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Protein

SPS-sensor serine protease component SSY5

Gene

SSY5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • serine-type endopeptidase activity Source: SGD

GO - Biological processi

  • protein processing Source: SGD
  • response to amino acid Source: SGD
Complete GO annotation...

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 Componenti: Chromosome X

Organism-specific databases

CYGDiYJL156c.
EuPathDBiFungiDB:YJL156C.
SGDiS000003692. SSY5.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of plasma membrane Source: SGD
Complete GO annotation...

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. 1 Publication
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.
InParanoidiP47002.
OMAiCVKDYIK.
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

        10         20         30         40         50
MVRFFGLNKK KNEEKENTDL PADNEQNAAE TSSSNVSGNE ERIDPNSHDT
60 70 80 90 100
NPENANNDDA STTFGSSIQS SSIFSRGRMT YGTGASSSMA TSEMRSHSSG
110 120 130 140 150
HSGSKNSKNL QGFKDVGKPL RAVSFLSPVK EEESQDTQNT LDVSSSTSST
160 170 180 190 200
LATSENAREN SFTSRRSITL EYIHKSLSEL EENLVDIMDD IHQDVISISK
210 220 230 240 250
AVIEAIEYFK EFLPTTRDRI PYRISLEKSS SLRKINKIVL HFLDNLLVSD
260 270 280 290 300
AFSNSRSILL RRFYFFLKKL NLITDDDLIS ESGVLPCLSV FCIGSHCNLP
310 320 330 340 350
SMDKLGMILD ELTKMDSSII SDQEGAFIAP ILRGITPKSS ILTIMFGLPN
360 370 380 390 400
LQHEHYEMIK VLYSLFPDVH MYCVKDYIKK AASAVGSIPS HTAATIDTIA
410 420 430 440 450
PTKFQFSPPY AVSENPLELP ISMSLSTETS AKITGTLGGY LFPQTGSDKK
460 470 480 490 500
FSQFASCSFA ITCAHVVLSE KQDYPNVMVP SNVLQTSYKK VLTKESDRYP
510 520 530 540 550
DGSVEKTAFL EEVQRIDQNL NWQKSNKFGQ VVWGERAIVD HRLSDFAIIK
560 570 580 590 600
VNSSFKCQNT LGNGLKSFPD PTLRFQNLHV KRKIFKMKPG MKVFKIGAST
610 620 630 640 650
GYTSGELNST KLVYWADGKL QSSEFVVASP TPLFASAGDS GAWILTKLED
660 670 680 690
RLGLGLVGML HSYDGEQRQF GLFTPIGDIL ERLHAVTKIQ WDIDPQLDG
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
Z49431 Genomic DNA. Translation: CAA89451.1. Frameshift.
BK006943 Genomic DNA. Translation: DAA08647.1.
PIRiS56939.
RefSeqiNP_012379.2. NM_001181589.1.

3D structure databases

ProteinModelPortaliP47002.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiS64.001.

Proteomic databases

PaxDbiP47002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYJL156c.
EuPathDBiFungiDB:YJL156C.
SGDiS000003692. SSY5.

Phylogenomic databases

eggNOGiNOG45404.
HOGENOMiHOG000142023.
InParanoidiP47002.
OMAiCVKDYIK.
OrthoDBiEOG7BGHVB.

Enzyme and pathway databases

BioCyciYEAST:G3O-31596-MONOMER.

Miscellaneous databases

NextBioi973582.
PROiP47002.

Gene expression databases

GenevestigatoriP47002.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 94 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.