ID   SSY1_YEAST              Reviewed;         852 AA.
AC   Q03770; D6VSE0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=SPS-sensor component SSY1;
DE   AltName: Full=Amino-acid permease homolog SSY1;
GN   Name=SSY1; Synonyms=APF7, SHR10; OrderedLocusNames=YDR160W;
GN   ORFNames=YD8358.14;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
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.
RX   PubMed=9489675; DOI=10.1046/j.1365-2958.1998.00714.x;
RA   Didion T., Regenberg B., Joergensen M.U., Kielland-Brandt M.C.,
RA   Andersen H.A.;
RT   "The permease homologue Ssy1p controls the expression of amino acid and
RT   peptide transporter genes in Saccharomyces cerevisiae.";
RL   Mol. Microbiol. 27:643-650(1998).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=9483800;
RX   DOI=10.1002/(sici)1097-0061(19980130)14:2<103::aid-yea203>3.0.co;2-c;
RA   Joergensen M.U., Bruun M.B., Didion T., Kielland-Brandt M.C.;
RT   "Mutations in five loci affecting GAP1-independent uptake of neutral amino
RT   acids in yeast.";
RL   Yeast 14:103-114(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=9891035; DOI=10.1128/mcb.19.2.989;
RA   Iraqui I., Vissers S., Bernard F., de Craene J.-O., Boles E.,
RA   Urrestarazu A., Andre B.;
RT   "Amino acid signaling in Saccharomyces cerevisiae: a permease-like sensor
RT   of external amino acids and F-Box protein Grr1p are required for
RT   transcriptional induction of the AGP1 gene, which encodes a broad-
RT   specificity amino acid permease.";
RL   Mol. Cell. Biol. 19:989-1001(1999).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10409731; DOI=10.1128/mcb.19.8.5405;
RA   Klasson H., Fink G.R., Ljungdahl P.O.;
RT   "Ssy1p and Ptr3p are plasma membrane components of a yeast system that
RT   senses extracellular amino acids.";
RL   Mol. Cell. Biol. 19:5405-5416(1999).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11154269; DOI=10.1128/mcb.21.3.814-826.2001;
RA   Forsberg H., Ljungdahl P.O.;
RT   "Genetic and biochemical analysis of the yeast plasma membrane Ssy1p-Ptr3p-
RT   Ssy5p sensor of extracellular amino acids.";
RL   Mol. Cell. Biol. 21:814-826(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=11679080; DOI=10.1046/j.1365-2958.2001.02627.x;
RA   Forsberg H., Gilstring C.F., Zargari A., Martinez P., Ljungdahl P.O.;
RT   "The role of the yeast plasma membrane SPS nutrient sensor in the metabolic
RT   response to extracellular amino acids.";
RL   Mol. Microbiol. 42:215-228(2001).
RN   [9]
RP   FUNCTION.
RX   PubMed=12073087; DOI=10.1007/s00294-002-0291-1;
RA   Kodama Y., Omura F., Takahashi K., Shirahige K., Ashikari T.;
RT   "Genome-wide expression analysis of genes affected by amino acid sensor
RT   Ssy1p in Saccharomyces cerevisiae.";
RL   Curr. Genet. 41:63-72(2002).
RN   [10]
RP   FUNCTION.
RX   PubMed=12502738; DOI=10.1101/gad.239202;
RA   Andreasson C., Ljungdahl P.O.;
RT   "Receptor-mediated endoproteolytic activation of two transcription factors
RT   in yeast.";
RL   Genes Dev. 16:3158-3172(2002).
RN   [11]
RP   FUNCTION, AND MUTAGENESIS OF THR-382.
RX   PubMed=14555474; DOI=10.1128/ec.2.5.922-929.2003;
RA   Gaber R.F., Ottow K., Andersen H.A., Kielland-Brandt M.C.;
RT   "Constitutive and hyperresponsive signaling by mutant forms of
RT   Saccharomyces cerevisiae amino acid sensor Ssy1.";
RL   Eukaryot. Cell 2:922-929(2003).
RN   [12]
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   [13]
RP   FUNCTION, AND INTERACTION WITH PTR3; SSY5 AND YCK1.
RX   PubMed=17984223; DOI=10.1128/mcb.00929-07;
RA   Liu Z., Thornton J., Spirek M., Butow R.A.;
RT   "Activation of the SPS amino acid-sensing pathway in Saccharomyces
RT   cerevisiae correlates with the phosphorylation state of a sensor component,
RT   Ptr3.";
RL   Mol. Cell. Biol. 28:551-563(2008).
CC   -!- FUNCTION: Amino acid sensor component of the SPS-sensor system, which
CC       regulates the expression of several amino acid-metabolizing enzymes and
CC       amino acid- and peptide-permeases in response to extracellular amino
CC       acid levels by controlling the activity of two transcription factors,
CC       STP1 and STP2. Amino-acid permease homolog that seems to interact
CC       directly with the extracellular signaling molecules, but has no amino
CC       acid transporter activity. May recruit casein kinases YCK1 and YCK2 to
CC       hyperphosphorylate and activate downstream component PTR3 in response
CC       to amino acid stimulus. {ECO:0000269|PubMed:10409731,
CC       ECO:0000269|PubMed:11154269, ECO:0000269|PubMed:11679080,
CC       ECO:0000269|PubMed:12073087, ECO:0000269|PubMed:12502738,
CC       ECO:0000269|PubMed:14555474, ECO:0000269|PubMed:17984223,
CC       ECO:0000269|PubMed:9489675, ECO:0000269|PubMed:9891035}.
