Reviewed, UniProtKB/Swiss-Prot P47002 (SSY5_YEAST)

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	699 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.2 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9
Subunit structure	Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor complex.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side.
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.7
Sequence similarities	Belongs to the peptidase S64 family.
Sequence caution	The sequence CAA89451.1 differs from that shown. Reason: Frameshift at position 685.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Molecular function	Hydrolase Protease
PTM	Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein processing Ref.2 Ref.9 Inferred from direct assay. Source: SGD response to amino acid stimulus Ref.4 Inferred from genetic interaction. Source: SGD
Cellular component	extrinsic to plasma membrane Ref.4 Inferred from direct assay. Source: SGD
Molecular function	serine-type endopeptidase activity Ref.2 Ref.9 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 381	381			PRO_0000377374
	Chain	382 – 699	318	SPS-sensor serine protease component SSY5		PRO_0000072232
Regions
	Region	459 – 699	241	Serine protease
Sites
	Active site	465	1	Charge relay system Potential
	Active site	545	1	Charge relay system Potential
	Active site	640	1	Charge relay system Potential
Experimental info
	Mutagenesis	131	1	E → K in SSY5-13; constitutively active, confers 9.3% increased STP1 processing in the absence of amino-acids. Ref.2
	Mutagenesis	420 – 424	5	Missing: Prevents maturation and amino-acid-induced STP1 cleavage.
	Mutagenesis	512	1	E → K in SSY5-6; constitutively active, confers 30% increased STP1 processing in the absence of amino-acids. Ref.8
	Mutagenesis	575	1	F → V in SSY5-14; constitutively active, confers 30% increased STP1 processing in the absence of amino-acids. Ref.2
	Mutagenesis	576	1	Q → P in SSY5-15; constitutively active, confers 30% increased STP1 processing in the absence of amino-acids. Ref.2
	Mutagenesis	581	1	K → N in SSY5-18; constitutively active, confers 15.5% increased STP1 processing in the absence of amino-acids; when associated with H-632. Ref.2
	Mutagenesis	632	1	P → H in SSY5-18; constitutively active, confers 15.5% increased STP1 processing in the absence of amino-acids; when associated with N-581. Ref.2
	Mutagenesis	640	1	S → A: Impairs maturation and amino-acid-induced STP1 cleavage. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P47002-1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: EF982A2717A71741	FASTA	699	77,527
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"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: 16524914] [Abstract] Cited for: PROTEIN SEQUENCE OF 382-399, FUNCTION, MUTAGENESIS OF GLU-131; PHE-575; GLN-576; LYS-581 AND PRO-632.
[3]	"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: 9483800] [Abstract] Cited for: IDENTIFICATION.
[4]	"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: 11154269] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]	"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: 11489133] [Abstract] Cited for: FUNCTION, INTERACTION WITH PTR3.
[6]	"Receptor-mediated endoproteolytic activation of two transcription factors in yeast." Andreasson C., Ljungdahl P.O. Genes Dev. 16:3158-3172(2002) [PubMed: 12502738] [Abstract] Cited for: FUNCTION.
[7]	"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: 15509782] [Abstract] Cited for: AUTOPROTEOLYTIC MATURATION, CLEAVAGE OF STP1, MUTAGENESIS OF 420-PRO--SER-424 AND SER-640.
[8]	"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: 15947203] [Abstract] Cited for: FUNCTION, IDENTIFICATION OF FRAMESHIFT, MUTAGENESIS OF GLU-512.
[9]	"Regulation of transcription factor latency by receptor-activated proteolysis." Andreasson C., Heessen S., Ljungdahl P.O. Genes Dev. 20:1563-1568(2006) [PubMed: 16778074] [Abstract] Cited for: FUNCTION, INTERACTION WITH STP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49431 Genomic DNA. Translation: CAA89451.1. Frameshift.
PIR	S56939.
RefSeq	NP_012379.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6591N.
STRING	P47002.
Protein family/group databases
MEROPS	S64.001.
Genome annotation databases
Ensembl	YJL156C; YJL156C; YJL156C; Saccharomyces cerevisiae. [Genome view]
GeneID	853285.
KEGG	sce:YJL156C.
NMPDR	fig|4932.3.peg.3344.
Organism-specific databases
CYGD	YJL156c.
SGD	S000003692. SSY5.
Phylogenomic databases
HOGENOM	P47002.
OrthoDB	EOG9SN34W
Gene expression databases
ArrayExpress	P47002.
Genevestigator	P47002.
GermOnline	YJL156C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR009003. Ser/Cys_Pept_Trypsin-like. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	973582.

Entry information

Entry name

SSY5_YEAST

Accession

Primary (citable) accession number: P47002

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	June 16, 2009
Last modified:	November 24, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)