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Q03770 (SSY1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SPS-sensor component SSY1
Alternative name(s):
Amino-acid permease homolog SSY1
Gene names
Name:SSY1
Synonyms:APF7, SHR10
Ordered Locus Names:YDR160W
ORF Names:YD8358.14
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length852 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Amino acid sensor component of the SPS-sensor system, which regulates the expression of several amino acid-metabolizing enzymes and amino acid- and peptide-permeases in response to extracellular amino acid levels by controlling the activity of two transcription factors, STP1 and STP2. Amino-acid permease homolog that seems to interact directly with the extracellular signaling molecules, but has no amino acid transporter activity. May recruit casein kinases YCK1 and YCK2 to hyperphosphorylate and activate downstream component PTR3 in response to amino acid stimulus. Ref.3 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Subunit structure

Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor complex. Interacts directly with PTR3 and SSY5. Interacts with YCK1. Ref.13

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.6 Ref.7.

Sequence similarities

Belongs to the amino acid-polyamine-organocation (APC) superfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 852852SPS-sensor component SSY1
PRO_0000054164

Regions

Topological domain1 – 285285Cytoplasmic Potential
Transmembrane286 – 30621Helical; Potential
Topological domain307 – 32923Extracellular Potential
Transmembrane330 – 35021Helical; Potential
Topological domain351 – 3577Cytoplasmic Potential
Transmembrane358 – 37821Helical; Potential
Topological domain379 – 40022Extracellular Potential
Transmembrane401 – 42121Helical; Potential
Topological domain4221Cytoplasmic Potential
Transmembrane423 – 44321Helical; Potential
Topological domain444 – 50057Extracellular Potential
Transmembrane501 – 52121Helical; Potential
Topological domain522 – 54019Cytoplasmic Potential
Transmembrane541 – 56121Helical; Potential
Topological domain562 – 62362Extracellular Potential
Transmembrane624 – 64421Helical; Potential
Topological domain645 – 67329Cytoplasmic Potential
Transmembrane674 – 69421Helical; Potential
Topological domain695 – 7039Extracellular Potential
Transmembrane704 – 72421Helical; Potential
Topological domain725 – 75531Cytoplasmic Potential
Transmembrane756 – 77621Helical; Potential
Topological domain777 – 7848Extracellular Potential
Transmembrane785 – 80521Helical; Potential
Topological domain806 – 85247Cytoplasmic Potential

Experimental info

Mutagenesis3821T → H or L: Constitutively active, up-regulates amino acid permease transcription in response to subthreshold concentraions of amino-acids. Ref.11
Mutagenesis3821T → K in SSY1-102; constitutively active, up-regulates amino acid permease transcription in the absence of amino-acids. Ref.11
Mutagenesis3821T → R: Constitutively active, up-regulates amino acid permease transcription in the absence of amino-acids. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q03770 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 81A94141DF4EEF7D

FASTA85295,744
        10         20         30         40         50         60 
MSSVNQIYDL FPNKHNIQFT DSHSQEHDTS SSLAKNDTDG TISIPGSIDT GILKSIIEEQ 

        70         80         90        100        110        120 
GWNDAELYRS SIQNQRFFLT DKYTKKKHLT MEDMLSPEEE QIYQEPIQDF QTYNKRVQRE 

       130        140        150        160        170        180 
YELRERMEEF FRQNTKNDLH ILNEDSLNQQ YSPLGPADYV LPLDRYSRMK HIASNFFRKK 

       190        200        210        220        230        240 
LGIPRKLKRR SHYNPNAEGH TKGNSSILSS TTDVIDNASY RNIAIDENVD ITHKEHAIDE 

       250        260        270        280        290        300 
INEQGASGSE SVVEGGSLLH DIEKVFNRSR ATRKYHIQRK LKVRHIQMLS IGACFSVGLF 

       310        320        330        340        350        360 
LTSGKAFSIA GPFGTLLGFG LTGSIILATM LSFTELSTLI PVSSGFSGLA SRFVEDAFGF 

       370        380        390        400        410        420 
ALGWTYWISC MLALPAQVSS STFYLSYYNN VNISKGVTAG FITLFSAFSI VVNLLDVSIM 

       430        440        450        460        470        480 
GEIVYVAGIS KVIIAILMVF TMIILNAGHG NDIHEGVGFR YWDSSKSVRN LTYGLYRPTF 

       490        500        510        520        530        540 
DLADAGEGSK KGISGPKGRF LATASVMLIS TFAFSGVEMT FLASGEAINP RKTIPSATKR 

       550        560        570        580        590        600 
TFSIVLISYV FLIFSVGINI YSGDPRLLSY FPGISEKRYE AIIKGTGMDW RLRTNCRGGI 

       610        620        630        640        650        660 
DYRQISVGTG YSSPWVVALQ NFGLCTFASA FNAILIFFTA TAGISSLFSC SRTLYAMSVQ 

