FCR3_CANAX
ID FCR3_CANAX Reviewed; 399 AA.
AC Q8X229;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Fluconazole resistance protein 3;
GN Name=FCR3;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476 {ECO:0000312|EMBL:AAL35299.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 11651 / B792 / 171D;
RX PubMed=11561289; DOI=10.1002/yea.770;
RA Yang X., Talibi D., Weber S., Poisson G., Raymond M.;
RT "Functional isolation of the Candida albicans FCR3 gene encoding a bZip
RT transcription factor homologous to Saccharomyces cerevisiae Yap3p.";
RL Yeast 18:1217-1225(2001).
RN [2] {ECO:0000305}
RP FUNCTION.
RC STRAIN=ATCC 11651 / B792 / 171D;
RX PubMed=9864335; DOI=10.1128/jb.181.1.231-240.1999;
RA Talibi D., Raymond M.;
RT "Isolation of a putative Candida albicans transcriptional regulator
RT involved in pleiotropic drug resistance by functional complementation of a
RT pdr1 pdr3 mutation in Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:231-240(1999).
CC -!- FUNCTION: Transcription factor that confers fluconazole resistance in
CC S.cerevisiae by activation of the PDR5 gene. Can also activate the
CC transcription of S.cerevisiae genes involved in 4-nitroquinoline-N-
CC oxide resistance. {ECO:0000269|PubMed:11561289,
CC ECO:0000269|PubMed:9864335}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000255|RuleBase:RU000470,
CC ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF342983; AAL35299.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8X229; -.
DR SMR; Q8X229; -.
DR VEuPathDB; FungiDB:C5_01810W_A; -.
DR VEuPathDB; FungiDB:CAWG_04566; -.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..399
FT /note="Fluconazole resistance protein 3"
FT /id="PRO_0000076538"
FT DOMAIN 210..273
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..234
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 235..242
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 103..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 44483 MW; 51AEB8481D2F4047 CRC64;
MNFKTENSTT PNGDWSQSKA FTNSGSSFPV LNGTCELDQE NLALSNSGQP ESIFTQDSGL
HGIDVAAPSD ITDLNNQSGY QYNNNLAHDL YFTGSMEMPT TQHPYITNTN NHLSYSNSSE
EFSPIGNNMS PDSTGGANSN NFTSGNKRKA SNESFSPLSG HHYGTESGNN NNNNGTSRSS
QSSSHKSRKK LLDEKDAALI ARDDSELTEE ELQMKRKAQN RAAQRAFRER KESKLKELEA
KLLASEEERQ KLLDELEQIK KQNISIATEN EILKHNGMGN INNDVQIGNL SSYGRLQVDK
FNFPKTQKDF IEHVLQGTNH QLKDENKDKV YNDNQGHKLL ALGAVWDYLQ IKAEEADLDF
NSIDFNDVME KLKGNEKCHG YGPAYPLELV NEAIESSLN
