STP1_YEAS7
ID STP1_YEAS7 Reviewed; 519 AA.
AC A6ZZ54;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Transcription factor STP1;
DE Flags: Precursor;
GN Name=STP1; ORFNames=SCY_1343;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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.
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; AAFW02000145; EDN60784.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZZ54; -.
DR TopDownProteomics; A6ZZ54; -.
DR EnsemblFungi; EDN60784; EDN60784; SCY_1343.
DR HOGENOM; CLU_025391_0_0_1; -.
DR Proteomes; UP000007060; 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_0000377647"
FT CHAIN ?..519
FT /note="Transcription factor STP1"
FT /id="PRO_0000377648"
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
