SKN7_YEAST
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 03-AUG-2022, entry version 187.
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; 273.
DR DIP; DIP-2403N; -.
DR IntAct; P38889; 8.
DR STRING; 4932.YHR206W; -.
DR ChEMBL; CHEMBL2146314; -.
DR iPTMnet; P38889; -.
DR MaxQB; P38889; -.
DR PaxDb; P38889; -.
DR PRIDE; P38889; -.
DR EnsemblFungi; YHR206W_mRNA; YHR206W; YHR206W.
DR GeneID; 856613; -.
DR KEGG; sce:YHR206W; -.
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; DQVCARI; -.
DR BioCyc; YEAST:G3O-31232-MON; -.
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 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:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:SGD.
DR GO; GO:0000304; P:response to singlet oxygen; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR014402; Sig_transdc_resp-reg_Skn7.
DR InterPro; IPR027718; TF_Skn7.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 2.
DR PANTHER; PTHR10015:SF361; PTHR10015:SF361; 2.
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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52172; SSF52172; 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
