SFU1_CANAL
ID SFU1_CANAL Reviewed; 517 AA.
AC Q5AP95; A0A1D8PER2;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Suppressor of ferric uptake 1;
GN Name=SFU1; OrderedLocusNames=CAALFM_C110020WA;
GN ORFNames=CaO19.12333, CaO19.4869;
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.
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 INDUCTION.
RX PubMed=18451059; DOI=10.1099/mic.0.2007/013441-0;
RA Woodacre A., Mason R.P., Jeeves R.E., Cashmore A.M.;
RT "Copper-dependent transcriptional regulation by Candida albicans Mac1p.";
RL Microbiology 154:1502-1512(2008).
RN [6]
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 [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=21131439; DOI=10.1128/ec.00158-10;
RA Hsu P.C., Yang C.Y., Lan C.Y.;
RT "Candida albicans Hap43 is a repressor induced under low-iron conditions
RT and is essential for iron-responsive transcriptional regulation and
RT virulence.";
RL Eukaryot. Cell 10:207-225(2011).
RN [8]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEF1.
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: Transcriptional regulator of iron-responsive genes. Represses
CC expression of SEF1 and genes for iron uptake if iron is present. Plays
CC also a transcription-independent role in the direct inhibition of SEF1
CC function through protein complex formation and translocation to the
CC cytoplasm, where SEF1 is destabilized. Promotes gastrointestinal
CC commensalism in mice. {ECO:0000269|PubMed:15387822,
CC ECO:0000269|PubMed:21131439, ECO:0000269|PubMed:21843869,
CC ECO:0000269|PubMed:23133381}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23133381}. Nucleus
CC {ECO:0000269|PubMed:23133381}.
CC -!- INDUCTION: Repressed by the HAP43 transcription regulator. Expression
CC is also under the control of MAC1. {ECO:0000269|PubMed:18451059,
CC ECO:0000269|PubMed:21131439, ECO:0000269|PubMed:21592964,
CC ECO:0000269|PubMed:21843869}.
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DR EMBL; CP017623; AOW26633.1; -; Genomic_DNA.
DR RefSeq; XP_723553.2; XM_718460.2.
DR AlphaFoldDB; Q5AP95; -.
DR SMR; Q5AP95; -.
DR BioGRID; 1217961; 3.
DR STRING; 237561.Q5AP95; -.
DR PRIDE; Q5AP95; -.
DR GeneID; 3634867; -.
DR KEGG; cal:CAALFM_C110020WA; -.
DR CGD; CAL0000194032; SFU1.
DR VEuPathDB; FungiDB:C1_10020W_A; -.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_040438_0_0_1; -.
DR InParanoid; Q5AP95; -.
DR OrthoDB; 1466754at2759; -.
DR PHI-base; PHI:2618; -.
DR PRO; PR:Q5AP95; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 2.
DR Pfam; PF00320; GATA; 2.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 2.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..517
FT /note="Suppressor of ferric uptake 1"
FT /id="PRO_0000422809"
FT ZN_FING 60..84
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 184..208
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 56353 MW; 61718B320CB0BE45 CRC64;
MPTSPTESIP NSSTKEQPIL PKMLPTAKSP HTTPAQSPQN SDHHHHHQQT PPQPTDGQQC
SNCGTTKTPL WRRAPDGTLI CNACGLYYRS NNTHRPVNLK RPPNTIAVVK EEEGSCKGDG
RCNGTGGSAA CKGCPAYNNR IVAKKALEKS PKNDSSRAPI DKSLKRSTST DATTEDESSL
AIACFNCGTT ITPLWRRDDA GNTICNACGL FYRLHGSHRP IKMKRPTIKR RKRNVSDKKS
KDEVQMHSSD QSPIVASDPI SPTPHNNENN NNVTNITTTT KTPTRSPHYY QPPPQYPYQH
HPINSTTSSA INRLPPISYQ SPYQTAPLSH SPMQSSSSYS PGASSVIPSS YYPPYSGSGR
IPNGPGPVPG PPPPPPPTQS QPHHQQITTS PTSQSYGSLR APIHITKRGY TPENIRLPSI
QLTSSTSSNS ETKLPPITNH SEKCCSNCAG PKSLAPMAID FTASYRFNNI DSQTKLTKED
QNDSEGVSRD NDTRDENKPI KQEEHRSALS IGKLLNG
