SSY5_YEAST
ID SSY5_YEAST Reviewed; 699 AA.
AC P47002; D6VW31;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=SPS-sensor serine protease component SSY5;
DE AltName: Full=Endoprotease SSY5;
DE Flags: Precursor;
GN Name=SSY5; Synonyms=APF8; OrderedLocusNames=YJL156C; ORFNames=J0570;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 382-399, FUNCTION, AND MUTAGENESIS OF GLU-131; PHE-575;
RP GLN-576; LYS-581 AND PRO-632.
RX PubMed=16524914; DOI=10.1128/ec.5.3.601-608.2006;
RA Poulsen P., Lo Leggio L., Kielland-Brandt M.C.;
RT "Mapping of an internal protease cleavage site in the Ssy5p component of
RT the amino acid sensor of Saccharomyces cerevisiae and functional
RT characterization of the resulting pro- and protease domains by gain-of-
RT function genetics.";
RL Eukaryot. Cell 5:601-608(2006).
RN [4]
RP IDENTIFICATION.
RX PubMed=9483800;
RX DOI=10.1002/(sici)1097-0061(19980130)14:2<103::aid-yea203>3.0.co;2-c;
RA Joergensen M.U., Bruun M.B., Didion T., Kielland-Brandt M.C.;
RT "Mutations in five loci affecting GAP1-independent uptake of neutral amino
RT acids in yeast.";
RL Yeast 14:103-114(1998).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11154269; DOI=10.1128/mcb.21.3.814-826.2001;
RA Forsberg H., Ljungdahl P.O.;
RT "Genetic and biochemical analysis of the yeast plasma membrane Ssy1p-Ptr3p-
RT Ssy5p sensor of extracellular amino acids.";
RL Mol. Cell. Biol. 21:814-826(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH PTR3.
RX PubMed=11489133; DOI=10.1046/j.1365-2958.2001.02538.x;
RA Bernard F., Andre B.;
RT "Genetic analysis of the signalling pathway activated by external amino
RT acids in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 41:489-502(2001).
RN [7]
RP FUNCTION.
RX PubMed=12502738; DOI=10.1101/gad.239202;
RA Andreasson C., Ljungdahl P.O.;
RT "Receptor-mediated endoproteolytic activation of two transcription factors
RT in yeast.";
RL Genes Dev. 16:3158-3172(2002).
RN [8]
RP AUTOCATALYTIC CLEAVAGE, CLEAVAGE OF STP1, AND MUTAGENESIS OF
RP 420-PRO--SER-424 AND SER-640.
RX PubMed=15509782; DOI=10.1128/mcb.24.22.9771-9785.2004;
RA Abdel-Sater F., El Bakkoury M., Urrestarazu A., Vissers S., Andre B.;
RT "Amino acid signaling in yeast: casein kinase I and the Ssy5 endoprotease
RT are key determinants of endoproteolytic activation of the membrane-bound
RT Stp1 transcription factor.";
RL Mol. Cell. Biol. 24:9771-9785(2004).
RN [9]
RP FUNCTION, IDENTIFICATION OF FRAMESHIFT, AND MUTAGENESIS OF GLU-512.
RX PubMed=15947203; DOI=10.1128/ec.4.6.1116-1124.2005;
RA Poulsen P., Wu B., Gaber R.F., Kielland-Brandt M.C.;
RT "Constitutive signal transduction by mutant Ssy5p and Ptr3p components of
RT the SPS amino acid sensor system in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 4:1116-1124(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH STP1.
RX PubMed=16778074; DOI=10.1101/gad.374206;
RA Andreasson C., Heessen S., Ljungdahl P.O.;
RT "Regulation of transcription factor latency by receptor-activated
RT proteolysis.";
RL Genes Dev. 20:1563-1568(2006).
CC -!- FUNCTION: Protease component of the SPS-sensor system, which regulates
CC the expression of several amino acid-metabolizing enzymes and amino
CC acid- and peptide-permeases in response to extracellular amino acid
CC levels by controlling the activity of two transcription factors, STP1
CC and STP2. Catalyzes the activation of these transcription factors,
CC which are synthesized as latent cytoplasmic precursors, by proteolytic
CC removal of an N-terminal inhibitory domain containing cytoplasmic
CC retention motifs. SSY5 binds as an inactive protease complex to STP1.
CC In response to extracellular amino acids and dependent on the other
CC SPS-sensor components, the inhibitory propeptide is induced to
CC dissociate, and thereby enables the catalytic domain to process STP1.
CC {ECO:0000269|PubMed:11154269, ECO:0000269|PubMed:11489133,
CC ECO:0000269|PubMed:12502738, ECO:0000269|PubMed:15947203,
CC ECO:0000269|PubMed:16524914, ECO:0000269|PubMed:16778074}.
CC -!- SUBUNIT: Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino
CC acid sensor complex.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11154269};
CC Peripheral membrane protein {ECO:0000269|PubMed:11154269}; Cytoplasmic
CC side {ECO:0000269|PubMed:11154269}.
CC -!- INDUCTION: Down-regulated after extracellular amino-acid addition.
CC -!- PTM: The propeptide is autoproteolytically cleaved from the catalytic
CC domain but remains associated, forming an inactive protease complex.
CC This processing occurs even in the absence of signaling.
CC {ECO:0000269|PubMed:15509782}.
CC -!- SIMILARITY: Belongs to the peptidase S64 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA89451.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z49431; CAA89451.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006943; DAA08647.1; -; Genomic_DNA.
DR PIR; S56939; S56939.