       670        680        690        700        710        720 
RKAPPVFEIC SKRGVPYVSV IFSSLFSVIA YIAVDQTAIE NFDVLANVSS ASTSIIWMGL 

       730        740        750        760        770        780 
NLSFLRFYYA LKQRKDIISR NDSSYPYKSP FQPYLAIYGL VGCSLFVIFM GYPNFIHHFW 

       790        800        810        820        830        840 
STKAFFSAYG GLMFFFISYT AYKVLGTSKI QRLDQLDMDS GRREMDRTDW TEHSQYLGTY 

       850 
RERAKKLVTW LI

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"The permease homologue Ssy1p controls the expression of amino acid and peptide transporter genes in Saccharomyces cerevisiae."
Didion T., Regenberg B., Joergensen M.U., Kielland-Brandt M.C., Andersen H.A.
Mol. Microbiol. 27:643-650(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Mutations in five loci affecting GAP1-independent uptake of neutral amino acids in yeast."
Joergensen M.U., Bruun M.B., Didion T., Kielland-Brandt M.C.
Yeast 14:103-114(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[5]"Amino acid signaling in Saccharomyces cerevisiae: a permease-like sensor of external amino acids and F-Box protein Grr1p are required for transcriptional induction of the AGP1 gene, which encodes a broad-specificity amino acid permease."
Iraqui I., Vissers S., Bernard F., de Craene J.-O., Boles E., Urrestarazu A., Andre B.
Mol. Cell. Biol. 19:989-1001(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Ssy1p and Ptr3p are plasma membrane components of a yeast system that senses extracellular amino acids."
Klasson H., Fink G.R., Ljungdahl P.O.
Mol. Cell. Biol. 19:5405-5416(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Genetic and biochemical analysis of the yeast plasma membrane Ssy1p-Ptr3p-Ssy5p sensor of extracellular amino acids."
Forsberg H., Ljungdahl P.O.
Mol. Cell. Biol. 21:814-826(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"The role of the yeast plasma membrane SPS nutrient sensor in the metabolic response to extracellular amino acids."
Forsberg H., Gilstring C.F., Zargari A., Martinez P., Ljungdahl P.O.
Mol. Microbiol. 42:215-228(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Genome-wide expression analysis of genes affected by amino acid sensor Ssy1p in Saccharomyces cerevisiae."
Kodama Y., Omura F., Takahashi K., Shirahige K., Ashikari T.
Curr. Genet. 41:63-72(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Receptor-mediated endoproteolytic activation of two transcription factors in yeast."
Andreasson C., Ljungdahl P.O.
Genes Dev. 16:3158-3172(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Constitutive and hyperresponsive signaling by mutant forms of Saccharomyces cerevisiae amino acid sensor Ssy1."
Gaber R.F., Ottow K., Andersen H.A., Kielland-Brandt M.C.
Eukaryot. Cell 2:922-929(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-382.
[12]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[13]"Activation of the SPS amino acid-sensing pathway in Saccharomyces cerevisiae correlates with the phosphorylation state of a sensor component, Ptr3."
Liu Z., Thornton J., Spirek M., Butow R.A.
Mol. Cell. Biol. 28:551-563(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PTR3; SSY5 AND YCK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z50046 Genomic DNA. Translation: CAA90380.1.
BK006938 Genomic DNA. Translation: DAA12000.1.
PIRS57984.
RefSeqNP_010444.1. NM_001180467.1.

3D structure databases

ProteinModelPortalQ03770.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2920N.
IntActQ03770. 2 interactions.
MINTMINT-1733718.
STRING4932.YDR160W.

Protein family/group databases

TCDB2.A.3.10.12. amino acid-polyamine-organocation (APC) family.

Proteomic databases

PaxDbQ03770.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR160W; YDR160W; YDR160W.
GeneID851738.
KEGGsce:YDR160W.

Organism-specific databases

CYGDYDR160w.
SGDS000002567. SSY1.

Phylogenomic databases

eggNOGCOG0833.
GeneTreeENSGT00510000049744.
HOGENOMHOG000065954.
KOK16261.
OMARFVEDAF.
OrthoDBEOG422DSX.

Gene expression databases

GenevestigatorQ03770.
GermOnlineYDR160W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004841. AA-permease_dom.
IPR002293. AA/rel_permease1.
IPR004762. Amino_acid_permease_fungi.
[Graphical view]
PANTHERPTHR11785. PTHR11785. 1 hit.
PfamPF00324. AA_permease. 1 hit.
[Graphical view]
TIGRFAMsTIGR00913. 2A0310. 1 hit.
PROSITEPS00218. AMINO_ACID_PERMEASE_1. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio969469.

Entry information

Entry nameSSY1_YEAST
AccessionPrimary (citable) accession number: Q03770
Secondary accession number(s): D6VSE0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents