SSY1_YEAST
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 03-AUG-2022, entry version 151.
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}.
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; 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; 106.
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; Q03770; -.
DR PRIDE; Q03770; -.
DR EnsemblFungi; YDR160W_mRNA; YDR160W; YDR160W.
DR GeneID; 851738; -.
DR KEGG; sce:YDR160W; -.
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 BioCyc; YEAST:G3O-29750-MON; -.
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:0016021; C:integral component of membrane; IBA:GO_Central.
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 InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 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, up-
FT regulates amino acid permease transcription in the absence
FT 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