CC   -!- SUBUNIT: Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino
CC       acid sensor complex. Interacts directly with PTR3 and SSY5. Interacts
CC       with YCK1. {ECO:0000269|PubMed:17984223}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10409731,
CC       ECO:0000269|PubMed:11154269}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:10409731, ECO:0000269|PubMed:11154269}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. {ECO:0000305}.
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DR   EMBL; Z50046; CAA90380.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12000.1; -; Genomic_DNA.
DR   PIR; S57984; S57984.
DR   RefSeq; NP_010444.1; NM_001180467.1.
DR   AlphaFoldDB; Q03770; -.
DR   BioGRID; 32211; 107.
DR   DIP; DIP-2920N; -.
DR   IntAct; Q03770; 4.
DR   MINT; Q03770; -.
DR   STRING; 4932.YDR160W; -.
DR   TCDB; 2.A.3.10.12; the amino acid-polyamine-organocation (apc) family.
DR   PaxDb; 4932-YDR160W; -.
DR   PeptideAtlas; Q03770; -.
DR   EnsemblFungi; YDR160W_mRNA; YDR160W; YDR160W.
DR   GeneID; 851738; -.
DR   KEGG; sce:YDR160W; -.
DR   AGR; SGD:S000002567; -.
DR   SGD; S000002567; SSY1.
DR   VEuPathDB; FungiDB:YDR160W; -.
DR   eggNOG; KOG1286; Eukaryota.
DR   HOGENOM; CLU_007946_8_6_1; -.
DR   InParanoid; Q03770; -.
DR   OMA; FIRFYYG; -.
DR   OrthoDB; 2048918at2759; -.
DR   BioCyc; YEAST:G3O-29750-MONOMER; -.
DR   BioGRID-ORCS; 851738; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q03770; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03770; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0043200; P:response to amino acid; IMP:SGD.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR004841; AA-permease/SLC12A_dom.
DR   InterPro; IPR004762; Amino_acid_permease_fungi.
DR   NCBIfam; TIGR00913; 2A0310; 1.
DR   PANTHER; PTHR43341; AMINO ACID PERMEASE; 1.
DR   PANTHER; PTHR43341:SF39; SPS-SENSOR COMPONENT SSY1; 1.
DR   Pfam; PF00324; AA_permease; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..852
FT                   /note="SPS-sensor component SSY1"
FT                   /id="PRO_0000054164"
FT   TOPO_DOM        1..285
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..329
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        351..357
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        379..400
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        444..500
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        501..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        522..540
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        541..561
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        562..623
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        624..644
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        645..673
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        674..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        695..703
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        704..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        725..755
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        756..776
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        777..784
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        785..805
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        806..852
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          21..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         382
FT                   /note="T->H,L: Constitutively active, up-regulates amino
FT                   acid permease transcription in response to subthreshold
FT                   concentrations of amino acids."
FT                   /evidence="ECO:0000269|PubMed:14555474"
FT   MUTAGEN         382
FT                   /note="T->K: In SSY1-102; constitutively active,
FT                   up-regulates amino acid permease transcription in the
FT                   absence of amino-acids."
FT                   /evidence="ECO:0000269|PubMed:14555474"
FT   MUTAGEN         382
FT                   /note="T->R: Constitutively active, up-regulates amino acid
FT                   permease transcription in the absence of amino acids."
FT                   /evidence="ECO:0000269|PubMed:14555474"
SQ   SEQUENCE   852 AA;  95744 MW;  81A94141DF4EEF7D CRC64;
     MSSVNQIYDL FPNKHNIQFT DSHSQEHDTS SSLAKNDTDG TISIPGSIDT GILKSIIEEQ
     GWNDAELYRS SIQNQRFFLT DKYTKKKHLT MEDMLSPEEE QIYQEPIQDF QTYNKRVQRE
     YELRERMEEF FRQNTKNDLH ILNEDSLNQQ YSPLGPADYV LPLDRYSRMK HIASNFFRKK
     LGIPRKLKRR SHYNPNAEGH TKGNSSILSS TTDVIDNASY RNIAIDENVD ITHKEHAIDE
     INEQGASGSE SVVEGGSLLH DIEKVFNRSR ATRKYHIQRK LKVRHIQMLS IGACFSVGLF
     LTSGKAFSIA GPFGTLLGFG LTGSIILATM LSFTELSTLI PVSSGFSGLA SRFVEDAFGF
     ALGWTYWISC MLALPAQVSS STFYLSYYNN VNISKGVTAG FITLFSAFSI VVNLLDVSIM
     GEIVYVAGIS KVIIAILMVF TMIILNAGHG NDIHEGVGFR YWDSSKSVRN LTYGLYRPTF
     DLADAGEGSK KGISGPKGRF LATASVMLIS TFAFSGVEMT FLASGEAINP RKTIPSATKR
     TFSIVLISYV FLIFSVGINI YSGDPRLLSY FPGISEKRYE AIIKGTGMDW RLRTNCRGGI
     DYRQISVGTG YSSPWVVALQ NFGLCTFASA FNAILIFFTA TAGISSLFSC SRTLYAMSVQ
     RKAPPVFEIC SKRGVPYVSV IFSSLFSVIA YIAVDQTAIE NFDVLANVSS ASTSIIWMGL
     NLSFLRFYYA LKQRKDIISR NDSSYPYKSP FQPYLAIYGL VGCSLFVIFM GYPNFIHHFW
     STKAFFSAYG GLMFFFISYT AYKVLGTSKI QRLDQLDMDS GRREMDRTDW TEHSQYLGTY
     RERAKKLVTW LI
//