNA; YCR037C; YCR037C.
DR GeneID; 850403; -.
DR KEGG; sce:YCR037C; -.
DR SGD; S000000633; PHO87.
DR VEuPathDB; FungiDB:YCR037C; -.
DR eggNOG; KOG1281; Eukaryota.
DR GeneTree; ENSGT01030000234550; -.
DR HOGENOM; CLU_005170_8_0_1; -.
DR InParanoid; P25360; -.
DR OMA; CKQELKS; -.
DR BioCyc; MetaCyc:G3O-29349-MON; -.
DR BioCyc; YEAST:G3O-29349-MON; -.
DR BRENDA; 7.3.2.1; 984.
DR PRO; PR:P25360; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25360; 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; IGI: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:0097080; P:plasma membrane selenite transport; IMP: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; 1.
DR PROSITE; PS51382; SPX; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Isopeptide bond; Membrane; Phosphate transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..923
FT /note="Inorganic phosphate transporter PHO87"
FT /id="PRO_0000172517"
FT TOPO_DOM 1..461
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..537
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..627
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..707
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 729..735
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..767
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..849
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 850..870
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 871..898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 920..923
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..334
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT REGION 40..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 72
FT /note="S -> P (in Ref. 1; CAA40229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 923 AA; 102540 MW; E94DC4C152355A47 CRC64;
MRFSHFLKYN AVPEWQNHYL DYNELKNLIY TLQTDELKQE TPTGDLNDDA DSQTPGPIAD
IESNIAAGEP SSSKRRFTHK LKRKLFGSKT PSGSKRGDSD EKAIDGNNIN EETIELDELS
PQGKTTSFNK NFIRKKFFES RSSSVSSEGK TLFSSYDTFV TNLSDEKLKV DDFYKRMEAK
FYERFDHLIN DLEKEGIVTR LNETFNPEIQ ALPPLREIIS GTSETHSSNN PFEIHSSNID
SELRNRFDYS EEEMDEDDDV DVFADTTDNT ALLNYSQFNI KSQKKSLLKQ TIINLYIDLC
QLKSFIELNR MGFSKITKKS DKVLHMNTRQ ELIESEEFFK DTYIFQHETL SSLNSKIAQL
IEFYAVLMGQ PGNVDSCKQE LKSYLHDHIV WERSNTWKDM LGLSSQNNDI ITIEDEAEKL
MQEKLQIEYF KYPLPKPINL KFTKIENLAV PKLFFGKRAM KIGFIIIVTG VLLGVKTFND
PVEHRCMALV ECCAFLWASE AIPLHITGLL VPLLTVLFRV LKDDDGKVMG AAAASTEILG
TMWSSTIMIL LAGFTLGEAL SQYNVAKVLA SWLLALAGTK PRNVLLMAMS VVFFLSMWIS
NVASPVLTYS LLTPLLDPLD YTSPFAKALV MGVALSADIG GMASPISSPQ NIISMQYLKP
YGIGWGQFFA VALPTGILSM LCSWALMILT FKIGKTKLEK FKPIRTRFTI KQYFIIIVTI
ATILLWCVES QIESAFGSSG EIAVIPIVLF FGTGLLSTKD FNTFPWSIVV LAMGGIALGK
AVSSSGLLVT IARALQKKIQ NDGVFAILCI FGILMLVVGT FVSHTVSAII IIPLVQEVGD
KLSDPKAAPI LVFGCALLAS CGMGLASSGF PNVTAISMTD KKGNRWLTVG AFISRGVPAS
LLAFVCVITL GYGISSSVLK GST
