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P47002

- SSY5_YEAST

UniProt

P47002 - SSY5_YEAST

Protein

SPS-sensor serine protease component SSY5

Gene

SSY5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    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 STP1.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei465 – 4651Charge relay systemSequence Analysis
    Active sitei545 – 5451Charge relay systemSequence Analysis
    Active sitei640 – 6401Charge relay systemSequence Analysis

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: SGD

    GO - Biological processi

    1. protein processing Source: SGD
    2. response to amino acid Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31596-MONOMER.

    Protein family/group databases

    MEROPSiS64.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SPS-sensor serine protease component SSY5
    Alternative name(s):
    Endoprotease SSY5
    Gene namesi
    Name:SSY5
    Synonyms:APF8
    Ordered Locus Names:YJL156C
    ORF Names:J0570
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL156c.
    SGDiS000003692. SSY5.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

    GO - Cellular componenti

    1. extrinsic component of plasma membrane Source: SGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1311E → K in SSY5-13; constitutively active, confers 9.3% increased STP1 processing in the absence of amino acids. 1 Publication
    Mutagenesisi420 – 4245Missing: Prevents maturation and amino-acid-induced STP1 cleavage.
    Mutagenesisi512 – 5121E → K in SSY5-6; constitutively active, confers 30% increased STP1 processing in the absence of amino acids. 1 Publication
    Mutagenesisi575 – 5751F → V in SSY5-14; constitutively active, confers 30% increased STP1 processing in the absence of amino acids. 1 Publication
    Mutagenesisi576 – 5761Q → P in SSY5-15; constitutively active, confers 30% increased STP1 processing in the absence of amino acids. 1 Publication
    Mutagenesisi581 – 5811K → N in SSY5-18; constitutively active, confers 15.5% increased STP1 processing in the absence of amino acids; when associated with H-632. 1 Publication
    Mutagenesisi632 – 6321P → H in SSY5-18; constitutively active, confers 15.5% increased STP1 processing in the absence of amino acids; when associated with N-581. 1 Publication
    Mutagenesisi640 – 6401S → A: Impairs maturation and amino acid-induced STP1 cleavage. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 3813811 PublicationPRO_0000377374Add
    BLAST
    Chaini382 – 699318SPS-sensor serine protease component SSY5PRO_0000072232Add
    BLAST

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Autocatalytic cleavage, Zymogen

    Proteomic databases

    PaxDbiP47002.

    Expressioni

    Inductioni

    Down-regulated after extracellular amino-acid addition.

    Gene expression databases

    GenevestigatoriP47002.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi33604. 12 interactions.
    DIPiDIP-6591N.
    STRINGi4932.YJL156C.

    Structurei

    3D structure databases

    ProteinModelPortaliP47002.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni459 – 699241Serine proteaseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S64 family.Curated

    Phylogenomic databases

    eggNOGiNOG45404.
    HOGENOMiHOG000142023.
    OMAiDQDGAFI.
    OrthoDBiEOG7BGHVB.

    Family and domain databases

    InterProiIPR012985. Peptidase_S64_Ssy5.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF08192. Peptidase_S64. 1 hit.
    [Graphical view]
    PIRSFiPIRSF011716. Peptidase_S64_Ssy5. 1 hit.
    SUPFAMiSSF50494. SSF50494. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P47002-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRFFGLNKK KNEEKENTDL PADNEQNAAE TSSSNVSGNE ERIDPNSHDT    50
    NPENANNDDA STTFGSSIQS SSIFSRGRMT YGTGASSSMA TSEMRSHSSG 100
    HSGSKNSKNL QGFKDVGKPL RAVSFLSPVK EEESQDTQNT LDVSSSTSST 150
    LATSENAREN SFTSRRSITL EYIHKSLSEL EENLVDIMDD IHQDVISISK 200
    AVIEAIEYFK EFLPTTRDRI PYRISLEKSS SLRKINKIVL HFLDNLLVSD 250
    AFSNSRSILL RRFYFFLKKL NLITDDDLIS ESGVLPCLSV FCIGSHCNLP 300
    SMDKLGMILD ELTKMDSSII SDQEGAFIAP ILRGITPKSS ILTIMFGLPN 350
    LQHEHYEMIK VLYSLFPDVH MYCVKDYIKK AASAVGSIPS HTAATIDTIA 400
    PTKFQFSPPY AVSENPLELP ISMSLSTETS AKITGTLGGY LFPQTGSDKK 450
    FSQFASCSFA ITCAHVVLSE KQDYPNVMVP SNVLQTSYKK VLTKESDRYP 500
    DGSVEKTAFL EEVQRIDQNL NWQKSNKFGQ VVWGERAIVD HRLSDFAIIK 550
    VNSSFKCQNT LGNGLKSFPD PTLRFQNLHV KRKIFKMKPG MKVFKIGAST 600
    GYTSGELNST KLVYWADGKL QSSEFVVASP TPLFASAGDS GAWILTKLED 650
    RLGLGLVGML HSYDGEQRQF GLFTPIGDIL ERLHAVTKIQ WDIDPQLDG 699
    Length:699
    Mass (Da):77,527
    Last modified:June 16, 2009 - v2
    Checksum:iEF982A2717A71741
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49431 Genomic DNA. Translation: CAA89451.1. Frameshift.
    BK006943 Genomic DNA. Translation: DAA08647.1.
    PIRiS56939.
    RefSeqiNP_012379.2. NM_001181589.1.

    Genome annotation databases

    EnsemblFungiiYJL156C; YJL156C; YJL156C.
    GeneIDi853285.
    KEGGisce:YJL156C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49431 Genomic DNA. Translation: CAA89451.1 . Frameshift.
    BK006943 Genomic DNA. Translation: DAA08647.1 .
    PIRi S56939.
    RefSeqi NP_012379.2. NM_001181589.1.

    3D structure databases

    ProteinModelPortali P47002.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33604. 12 interactions.
    DIPi DIP-6591N.
    STRINGi 4932.YJL156C.

    Protein family/group databases

    MEROPSi S64.001.

    Proteomic databases

    PaxDbi P47002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL156C ; YJL156C ; YJL156C .
    GeneIDi 853285.
    KEGGi sce:YJL156C.

    Organism-specific databases

    CYGDi YJL156c.
    SGDi S000003692. SSY5.

    Phylogenomic databases

    eggNOGi NOG45404.
    HOGENOMi HOG000142023.
    OMAi DQDGAFI.
    OrthoDBi EOG7BGHVB.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31596-MONOMER.

    Miscellaneous databases

    NextBioi 973582.

    Gene expression databases

    Genevestigatori P47002.

    Family and domain databases

    InterProi IPR012985. Peptidase_S64_Ssy5.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF08192. Peptidase_S64. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF011716. Peptidase_S64_Ssy5. 1 hit.
    SUPFAMi SSF50494. SSF50494. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiSSY5_YEAST
    AccessioniPrimary (citable) accession number: P47002
    Secondary accession number(s): D6VW31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3