ID   SKN7_YEAST              Reviewed;         622 AA.
AC   P38889; D3DLF5; E9P959; P39747;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Transcription factor SKN7;
DE   AltName: Full=Peroxide sensitivity protein 9;
GN   Name=SKN7; Synonyms=BRY1, POS9; OrderedLocusNames=YHR206W;
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.
RX   PubMed=8226633; DOI=10.1128/jb.175.21.6908-6915.1993;
RA   Brown J.L., North S., Bussey H.;
RT   "SKN7, a yeast multicopy suppressor of a mutation affecting cell wall beta-
RT   glucan assembly, encodes a product with domains homologous to prokaryotic
RT   two-component regulators and to heat shock transcription factors.";
RL   J. Bacteriol. 175:6908-6915(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF ASP-427.
RX   PubMed=8598053; DOI=10.1007/bf02208613;
RA   Krems B., Charizanis C., Entian K.-D.;
RT   "The response regulator-like protein Pos9/Skn7 of Saccharomyces cerevisiae
RT   is involved in oxidative stress resistance.";
RL   Curr. Genet. 29:327-334(1996).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   FUNCTION, AND MUTAGENESIS OF ASP-427.
RX   PubMed=7957083; DOI=10.1002/j.1460-2075.1994.tb06849.x;
RA   Brown J.L., Bussey H., Stewart R.C.;
RT   "Yeast Skn7p functions in a eukaryotic two-component regulatory pathway.";
RL   EMBO J. 13:5186-5194(1994).
RN   [7]
RP   FUNCTION, AND PHOSPHORYLATION AT ASP-427.
RX   PubMed=9843501; DOI=10.1093/emboj/17.23.6952;
RA   Li S., Ault A., Malone C.L., Raitt D., Dean S., Johnston L.H.,
RA   Deschenes R.J., Fassler J.S.;
RT   "The yeast histidine protein kinase, Sln1p, mediates phosphotransfer to two
RT   response regulators, Ssk1p and Skn7p.";
RL   EMBO J. 17:6952-6962(1998).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10888672; DOI=10.1091/mbc.11.7.2335;
RA   Raitt D.C., Johnson A.L., Erkine A.M., Makino K., Morgan B., Gross D.S.,
RA   Johnston L.H.;
RT   "The Skn7 response regulator of Saccharomyces cerevisiae interacts with
RT   Hsf1 in vivo and is required for the induction of heat shock genes by
RT   oxidative stress.";
RL   Mol. Biol. Cell 11:2335-2347(2000).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14665464; DOI=10.1128/ec.2.6.1304-1314.2003;
RA   Lu J.M.-Y., Deschenes R.J., Fassler J.S.;
RT   "Saccharomyces cerevisiae histidine phosphotransferase Ypd1p shuttles
RT   between the nucleus and cytoplasm for SLN1-dependent phosphorylation of
RT   Ssk1p and Skn7p.";
RL   Eukaryot. Cell 2:1304-1314(2003).
RN   [10]
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   [11]
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 that is part of a SLN1-YPD1-SKN7 two-
CC       component regulatory system, which controls gene expression in response
CC       to changes in the osmolarity of the extracellular environment. Under
CC       low osmotic conditions, phosphorylated and activated by the
CC       phosphorelay intermediate protein YPD1. Also activated in response to
CC       oxidative stress, independent on the two-component regulatory system.
CC       Regulates heat shock genes in response to oxidative stress and genes
CC       involved in cell wall integrity in response to osmotic changes.
CC       {ECO:0000269|PubMed:10888672, ECO:0000269|PubMed:7957083,
CC       ECO:0000269|PubMed:8598053, ECO:0000269|PubMed:9843501}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:G0SB31}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10888672,
CC       ECO:0000269|PubMed:14665464}.
CC   -!- DOMAIN: Homotrimerization occurs through formation of a three-stranded
CC       coiled-coil structure generated by intermolecular interactions between
CC       HR-A/B regions allowing DNA-binding activity.
CC       {ECO:0000250|UniProtKB:G0SB31}.
CC   -!- PTM: The phosphorelay mechanism involves the sequential transfer of a
CC       phosphate group from 'His-576' (H1) to 'Asp-1144' (D1) of SLN1, then to
CC       'His-64' (H2) of YPD1 and finally to Asp-427 (D2) of SKN7.
CC   -!- MISCELLANEOUS: Present with 2570 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SKN7 family. {ECO:0000305}.
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DR   EMBL; U00485; AAC48911.1; -; Unassigned_DNA.
DR   EMBL; X83031; CAA58143.1; -; Genomic_DNA.
DR   EMBL; U00029; AAB69734.1; -; Genomic_DNA.
DR   EMBL; AY723828; AAU09745.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06899.1; -; Genomic_DNA.
DR   PIR; A49344; A49344.
DR   RefSeq; NP_012076.3; NM_001179337.3.
