SKN7_CANAL
ID SKN7_CANAL Reviewed; 559 AA.
AC Q5A4X5; A0A1D8PMV6;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transcription factor SKN7;
GN Name=SKN7; OrderedLocusNames=CAALFM_C500240WA;
GN ORFNames=CaO19.8586, CaO19.971;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=15039366; DOI=10.1128/iai.72.4.2390-2394.2004;
RA Singh P., Chauhan N., Ghosh A., Dixon F., Calderone R.;
RT "SKN7 of Candida albicans: mutant construction and phenotype analysis.";
RL Infect. Immun. 72:2390-2394(2004).
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:0000250|UniProtKB:P38889}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:G0SB31}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38889}.
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: Phosphorylated by the phosphorelay intermediate protein YPD1.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Leads to sensitivity to H(2)O(2) in vitro, but
CC only mildly attenuated virulence. {ECO:0000269|PubMed:15039366}.
CC -!- SIMILARITY: Belongs to the SKN7 family. {ECO:0000305}.
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DR EMBL; CP017627; AOW29470.1; -; Genomic_DNA.
DR RefSeq; XP_716809.1; XM_711716.1.
DR AlphaFoldDB; Q5A4X5; -.
DR SMR; Q5A4X5; -.
DR STRING; 237561.Q5A4X5; -.
DR PRIDE; Q5A4X5; -.
DR GeneID; 3641563; -.
DR KEGG; cal:CAALFM_C500240WA; -.
DR CGD; CAL0000174257; SKN7.
DR VEuPathDB; FungiDB:C5_00240W_A; -.
DR eggNOG; KOG0519; Eukaryota.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_008776_3_1_1; -.
DR InParanoid; Q5A4X5; -.
DR OMA; NWQSPGQ; -.
DR OrthoDB; 1154048at2759; -.
DR PHI-base; PHI:380; -.
DR PRO; PR:Q5A4X5; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000156; F:phosphorelay response regulator activity; ISS:CGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0000160; P:phosphorelay signal transduction system; ISS:CGD.
DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0008361; P:regulation of cell size; IEA:EnsemblFungi.
DR GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0000304; P:response to singlet oxygen; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
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; 1.
DR PANTHER; PTHR10015:SF361; PTHR10015:SF361; 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Stress response; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..559
FT /note="Transcription factor SKN7"
FT /id="PRO_0000425801"
FT DOMAIN 425..539
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..131
FT /note="DNA-binding domain"
FT /evidence="ECO:0000250|UniProtKB:G0SB31"
FT REGION 151..222
FT /note="Hydrophobic repeat HR-A/B"
FT /evidence="ECO:0000250|UniProtKB:G0SB31"
FT REGION 312..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 166..193
FT /evidence="ECO:0000255"
FT COMPBIAS 312..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 474
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 559 AA; 61058 MW; 90FECE66BC208EBC CRC64;
MSSLQQPIPP NSTLATTASS NQSGSNDFVK KLFLMLQEDS YKEVVRWTVK GDSFVVINTN
EFTKDILPKH FKHSNFASFV RQLNKYDFHK VKISNEAKAS YPYGEDAWEF KHPEFRINDA
EALENIKRKG PTAKKSASNV TIKTEANNNG TQPTCNHNYS QLVSATNHLK EQVESLKNDK
HSLYQEISVL ERKYKTVVEN IVAINTFNER YYRSMNVLIN SIVQNGMKLP PLDFPPPVQL
GPDSGIGSNL GPISSDTALP SISHHLSSPL PHHQQLLNRT IRPISSPIDG IPLVKLQQQS
LGQNLQAPIG TPSAVPFSEE ASSSIQAATP APLAQPVAQP INQPPPPPPP PATQQQPLPP
PPPPATATSQ IPSAPPPPTQ QQVGTSSSSV PTISPKSQGI VVSNSASPTT SAQISTTSVP
NPKFHVLLVE DDNVCIQLCR KFLVKYGCSV TVVTDGLNAI STVEHTKYDL VLMDIVMPNL
DGATATSVIR SFDTKTPIIA MTGNIEDNDL VTYLQNGMSD ILAKPFTKDD LYAILSKHLL
DPKENKQDNE PTVKKQKLS
