PHO88_YEAST
ID PHO88_YEAST Reviewed; 188 AA.
AC P38264; D6VQA5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=SRP-independent targeting protein 3 {ECO:0000303|PubMed:27905431};
DE AltName: Full=Inorganic phosphate transport protein PHO88 {ECO:0000305|PubMed:8709965};
DE AltName: Full=Phosphate metabolism protein PHO88;
GN Name=PHO88 {ECO:0000303|PubMed:8709965};
GN Synonyms=SND3 {ECO:0000303|PubMed:27905431};
GN OrderedLocusNames=YBR106W {ECO:0000312|SGD:S000000310}; ORFNames=YBR0835;
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=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8709965; DOI=10.1007/bf02173648;
RA Yompakdee C., Ogawa N., Harashima S., Oshima Y.;
RT "A putative membrane protein, Pho88p, involved in inorganic phosphate
RT transport in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 251:580-590(1996).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [9]
RP FUNCTION.
RX PubMed=16552446; DOI=10.1371/journal.pgen.0020035;
RA Gatbonton T., Imbesi M., Nelson M., Akey J.M., Ruderfer D.M., Kruglyak L.,
RA Simon J.A., Bedalov A.;
RT "Telomere length as a quantitative trait: genome-wide survey and genetic
RT mapping of telomere length-control genes in yeast.";
RL PLoS Genet. 2:304-315(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, 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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ENV10.
RX PubMed=27905431; DOI=10.1038/nature20169;
RA Aviram N., Ast T., Costa E.A., Arakel E.C., Chuartzman S.G., Jan C.H.,
RA Hassdenteufel S., Dudek J., Jung M., Schorr S., Zimmermann R.,
RA Schwappach B., Weissman J.S., Schuldiner M.;
RT "The SND proteins constitute an alternative targeting route to the
RT endoplasmic reticulum.";
RL Nature 540:134-138(2016).
CC -!- FUNCTION: Functions in the SND pathway, a SRP (signal recognition
CC particle) and GET (guided entry of tail-anchored proteins) independent
CC pathway for targeting a broad range of substrate proteins to the
CC endoplasmic reticulum. SND functions in parallel to GET in targeting
CC proteins with downstream hydrophobic motifs (PubMed:27905431). Involved
CC in inorganic phosphate uptake (PubMed:8709965). Also involved in
CC telomere length regulation and maintenance (PubMed:16552446).
CC {ECO:0000269|PubMed:16552446, ECO:0000269|PubMed:27905431,
CC ECO:0000269|PubMed:8709965}.
CC -!- SUBUNIT: Interacts with ENV10/SND2. ENV10/SND2 and PHO88/SND3 form a
CC complex with the translocon in the endoplasmic reticulum membrane.
CC {ECO:0000269|PubMed:27905431}.
CC -!- INTERACTION:
CC P38264; P17064: FCY2; NbExp=3; IntAct=EBI-13350, EBI-2047850;
CC P38264; P38353: SSH1; NbExp=3; IntAct=EBI-13350, EBI-18175;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:27905431}; Single-pass
CC membrane protein {ECO:0000255}. Mitochondrion
CC {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:8709965}.
CC -!- MISCELLANEOUS: Present with 61800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PHO88 family. {ECO:0000305}.
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DR EMBL; X78993; CAA55609.1; -; Genomic_DNA.
DR EMBL; Z35975; CAA85061.1; -; Genomic_DNA.
DR EMBL; AY558180; AAS56506.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07225.1; -; Genomic_DNA.
DR PIR; S48271; S48271.
DR RefSeq; NP_009664.1; NM_001178454.1.
DR AlphaFoldDB; P38264; -.
DR BioGRID; 32810; 337.
DR DIP; DIP-4888N; -.
DR IntAct; P38264; 83.
DR MINT; P38264; -.
DR STRING; 4932.YBR106W; -.
DR TCDB; 9.A.64.1.1; the srp-independent targeting (snd) family.
DR iPTMnet; P38264; -.
DR MaxQB; P38264; -.
DR PaxDb; P38264; -.
DR PRIDE; P38264; -.
DR EnsemblFungi; YBR106W_mRNA; YBR106W; YBR106W.
DR GeneID; 852403; -.
DR KEGG; sce:YBR106W; -.
DR SGD; S000000310; PHO88.
DR VEuPathDB; FungiDB:YBR106W; -.
DR eggNOG; KOG4554; Eukaryota.
DR HOGENOM; CLU_099163_0_0_1; -.
DR InParanoid; P38264; -.
DR OMA; ERPWKAA; -.
DR BioCyc; YEAST:G3O-29068-MON; -.
DR PRO; PR:P38264; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38264; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR GO; GO:0051604; P:protein maturation; IMP:SGD.
DR GO; GO:0045047; P:protein targeting to ER; IMP:SGD.
DR InterPro; IPR012098; SND3_fun.
DR PANTHER; PTHR28112; PTHR28112; 1.
DR Pfam; PF10032; Pho88; 1.
DR PIRSF; PIRSF008756; P_tr_PHO88; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Mitochondrion; Phosphate transport;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..188
FT /note="SRP-independent targeting protein 3"
FT /id="PRO_0000058405"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 157..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 188 AA; 21137 MW; 748B685C4D3C3E78 CRC64;
MNPQVSNIII MLVMMQLSRR IDMEDPTIIM YIRILYCSSI GISWIIYQMA RKRIVAKNDM
TTMKYVEPGN AMSGEGEKLQ VTTVRDYDLK EIDSAIKSIY TGMAMMGFMH LYLKYTNPLF
MQSISPVKSA LEHNEVKIHL FGKPATGDLK RPFKAPSLFG GMGQTGPKTD KKSIEEAERA
GNAGVKAE