DR   AlphaFoldDB; P38889; -.
DR   SMR; P38889; -.
DR   BioGRID; 36640; 281.
DR   DIP; DIP-2403N; -.
DR   IntAct; P38889; 8.
DR   STRING; 4932.YHR206W; -.
DR   ChEMBL; CHEMBL2146314; -.
DR   iPTMnet; P38889; -.
DR   MaxQB; P38889; -.
DR   PaxDb; 4932-YHR206W; -.
DR   PeptideAtlas; P38889; -.
DR   EnsemblFungi; YHR206W_mRNA; YHR206W; YHR206W.
DR   GeneID; 856613; -.
DR   KEGG; sce:YHR206W; -.
DR   AGR; SGD:S000001249; -.
DR   SGD; S000001249; SKN7.
DR   VEuPathDB; FungiDB:YHR206W; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_008776_3_0_1; -.
DR   InParanoid; P38889; -.
DR   OMA; NWQSPGQ; -.
DR   OrthoDB; 1117127at2759; -.
DR   BioCyc; YEAST:G3O-31232-MONOMER; -.
DR   Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-SCE-3371511; HSF1 activation.
DR   Reactome; R-SCE-3371568; Attenuation phase.
DR   Reactome; R-SCE-3371571; HSF1-dependent transactivation.
DR   BioGRID-ORCS; 856613; 6 hits in 13 CRISPR screens.
DR   PRO; PR:P38889; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38889; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IDA:SGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0008361; P:regulation of cell size; IMP:SGD.
DR   GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0000304; P:response to singlet oxygen; IMP:SGD.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:SGD.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR000232; HSF_DNA-bd.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR014402; Sig_transdc_resp-reg_Skn7.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00447; HSF_DNA-bind; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF002595; RR_SKN7; 1.
DR   PRINTS; PR00056; HSFDOMAIN.
DR   SMART; SM00415; HSF; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00434; HSF_DOMAIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..622
FT                   /note="Transcription factor SKN7"
FT                   /id="PRO_0000081404"
FT   DOMAIN          378..492
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..190
FT                   /note="DNA-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:G0SB31"
FT   REGION          212..303
FT                   /note="Hydrophobic repeat HR-A/B"
FT                   /evidence="ECO:0000250|UniProtKB:G0SB31"
FT   REGION          501..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          240..260
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        502..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         427
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT                   ECO:0000269|PubMed:9843501"
FT   MUTAGEN         427
FT                   /note="D->A: No activity."
FT                   /evidence="ECO:0000269|PubMed:7957083,
FT                   ECO:0000269|PubMed:8598053"
FT   MUTAGEN         427
FT                   /note="D->E: Augments activity."
FT                   /evidence="ECO:0000269|PubMed:7957083,
FT                   ECO:0000269|PubMed:8598053"
FT   MUTAGEN         427
FT                   /note="D->N: Diminishes activity."
FT                   /evidence="ECO:0000269|PubMed:7957083,
FT                   ECO:0000269|PubMed:8598053"
FT   MUTAGEN         427
FT                   /note="D->R: No activity."
FT                   /evidence="ECO:0000269|PubMed:7957083,
FT                   ECO:0000269|PubMed:8598053"
FT   CONFLICT        45
FT                   /note="T -> A (in Ref. 5; AAU09745)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   622 AA;  69202 MW;  4C732FD66E326742 CRC64;
     MSFSTINSNV NKTTGDSNNN TTENSSTADL LGMDLLQSGP RLMNTMQPNN SSDMLHINNK
     TNNVQQPAGN TNISSANAGA KAPANEFVRK LFRILENNEY PDIVTWTENG KSFVVLDTGK
     FTTHILPNHF KHSNFASFVR QLNKYDFHKV KRSPEERQRC KYGEQSWEFQ HPEFRVHYGK
     GLDNIKRKIP AQRKVLLDES QKALLHFNSE GTNPNNPSGS LLNESTTELL LSNTVSKDAF
     GNLRRRVDKL QKELDMSKME SYATKVELQK LNSKYNTVIE SLITFKTINE NLLNNFNTLC
     STLANNGIEV PIFGDNGNRN PTGNTNPATT TAIQSNNNTN NASPATSTVS LQLPNLPDQN
     SLTPNAQNNT VTLRKGFHVL LVEDDAVSIQ LCSKFLRKYG CTVQVVSDGL SAISTLEKYR
     YDLVLMDIVM PNLDGATATS IVRSFDNETP IIAMTGNIMN QDLITYLQHG MNDILAKPFT
     RDDLHSILIR YLKDRIPLCE QQLPPRNSSP QTHSNTNTAN SNPNTINEQS LAMLPQDNPS
     TTTPVTPGAS ISSAQHVQQG QQEQQHQIFH AQQQQQHHNA IANARSDVAI PNLEHEINTV
     PHSSMGSTPQ LPQSTLQENQ LS
//