(data stored in SCRATCH zone)

SWISSPROT: Q757W7_ASHGO

ID   Q757W7_ASHGO            Unreviewed;       669 AA.
AC   Q757W7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=SPS-sensor serine protease component SSY5 {ECO:0000256|PIRNR:PIRNR011716};
DE   AltName: Full=Endoprotease SSY5 {ECO:0000256|PIRNR:PIRNR011716};
GN   ORFNames=AGOS_AEL105W {ECO:0000313|EMBL:AAS52580.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52580.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52580.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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:0000256|PIRNR:PIRNR011716}.
CC   -!- SUBUNIT: Component of the plasma membrane SPS (SSY1-PTR3-SSY5) amino
CC       acid sensor complex. {ECO:0000256|PIRNR:PIRNR011716}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR011716};
CC       Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR011716};
CC       Cytoplasmic side {ECO:0000256|PIRNR:PIRNR011716}.
CC   -!- SIMILARITY: Belongs to the peptidase S64 family.
CC       {ECO:0000256|PIRNR:PIRNR011716}.
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DR   EMBL; AE016818; AAS52580.1; -; Genomic_DNA.
DR   RefSeq; NP_984756.1; NM_210110.1.
DR   STRING; 33169.AAS52580; -.
DR   MEROPS; S64.001; -.
DR   EnsemblFungi; AAS52580; AAS52580; AGOS_AEL105W.
DR   GeneID; 4620945; -.
DR   KEGG; ago:AGOS_AEL105W; -.
DR   HOGENOM; HOG000142023; -.
DR   InParanoid; Q757W7; -.
DR   OMA; EVTNIKW; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0016540; P:protein autoprocessing; IEA:EnsemblFungi.
DR   GO; GO:0043200; P:response to amino acid; IEA:EnsemblFungi.
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   3: Inferred from homology;
DR   PRODOM; Q757W7.
DR   SWISS-2DPAGE; Q757W7.
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR011716};
KW   Membrane {ECO:0000256|PIRNR:PIRNR011716};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..34
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   669 AA;  74233 MW;  D76982F48EDE9D4E CRC64;
     MVRGLFGFGK RSGQDRNREP ERRKCDEEDM LGEDPKQPIL LSGKTCESVQ SSSIFSRGLR
     TCGTDISTSG AFSESGARVD KDIGKPLRVT GVGTALGTVA EHEEGSQTLG LVPSGTDSTG
     DAYEETHPDR RGAGQLETEL QELGDKLDSV MDEIVQNVTN VSKAVIQAIE HFKNFLEQAE
     GCHYGVSTEH SAAFRRITKI VLHFQDNLLQ SDVFSNSRAI LLRWYIKFLT SLNLEVHDLP
     PADVKRMPLP SLKIYAIGQD CNLPNRDKIS TIIEEIAGAN DSSISDQEGA FIAPVLRGLD
     KNSAILTILF GFPRPQQAHY EMVKVLYSLF RDVHFYCVKD YITPCAANVA PNVVPSSIPM
     QAFSPQRTQF IPPYTLPSDV MAPPMSMSLS SEDSVSMTGT LGGYLFPQIP ESEEHLSGFA
     GAAFGITCAH VVLTESQDHP YVSVPSRVLQ NIYKKTLKEE LTRYPEGSIE RLSFEDEISR
     IEQNLEWQQE NKFGQVVWGE RSIVKQKLSD FAIIKLNPKI RCRNYLGDDL SGIPDPVLRF
     KNLYVRKKLM TLRPGLEVFK VGASSKYTRG TVNGSKIVYW ADGKIQSTEF VISSPQPFFA
     TGGDSGAWLL TKLDDELGLG VVGMLHSYDG EQKQFGLYTP IADILERLHD VTGVIWDIDQ
     PPELSKYID
//

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