SEF1_CANAL
ID SEF1_CANAL Reviewed; 917 AA.
AC Q59UY7; A0A1D8PS54;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transcriptional regulatory protein SEF1;
GN Name=SEF1; OrderedLocusNames=CAALFM_CR02190CA;
GN ORFNames=CaO19.11237, CaO19.3753;
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 INDUCTION.
RX PubMed=15387822; DOI=10.1111/j.1365-2958.2004.04214.x;
RA Lan C.Y., Rodarte G., Murillo L.A., Jones T., Davis R.W., Dungan J.,
RA Newport G., Agabian N.;
RT "Regulatory networks affected by iron availability in Candida albicans.";
RL Mol. Microbiol. 53:1451-1469(2004).
RN [5]
RP DOMAIN.
RX PubMed=18629206; DOI=10.1002/cfg.492;
RA Maicas S., Moreno I., Nieto A., Gomez M., Sentandreu R., Valentin E.;
RT "In silico analysis for transcription factors with Zn(II)(2)C(6) binuclear
RT cluster DNA-binding domains in Candida albicans.";
RL Comp. Funct. Genomics 6:345-356(2005).
RN [6]
RP FUNCTION.
RX PubMed=20041210; DOI=10.1371/journal.pgen.1000783;
RA Homann O.R., Dea J., Noble S.M., Johnson A.D.;
RT "A phenotypic profile of the Candida albicans regulatory network.";
RL PLoS Genet. 5:E1000783-E1000783(2009).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=21050438; DOI=10.1186/1752-0509-4-148;
RA Linde J., Wilson D., Hube B., Guthke R.;
RT "Regulatory network modelling of iron acquisition by a fungal pathogen in
RT contact with epithelial cells.";
RL BMC Syst. Biol. 4:148-148(2010).
RN [8]
RP FUNCTION, DNA-BINDING, AND INDUCTION.
RX PubMed=21843869; DOI=10.1016/j.chom.2011.07.005;
RA Chen C., Pande K., French S.D., Tuch B.B., Noble S.M.;
RT "An iron homeostasis regulatory circuit with reciprocal roles in Candida
RT albicans commensalism and pathogenesis.";
RL Cell Host Microbe 10:118-135(2011).
RN [9]
RP FUNCTION IN VIRULENCE.
RX PubMed=22073120; DOI=10.1371/journal.pone.0026962;
RA Vandeputte P., Ischer F., Sanglard D., Coste A.T.;
RT "In vivo systematic analysis of Candida albicans Zn2-Cys6 transcription
RT factors mutants for mice organ colonization.";
RL PLoS ONE 6:E26962-E26962(2011).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY SSN3, AND INTERACTION
RP WITH SSN3 AND SFU1.
RX PubMed=23133381; DOI=10.1371/journal.ppat.1002956;
RA Chen C., Noble S.M.;
RT "Post-transcriptional regulation of the Sef1 transcription factor controls
RT the virulence of Candida albicans in its mammalian host.";
RL PLoS Pathog. 8:E1002956-E1002956(2012).
CC -!- FUNCTION: Transcription factor which plays an essential role in
CC virulence by activating the transcription of iron uptake genes such as
CC FRE7 in iron-poor environments such as the host bloodstream and
CC internal organs. Promotes commensalism in a mouse model of
CC gastrointestinal infection. {ECO:0000269|PubMed:20041210,
CC ECO:0000269|PubMed:21050438, ECO:0000269|PubMed:21843869,
CC ECO:0000269|PubMed:22073120, ECO:0000269|PubMed:23133381}.
CC -!- SUBUNIT: Interacts with SSN3 and SFU1. {ECO:0000269|PubMed:23133381}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23133381}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:23133381}.
CC Note=Interaction with SFU1 promotes cytoplasmic localization whereas
CC interaction with SSN3 and subsequent phosphorylation promotes nuclear
CC localization. Nuclear localization is associated with virulence.
CC -!- INDUCTION: Expression is regulated by changes of iron conditions with
CC an increase in low iron. Transcription is negatively regulated by SFU1.
