STP2_YEAST
ID STP2_YEAST Reviewed; 541 AA.
AC P38704; D3DKV0; E9P956;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Transcription factor STP2;
DE Flags: Precursor;
GN Name=STP2; OrderedLocusNames=YHR006W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP DOMAIN ATYPICAL ZINC-FINGER.
RX PubMed=9171100; DOI=10.1093/nar/25.12.2464;
RA Boehm S., Frishman D., Mewes H.-W.;
RT "Variations of the C2H2 zinc finger motif in the yeast genome and
RT classification of yeast zinc finger proteins.";
RL Nucleic Acids Res. 25:2464-2469(1997).
RN [5]
RP FUNCTION IN TRANSCRIPTION REGULATION.
RX PubMed=10648791; DOI=10.1093/nar/28.4.974;
RA de Boer M., Nielsen P.S., Bebelman J.-P., Heerikhuizen H., Andersen H.A.,
RA Planta R.J.;
RT "Stp1p, Stp2p and Abf1p are involved in regulation of expression of the
RT amino acid transporter gene BAP3 of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 28:974-981(2000).
RN [6]
RP DNA-BINDING.
RX PubMed=11212916; DOI=10.1007/s004380000347;
RA Nielsen P.S., van den Hazel B., Didion T., de Boer M., Joergensen M.U.,
RA Planta R.J., Kielland-Brandt M.C., Andersen H.A.;
RT "Transcriptional regulation of the Saccharomyces cerevisiae amino acid
RT permease gene BAP2.";
RL Mol. Gen. Genet. 264:613-622(2001).
RN [7]
RP PROTEOLYTIC PROCESSING, MUTAGENESIS OF 2-PRO--PHE-74, AND SUBCELLULAR
RP LOCATION.
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP DOMAIN.
RX PubMed=15314160; DOI=10.1128/mcb.24.17.7503-7513.2004;
RA Andreasson C., Ljungdahl P.O.;
RT "The N-terminal regulatory domain of Stp1p is modular and, fused to an
RT artificial transcription factor, confers full Ssy1p-Ptr3p-Ssy5p sensor
RT control.";
RL Mol. Cell. Biol. 24:7503-7513(2004).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15197729; DOI=10.1002/yea.1120;
RA Eckert-Boulet N., Nielsen P.S., Friis C., dos Santos M.M., Nielsen J.,
RA Kielland-Brandt M.C., Regenberg B.;
RT "Transcriptional profiling of extracellular amino acid sensing in
RT Saccharomyces cerevisiae and the role of Stp1p and Stp2p.";
RL Yeast 21:635-648(2004).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16735580; DOI=10.1083/jcb.200601011;
RA Boban M., Zargari A., Andreasson C., Heessen S., Thyberg J.,
RA Ljungdahl P.O.;
RT "Asi1 is an inner nuclear membrane protein that restricts promoter access
RT of two latent transcription factors.";
RL J. Cell Biol. 173:695-707(2006).
RN [13]
RP FUNCTION.
RX PubMed=17085444; DOI=10.1074/jbc.m609201200;
RA Zargari A., Boban M., Heessen S., Andreasson C., Thyberg J.,
RA Ljungdahl P.O.;
RT "Inner nuclear membrane proteins Asi1, Asi2, and Asi3 function in concert
RT to maintain the latent properties of transcription factors Stp1 and Stp2.";
RL J. Biol. Chem. 282:594-605(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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 BAP2 and BAP3. Binding to promoters is facilitated
CC by DAL81 (By similarity). Involved in the repression of genes subject
CC to nitrogen catabolite repression and genes involved in stress
CC response. Negatively regulated by inner nuclear membrane proteins ASI1,
CC ASI2 and ASI3, which prevent unprocessed precursor forms that escape
CC cytoplasmic anchoring from inducing SPS-sensor-regulated genes.
CC {ECO:0000250, ECO:0000269|PubMed:10648791, ECO:0000269|PubMed:15197729,
CC ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:17085444}.
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:0000269|PubMed:12502738, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15197729, ECO:0000269|PubMed:16735580}.
CC Note=Localizes to the cytoplasm in its unprocessed form and is targeted
CC to the nucleus after proteolytic processing upon induction by amino
CC acids.
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 (By similarity). Region I is also
CC required for ASI1/2/3-mediated negative regulation of transcription.
CC {ECO:0000250, ECO:0000269|PubMed:15314160, ECO:0000269|PubMed:9171100}.
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}.
CC -!- MISCELLANEOUS: Present with 6490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U10555; AAB68423.1; -; Genomic_DNA.
DR EMBL; AY723821; AAU09738.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06694.1; -; Genomic_DNA.
DR PIR; S46794; S46794.
DR RefSeq; NP_011870.1; NM_001179136.1.
DR AlphaFoldDB; P38704; -.
DR BioGRID; 36433; 109.
DR IntAct; P38704; 5.
DR MINT; P38704; -.
DR STRING; 4932.YHR006W; -.
DR iPTMnet; P38704; -.
DR MaxQB; P38704; -.
DR PaxDb; P38704; -.
DR PRIDE; P38704; -.
DR EnsemblFungi; YHR006W_mRNA; YHR006W; YHR006W.
DR GeneID; 856397; -.
DR KEGG; sce:YHR006W; -.
DR SGD; S000001048; STP2.
DR VEuPathDB; FungiDB:YHR006W; -.
DR eggNOG; ENOG502S1NP; Eukaryota.
DR HOGENOM; CLU_025391_1_0_1; -.
DR InParanoid; P38704; -.
DR OMA; HIEAGSC; -.
DR BioCyc; YEAST:G3O-31071-MON; -.
DR PRO; PR:P38704; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38704; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell membrane; DNA-binding; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc; Zinc-finger; Zymogen.
FT PROPEP 1..?
FT /id="PRO_0000377649"
FT CHAIN ?..541
FT /note="Transcription factor STP2"
FT /id="PRO_0000046854"
FT ZN_FING 204..226
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 232..267
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..309
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 13..32
FT /note="I"
FT REGION 35..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..105
FT /note="II"
FT REGION 452..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 2..74
FT /note="Missing: Dominant active transcription factor."
FT /evidence="ECO:0000269|PubMed:12502738"
FT CONFLICT 101
FT /note="E -> G (in Ref. 3; AAU09738)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 60792 MW; BAF84576CE07180C CRC64;
MPILSLSSTR NSVLTRIYDY LKALVQQVIV PNVEDDKSSK STPFEKLEPA KQNHPQKDCC
ATEKDDLVDV SELFPKQNNK QLSLTSKSSV VPCALNLDNL ETPFSIKIDN NGAVTTQLNL
DEPILRGPSR GEPAKLQNDL ISSPPLEESY INNDQYKALF PSNFLPITPV SSVITPASKK
SIDESPLSDE VQGIADESSE TLPYICHYCD ARFRIRGYLT RHIKKHAKRK AYHCPFFDNS
ISQELRCHTS GGFSRRDTYK THLKSRHFTY PEGVKPQDRN KSPGVCTQCG EHFSTSESWV
ENHIEAGSCK GLPEGYSEGI REKKKTSKMK MIKTSDGQTR FISSDESVSE PALQNKNCIE
ATVMQSKERP NDKIIPTKTE KNDFGIGTQW FERKQISRPT QTTQSRGPTE VQNLKEWSII
SPPILSPQNA SSVPQEYQSS RYTLHMDSPA LSSASSALSP LSGDPITTTE TNKSYPLDSE
QSLLEPDKTE EDAINQSKES NMISINEMLQ KQMDFELLGE NHLKETQDYL ALYKKAYGIE
F
