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P47002 (SSY5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Names and origin

Protein namesRecommended name:
SPS-sensor serine protease component SSY5
Alternative name(s):
Endoprotease SSY5
Gene names
Name:SSY5
Synonyms:APF8
Ordered Locus Names:YJL156C
ORF Names:J0570
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length699 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protease 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. Catalyzes the activation of these transcription factors, which are synthesized as latent cytoplasmic precursors, by proteolytic removal of an N-terminal inhibitory domain containing cytoplasmic retention motifs. SSY5 binds as an inactive protease complex to STP1. In response to extracellular amino acids and dependent on the other SPS-sensor components, the inhibitory propeptide is induced to dissociate, and thereby enables the catalytic domain to process STP1. Ref.3 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10

Subunit structure

Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor complex.

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.5.

Induction

Down-regulated after extracellular amino-acid addition.

Post-translational modification

The propeptide is autoproteolytically cleaved from the catalytic domain but remains associated, forming an inactive protease complex. This processing occurs even in the absence of signaling. Ref.8

Sequence similarities

Belongs to the peptidase S64 family.

Sequence caution

The sequence CAA89451.1 differs from that shown. Reason: Frameshift at position 685.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 381381
PRO_0000377374
Chain382 – 699318SPS-sensor serine protease component SSY5
PRO_0000072232

Regions

Region459 – 699241Serine protease

Sites

Active site4651Charge relay system Potential
Active site5451Charge relay system Potential
Active site6401Charge relay system Potential

Experimental info

Mutagenesis1311E → K in SSY5-13; constitutively active, confers 9.3% increased STP1 processing in the absence of amino acids. Ref.3
Mutagenesis420 – 4245Missing: Prevents maturation and amino-acid-induced STP1 cleavage. Ref.8
Mutagenesis5121E → K in SSY5-6; constitutively active, confers 30% increased STP1 processing in the absence of amino acids. Ref.9
Mutagenesis5751F → V in SSY5-14; constitutively active, confers 30% increased STP1 processing in the absence of amino acids. Ref.3
Mutagenesis5761Q → P in SSY5-15; constitutively active, confers 30% increased STP1 processing in the absence of amino acids. Ref.3
Mutagenesis5811K → N in SSY5-18; constitutively active, confers 15.5% increased STP1 processing in the absence of amino acids; when associated with H-632. Ref.3
Mutagenesis6321P → H in SSY5-18; constitutively active, confers 15.5% increased STP1 processing in the absence of amino acids; when associated with N-581. Ref.3
Mutagenesis6401S → A: Impairs maturation and amino acid-induced STP1 cleavage. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P47002 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: EF982A2717A71741

FASTA69977,527
        10         20         30         40         50         60 
MVRFFGLNKK KNEEKENTDL PADNEQNAAE TSSSNVSGNE ERIDPNSHDT NPENANNDDA 

        70         80         90        100        110        120 
STTFGSSIQS SSIFSRGRMT YGTGASSSMA TSEMRSHSSG HSGSKNSKNL QGFKDVGKPL 

       130        140        150        160        170        180 
RAVSFLSPVK EEESQDTQNT LDVSSSTSST LATSENAREN SFTSRRSITL EYIHKSLSEL 

       190        200        210        220        230        240 
EENLVDIMDD IHQDVISISK AVIEAIEYFK EFLPTTRDRI PYRISLEKSS SLRKINKIVL 

       250        260        270        280        290        300 
HFLDNLLVSD AFSNSRSILL RRFYFFLKKL NLITDDDLIS ESGVLPCLSV FCIGSHCNLP 

       310        320        330        340        350        360 
SMDKLGMILD ELTKMDSSII SDQEGAFIAP ILRGITPKSS ILTIMFGLPN LQHEHYEMIK 

       370        380        390        400        410        420 
VLYSLFPDVH MYCVKDYIKK AASAVGSIPS HTAATIDTIA PTKFQFSPPY AVSENPLELP 