CC {ECO:0000269|PubMed:15387822, ECO:0000269|PubMed:21050438,
CC ECO:0000269|PubMed:21843869}.
CC -!- PTM: Phosphorylated by SSN3 under iron-depleted conditions which leads
CC to nuclear localization. {ECO:0000269|PubMed:23133381}.
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DR EMBL; CP017630; AOW30969.1; -; Genomic_DNA.
DR RefSeq; XP_713441.1; XM_708348.2.
DR AlphaFoldDB; Q59UY7; -.
DR SMR; Q59UY7; -.
DR BioGRID; 1228003; 3.
DR STRING; 237561.Q59UY7; -.
DR PRIDE; Q59UY7; -.
DR GeneID; 3644945; -.
DR KEGG; cal:CAALFM_CR02190CA; -.
DR CGD; CAL0000189760; SEF1.
DR VEuPathDB; FungiDB:CR_02190C_A; -.
DR eggNOG; ENOG502QR4T; Eukaryota.
DR HOGENOM; CLU_010150_0_0_1; -.
DR InParanoid; Q59UY7; -.
DR OMA; LVWCVHE; -.
DR OrthoDB; 1049786at2759; -.
DR PHI-base; PHI:2617; -.
DR PRO; PR:Q59UY7; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005737; C:cytoplasm; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IDA:CGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:CGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:CGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:CGD.
DR GO; GO:0071469; P:cellular response to alkaline pH; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; DNA-binding; Iron; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Virulence; Zinc.
FT CHAIN 1..917
FT /note="Transcriptional regulatory protein SEF1"
FT /id="PRO_0000422808"
FT DNA_BIND 90..120
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 129..164
FT /evidence="ECO:0000255"
FT COMPBIAS 14..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 103901 MW; FA39DFF4116EC1BC CRC64;
MKFEKGKVRI LPKPSPTPTN PQTPLPLLPA QTKPVNSKRK SAASTPGNES KKSRKSNSTA
STPNSATPTS VGTPPQKTSK PTGHRPVTSC TFCRQHKIKC NASDNYPNPC ERCKKMGLKC
EIDPEFRPRK GSQIQSLKSD VDELKAKIEM LTKNESLLTQ ALNQHNLNHA SQQQQSSGSQ
SQQQHPPNPQ RALSYTSANS SPQVAFSNAS PIPSVTSIQQ NAPLTHENSD NSPYALNTPE
NIEELQPISE FILGDVTLPL NRANELHDKF MTTHLPFLPI IISRSATELY HKSQLLFWAV
ILTASLSEPE PKLYMSLASL IKQLAIETCW IKTPRSTHVI QALIILSIWP LPNEKVLDDC
SYRFVGLAKN LSLQLGLHRG GEFIQEFSRN QVSLGPDAER WRTRSWLAVF FCEQFWSSLL
GLPPSINTTD YLLENARVDK SLPKNFRCLI SLSIFQCKLV NIMGISVTRP DGLLEPSNRA
GSLSLLDREL ERLRFKLQFE EGGPIEVYYL YIKLMICCFA FLPGTPIEDQ VKYVSFAYLS
ATRIVTIVSK MVNDISLIEL PIYIRQAVTY SVFMLFKLHL SRYLIDKYVD SARQSIVTVH
RLFRNTLSSW KDLQNDISRT AKVLENLNMV LYNYPEIFLN DSENEDSSII TRMRSHLTAS
LFYDLVWCVH EARRRSVLDK GKRQAQPNKK ILPLPFYNQI TKDDFKTITT TSPNGTTITT
LVPTDQAMNQ AKSKSFDSSK PLEINGIPLP MLEATGSTRE VLDSLPSQSL PSQAPTLQQY
PMQQDQQQQE PSQQQQQKHS QQSQQYQQQQ QSNQQQPHLQ HQRQFQQSPP PQFSMISSTP
PLQQPPFILA NSPLPQTYLP KIDEMNMSPE VKQENSVAPF ASQITNFFDQ QTSGWFNNDN
QDDDFLGWFD VNMMQEK
