ID   STP1_YEAS1              Reviewed;         519 AA.
AC   B3LFK1;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Transcription factor STP1;
DE   Flags: Precursor;
GN   Name=STP1; ORFNames=SCRG_00076;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor involved in the regulation of gene
CC       expression in response to extracellular amino acid levels. Synthesized
CC       as latent cytoplasmic precursor, which, upon a signal initiated by the
CC       plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system, becomes
CC       proteolytically activated and relocates to the nucleus, where it
CC       induces the expression of SPS-sensor-regulated genes, including the
CC       amino-acid permeases AGP1, BAP2, BAP3 and GNP1. Binding to promoters is
CC       facilitated by DAL81. Involved in the repression of genes subject to
CC       nitrogen catabolite repression and genes involved in stress response.
CC       Negatively regulated by inner nuclear membrane proteins ASI1, ASI2 and
CC       ASI3, which prevent unprocessed precursor forms that escape cytoplasmic
CC       anchoring from inducing SPS-sensor-regulated genes. May be involved in
CC       pre-tRNA splicing (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via Region II) with SSY5; protease component of the
CC       SPS-sensor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Localizes to the cytoplasm in its unprocessed form
CC       and is targeted to the nucleus after proteolytic processing upon
CC       induction by amino acids. The SCF(MET30) ubiquitin ligase complex
CC       negatively regulates nuclear accumulation of the processed form in the
CC       absence of high extracellular methionine levels (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal inhibitory domain contains conserved sequence
CC       elements important for cytoplasmic retention (Region I) and proteolytic
CC       processing (Region II) of the protein. Region I is also required for
CC       ASI1/2/3-mediated negative regulation of transcription (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by casein kinase I. Phosphorylation is not
CC       dependent on the extracellular amino acid levels, but is a prerequisite
CC       for proteolytic processing (By similarity). {ECO:0000250}.
CC   -!- PTM: Activated by the amino acid-induced proteolytic removal of an N-
CC       terminal inhibitory domain by serine protease SSY5, an intrinsic
CC       component of the SPS-sensor. Processing requires at least 2 components
CC       of the SCF(GRR1) ubiquitin ligase complex, namely the F-box protein
CC       GRR1 and the E2 enzyme CDC34, but does not depend on the proteasome.
CC       Processing is negatively regulated by the protein phosphatase 2A
CC       regulatory subunit RTS1 (By similarity). {ECO:0000250}.
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DR   EMBL; CH408043; EDV07880.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LFK1; -.
DR   PRIDE; B3LFK1; -.
DR   EnsemblFungi; EDV07880; EDV07880; SCRG_00076.
DR   HOGENOM; CLU_025391_0_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; DNA-binding; Membrane; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; tRNA processing; Zinc; Zinc-finger; Zymogen.
FT   PROPEP          1..?
FT                   /id="PRO_0000377643"
FT   CHAIN           ?..519
FT                   /note="Transcription factor STP1"
FT                   /id="PRO_0000377644"
FT   ZN_FING         160..182
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         188..223
FT                   /note="C2H2-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         240..265
FT                   /note="C2H2-type 3; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          16..35
FT                   /note="I"
FT   REGION          47..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..97
FT                   /note="II"
FT   REGION          115..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  58088 MW;  F95987994B74FA47 CRC64;
     MPSTTLLFPQ KHIRAIPGKI YAFFRELVSG VIISKPDLSH HYSCENATKE EGKDAADEEK
     TTTSLFPESN NIDRSLNGGC SVIPCSMDVS DLNTPISITL SPENRIKSEV NAKSLLGSRP
     EQDTGAPIKM STGVTSSPLS PSGSTPEHST KVLNNGEEEF ICHYCDATFR IRGYLTRHIK
     KHAIEKAYHC PFFNSATPPD LRCHNSGGFS RRDTYKTHLK ARHVLYPKGV KPQDRNKSSG
     HCAQCGEYFS TIENFVENHI ESGDCKALPQ GYTKKNEKRS GKLRKIKTSN GHSRFISTSQ
     SVVEPKVLFN KDAVEAMTIV ANNSSGNDII SKYGNNKLML NSENFKVDIP KRKRKYIKKK
     QQQVSGSTVT TPEVATQNNQ EVAPDEISSA TIFSPFDTHL LEPVPSSSSE SSAEVMFHGK
     QMKNFLIDIN SFTNQQQQAQ DNPSFLPLDI EQSSYDLSED AMSYPIISTQ SNRDCTQYDN
     TKISQILQSQ LNPEYLSENH MRETQQYLNF YNDNFGSQF