       430        440        450        460        470        480 
ISMSLSTETS AKITGTLGGY LFPQTGSDKK FSQFASCSFA ITCAHVVLSE KQDYPNVMVP 

       490        500        510        520        530        540 
SNVLQTSYKK VLTKESDRYP DGSVEKTAFL EEVQRIDQNL NWQKSNKFGQ VVWGERAIVD 

       550        560        570        580        590        600 
HRLSDFAIIK VNSSFKCQNT LGNGLKSFPD PTLRFQNLHV KRKIFKMKPG MKVFKIGAST 

       610        620        630        640        650        660 
GYTSGELNST KLVYWADGKL QSSEFVVASP TPLFASAGDS GAWILTKLED RLGLGLVGML 

       670        680        690 
HSYDGEQRQF GLFTPIGDIL ERLHAVTKIQ WDIDPQLDG 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Mapping of an internal protease cleavage site in the Ssy5p component of the amino acid sensor of Saccharomyces cerevisiae and functional characterization of the resulting pro- and protease domains by gain-of-function genetics."
Poulsen P., Lo Leggio L., Kielland-Brandt M.C.
Eukaryot. Cell 5:601-608(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 382-399, FUNCTION, MUTAGENESIS OF GLU-131; PHE-575; GLN-576; LYS-581 AND PRO-632.
[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]"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.
[6]"Genetic analysis of the signalling pathway activated by external amino acids in Saccharomyces cerevisiae."
Bernard F., Andre B.
Mol. Microbiol. 41:489-502(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PTR3.
[7]"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.
[8]"Amino acid signaling in yeast: casein kinase I and the Ssy5 endoprotease are key determinants of endoproteolytic activation of the membrane-bound Stp1 transcription factor."
Abdel-Sater F., El Bakkoury M., Urrestarazu A., Vissers S., Andre B.
Mol. Cell. Biol. 24:9771-9785(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOCATALYTIC CLEAVAGE, CLEAVAGE OF STP1, MUTAGENESIS OF 420-PRO--SER-424 AND SER-640.
[9]"Constitutive signal transduction by mutant Ssy5p and Ptr3p components of the SPS amino acid sensor system in Saccharomyces cerevisiae."
Poulsen P., Wu B., Gaber R.F., Kielland-Brandt M.C.
Eukaryot. Cell 4:1116-1124(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION OF FRAMESHIFT, MUTAGENESIS OF GLU-512.
[10]"Regulation of transcription factor latency by receptor-activated proteolysis."
Andreasson C., Heessen S., Ljungdahl P.O.
Genes Dev. 20:1563-1568(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49431 Genomic DNA. Translation: CAA89451.1. Frameshift.
BK006943 Genomic DNA. Translation: DAA08647.1.
PIRS56939.
RefSeqNP_012379.2. NM_001181589.1.

3D structure databases

ProteinModelPortalP47002.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33604. 12 interactions.
DIPDIP-6591N.
STRING4932.YJL156C.

Protein family/group databases

MEROPSS64.001.

Proteomic databases

PaxDbP47002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL156C; YJL156C; YJL156C.
GeneID853285.
KEGGsce:YJL156C.

Organism-specific databases

CYGDYJL156c.
SGDS000003692. SSY5.

Phylogenomic databases

eggNOGNOG45404.
HOGENOMHOG000142023.
OMADQDGAFI.
OrthoDBEOG7BGHVB.

Enzyme and pathway databases

BioCycYEAST:G3O-31596-MONOMER.

Gene expression databases

GenevestigatorP47002.

Family and domain databases

InterProIPR012985. Peptidase_S64_Ssy5.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF08192. Peptidase_S64. 1 hit.
[Graphical view]
PIRSFPIRSF011716. Peptidase_S64_Ssy5. 1 hit.
SUPFAMSSF50494. SSF50494. 2 hits.
ProtoNetSearch...

Other

NextBio973582.

Entry information

Entry nameSSY5_YEAST
AccessionPrimary (citable) accession number: P47002
Secondary accession number(s): D6VW31
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: June 16, 2009
Last modified: June 11, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries