ID   SFL1_CANAL              Reviewed;         805 AA.
AC   Q5A287; A0A1D8PT48; Q5A2D8;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Transcription factor SFL1;
GN   Name=SFL1; OrderedLocusNames=CAALFM_CR05990CA;
GN   ORFNames=CaO19.454, CaO19.8085;
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   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=17766464; DOI=10.1128/ec.00236-07;
RA   Bauer J., Wendland J.;
RT   "Candida albicans Sfl1 suppresses flocculation and filamentation.";
RL   Eukaryot. Cell 6:1736-1744(2007).
RN   [5]
RP   IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17715361; DOI=10.1128/ec.00199-07;
RA   Li Y., Su C., Mao X., Cao F., Chen J.;
RT   "Roles of Candida albicans Sfl1 in hyphal development.";
RL   Eukaryot. Cell 6:2112-2121(2007).
RN   [6]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21666074; DOI=10.1128/ec.05060-11;
RA   Hall R.A., Turner K.J., Chaloupka J., Cottier F., De Sordi L., Sanglard D.,
RA   Levin L.R., Buck J., Muhlschlegel F.A.;
RT   "The quorum-sensing molecules farnesol/homoserine lactone and dodecanol
RT   operate via distinct modes of action in Candida albicans.";
RL   Eukaryot. Cell 10:1034-1042(2011).
RN   [7]
RP   FUNCTION.
RX   PubMed=21205158; DOI=10.1111/j.1567-1364.2010.00710.x;
RA   Song W., Wang H., Chen J.;
RT   "Candida albicans Sfl2, a temperature-induced transcriptional regulator, is
RT   required for virulence in a murine gastrointestinal infection model.";
RL   FEMS Yeast Res. 11:209-222(2011).
RN   [8]
RP   FUNCTION.
RX   PubMed=23049891; DOI=10.1371/journal.pone.0045912;
RA   Chauvel M., Nesseir A., Cabral V., Znaidi S., Goyard S.,
RA   Bachellier-Bassi S., Firon A., Legrand M., Diogo D., Naulleau C.,
RA   Rossignol T., d'Enfert C.;
RT   "A versatile overexpression strategy in the pathogenic yeast Candida
RT   albicans: identification of regulators of morphogenesis and fitness.";
RL   PLoS ONE 7:E45912-E45912(2012).
RN   [9]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=23966855; DOI=10.1371/journal.ppat.1003519;
RA   Znaidi S., Nesseir A., Chauvel M., Rossignol T., d'Enfert C.;
RT   "A comprehensive functional portrait of two heat shock factor-type
RT   transcriptional regulators involved in Candida albicans morphogenesis and
RT   virulence.";
RL   PLoS Pathog. 9:E1003519-E1003519(2013).
CC   -!- FUNCTION: Transcription factor that plays a role of repressor of
CC       filamentous growth and flocculation. Antagonizes functions of SFL2 and
CC       FLO8. Plays a role in the hyphal repression induced by secreted factors
CC       like dodecanol by competitors such as Pseudomonas aeruginosa and
CC       Burkholderia cenocepacia. {ECO:0000269|PubMed:17715361,
CC       ECO:0000269|PubMed:17766464, ECO:0000269|PubMed:21205158,
CC       ECO:0000269|PubMed:21666074, ECO:0000269|PubMed:23049891,
CC       ECO:0000269|PubMed:23966855}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17715361,
CC       ECO:0000269|PubMed:17766464, ECO:0000269|PubMed:21666074}.
CC       Note=Localizes to the nucleus in both yeast and hyphal cells.
CC   -!- DISRUPTION PHENOTYPE: Enhances flocculation, filamentous growth, and
CC       hypha-specific gene expression in several media and at several growth
CC       temperatures. {ECO:0000269|PubMed:17715361,
CC       ECO:0000269|PubMed:17766464, ECO:0000269|PubMed:21666074}.
CC   -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR   EMBL; CP017630; AOW31310.1; -; Genomic_DNA.
DR   RefSeq; XP_715888.2; XM_710795.2.
DR   AlphaFoldDB; Q5A287; -.
DR   SMR; Q5A287; -.
DR   BioGRID; 1225536; 3.
DR   STRING; 237561.Q5A287; -.
DR   PRIDE; Q5A287; -.
DR   GeneID; 3642498; -.
DR   KEGG; cal:CAALFM_CR05990CA; -.
DR   CGD; CAL0000178027; SFL1.
DR   VEuPathDB; FungiDB:CR_05990C_A; -.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_370877_0_0_1; -.
DR   OrthoDB; 1154048at2759; -.
DR   PRO; PR:Q5A287; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IEA:UniProt.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000232; HSF_DNA-bd.
DR   InterPro; IPR027725; HSF_fam.
DR   InterPro; IPR027722; Sfl1.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10015; PTHR10015; 1.
DR   PANTHER; PTHR10015:SF388; PTHR10015:SF388; 1.
DR   Pfam; PF00447; HSF_DNA-bind; 1.
DR   PRINTS; PR00056; HSFDOMAIN.
DR   SMART; SM00415; HSF; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00434; HSF_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Virulence.
FT   CHAIN           1..805
FT                   /note="Transcription factor SFL1"
FT                   /id="PRO_0000425614"
FT   DNA_BIND        117..226
FT                   /evidence="ECO:0000250"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..569
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..805
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   805 AA;  90145 MW;  3C38ABDAE94513F7 CRC64;
     MSHLVSSSLG TTTTATPTSR SPHTNHSTPY NQNSITSNRS SPVPKNSVNS RIIPQTMNPP
     IDMKSNNILN PEKDTDTSRG DHSESKASSI SSASGTTTTN NNNVSNNNST GKTQIVFIHK
     LYDMLHDESI SHLIWWSPSL DSFYVTPGEE FSRVLSQYFK HTNIASFIRQ LNMYGFHKVN
     EPFLNQDDQQ QQQQLQSNRW EFRHSTNQFR KGDTESLKNI KRRSSKTLNA QKEVVNIKSL
     PPTSHPMEYN TGYSYQNEDS AHYFVHHHSI TTMQSPADMR PRSPSTPIPM QPLAQQQQQQ
     QQQQQQQQQQ LPSQPVPNGP PVFSGPIPPG AVNQSPQEYL TRPSILNNVQ GSFENATNFK
     FVELTNQINL LRNDFFTMNN RYEILQNELK YQTADSMAVL EILEKLSNDN RIATDIRDLK
     NVVSQRMQRL NNQFIPQQSN FAPHIPGQQQ QQQHGNSVSS NYHLESTNVS RNPSTTNLNV
     APQPYPLNPH YTIYANNRAS GSSEINNGVF RAREDSNNSK RNLSVYDPLQ PVPSRNSSRI
     LIEESTPTHP PTNFNPQQSQ SQSQVQLGPA MPPQGFRNRA ESTYSPLSHS SNKSQILNKA
     PTPVNHSPLV QQQQKEAKQE LNDSSVAPPS QSSLPVTRPL SRQQQQQQQT LHHPSTTSSR
     TNSLPNPVAE HPAPQSSYFM QRNSFNTVYE HQKSLRVPSP KRVRYATPPR SIPEQPISST
     APTTMITSTS KPTSTSGAAI SRSENHSVVS LTGGALPSVS ELDKSIRTGS SVSLPPIKSI
     KDNDNKNDNG NSDDNGNDHK KRKLE