DR RefSeq; NP_012379.2; NM_001181589.1.
DR AlphaFoldDB; P47002; -.
DR SMR; P47002; -.
DR BioGRID; 33604; 30.
DR DIP; DIP-6591N; -.
DR IntAct; P47002; 1.
DR STRING; 4932.YJL156C; -.
DR MEROPS; S64.001; -.
DR iPTMnet; P47002; -.
DR PaxDb; P47002; -.
DR PRIDE; P47002; -.
DR EnsemblFungi; YJL156C_mRNA; YJL156C; YJL156C.
DR GeneID; 853285; -.
DR KEGG; sce:YJL156C; -.
DR SGD; S000003692; SSY5.
DR VEuPathDB; FungiDB:YJL156C; -.
DR eggNOG; ENOG502QR0D; Eukaryota.
DR HOGENOM; CLU_012881_1_0_1; -.
DR InParanoid; P47002; -.
DR OMA; SYDGEQK; -.
DR BioCyc; YEAST:G3O-31596-MON; -.
DR PRO; PR:P47002; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47002; protein.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:SGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:SGD.
DR GO; GO:0016540; P:protein autoprocessing; IMP:SGD.
DR GO; GO:0016485; P:protein processing; IDA:SGD.
DR GO; GO:0043200; P:response to amino acid; IMP:SGD.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR012985; Peptidase_S64_Ssy5.
DR Pfam; PF08192; Peptidase_S64; 1.
DR PIRSF; PIRSF011716; Peptidase_S64_Ssy5; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Cell membrane; Direct protein sequencing;
KW Hydrolase; Membrane; Protease; Reference proteome; Zymogen.
FT PROPEP 1..381
FT /evidence="ECO:0000269|PubMed:16524914"
FT /id="PRO_0000377374"
FT CHAIN 382..699
FT /note="SPS-sensor serine protease component SSY5"
FT /id="PRO_0000072232"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..699
FT /note="Serine protease"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 545
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 640
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT MUTAGEN 131
FT /note="E->K: In SSY5-13; constitutively active, confers
FT 9.3% increased STP1 processing in the absence of amino
FT acids."
FT /evidence="ECO:0000269|PubMed:16524914"
FT MUTAGEN 420..424
FT /note="Missing: Prevents maturation and amino-acid-induced
FT STP1 cleavage."
FT /evidence="ECO:0000269|PubMed:15509782"
FT MUTAGEN 512
FT /note="E->K: In SSY5-6; constitutively active, confers 30%
FT increased STP1 processing in the absence of amino acids."
FT /evidence="ECO:0000269|PubMed:15947203"
FT MUTAGEN 575
FT /note="F->V: In SSY5-14; constitutively active, confers 30%
FT increased STP1 processing in the absence of amino acids."
FT /evidence="ECO:0000269|PubMed:16524914"
FT MUTAGEN 576
FT /note="Q->P: In SSY5-15; constitutively active, confers 30%
FT increased STP1 processing in the absence of amino acids."
FT /evidence="ECO:0000269|PubMed:16524914"
FT MUTAGEN 581
FT /note="K->N: In SSY5-18; constitutively active, confers
FT 15.5% increased STP1 processing in the absence of amino
FT acids; when associated with H-632."
FT /evidence="ECO:0000269|PubMed:16524914"
FT MUTAGEN 632
FT /note="P->H: In SSY5-18; constitutively active, confers
FT 15.5% increased STP1 processing in the absence of amino
FT acids; when associated with N-581."
FT /evidence="ECO:0000269|PubMed:16524914"
FT MUTAGEN 640
FT /note="S->A: Impairs maturation and amino acid-induced STP1
FT cleavage."
FT /evidence="ECO:0000269|PubMed:15509782"
SQ SEQUENCE 699 AA; 77527 MW; EF982A2717A71741 CRC64;
MVRFFGLNKK KNEEKENTDL PADNEQNAAE TSSSNVSGNE ERIDPNSHDT NPENANNDDA
STTFGSSIQS SSIFSRGRMT YGTGASSSMA TSEMRSHSSG HSGSKNSKNL QGFKDVGKPL
RAVSFLSPVK EEESQDTQNT LDVSSSTSST LATSENAREN SFTSRRSITL EYIHKSLSEL
EENLVDIMDD IHQDVISISK AVIEAIEYFK EFLPTTRDRI PYRISLEKSS SLRKINKIVL
HFLDNLLVSD AFSNSRSILL RRFYFFLKKL NLITDDDLIS ESGVLPCLSV FCIGSHCNLP
SMDKLGMILD ELTKMDSSII SDQEGAFIAP ILRGITPKSS ILTIMFGLPN LQHEHYEMIK
VLYSLFPDVH MYCVKDYIKK AASAVGSIPS HTAATIDTIA PTKFQFSPPY AVSENPLELP
ISMSLSTETS AKITGTLGGY LFPQTGSDKK FSQFASCSFA ITCAHVVLSE KQDYPNVMVP
SNVLQTSYKK VLTKESDRYP DGSVEKTAFL EEVQRIDQNL NWQKSNKFGQ VVWGERAIVD
HRLSDFAIIK VNSSFKCQNT LGNGLKSFPD PTLRFQNLHV KRKIFKMKPG MKVFKIGAST
GYTSGELNST KLVYWADGKL QSSEFVVASP TPLFASAGDS GAWILTKLED RLGLGLVGML
HSYDGEQRQF GLFTPIGDIL ERLHAVTKIQ WDIDPQLDG
