ID   AP1_CANGA               Reviewed;         588 AA.
AC   Q6FRZ8;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=bZip transcription factor GAP1 {ECO:0000303|PubMed:17046176};
GN   Name=AP1 {ECO:0000303|PubMed:17046176}; OrderedLocusNames=CAGL0H04631g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17046176; DOI=10.1016/j.gene.2006.08.010;
RA   Chen K.H., Miyazaki T., Tsai H.F., Bennett J.E.;
RT   "The bZip transcription factor Cgap1p is involved in multidrug resistance
RT   and required for activation of multidrug transporter gene CgFLR1 in Candida
RT   glabrata.";
RL   Gene 386:63-72(2007).
CC   -!- FUNCTION: Transcription factor that plays a critical role in response
CC       to various stresses and reduces the stress through transcriptional
CC       activation of its target genes including multidrug transporter FLR1
CC       (PubMed:17046176). {ECO:0000269|PubMed:17046176}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- DOMAIN: Contains two cysteine rich domains (CRD), referred to as the
CC       N- and C-terminal CRD's, n-CRD and c-CRD, respectively (By similarity).
CC       A nuclear export signal is embedded in the c-CRD, with which the
CC       nuclear export protein CRM1/exportin 1 interacts only in the absence of
CC       disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or
CC       between the c-CRD and the n-CRD (By similarity).
CC       {ECO:0000250|UniProtKB:P19880}.
CC   -!- DISRUPTION PHENOTYPE: Leads to decreased resistance to hydrogen
CC       peroxide, 4-nitroquinoline-N-oxide (4-NQO), benomyl, and cadmium
CC       chloride (PubMed:17046176). {ECO:0000269|PubMed:17046176}.
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DR   EMBL; CR380954; CAG59929.1; -; Genomic_DNA.
DR   RefSeq; XP_446996.1; XM_446996.1.
DR   AlphaFoldDB; Q6FRZ8; -.
DR   SMR; Q6FRZ8; -.
DR   STRING; 5478.XP_446996.1; -.
DR   EnsemblFungi; CAG59929; CAG59929; CAGL0H04631g.
DR   GeneID; 2888604; -.
DR   KEGG; cgr:CAGL0H04631g; -.
DR   CGD; CAL0130344; AP1.
DR   VEuPathDB; FungiDB:CAGL0H04631g; -.
DR   eggNOG; ENOG502RPD7; Eukaryota.
DR   HOGENOM; CLU_032750_0_0_1; -.
DR   InParanoid; Q6FRZ8; -.
DR   OMA; VSTFCAK; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0005737; C:cytoplasm; IDA:CGD.
DR   GO; GO:0005634; C:nucleus; IDA:CGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IGI:CGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:CGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR   GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IEA:EnsemblFungi.
DR   GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IGI:CGD.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblFungi.
DR   GO; GO:0000304; P:response to singlet oxygen; IEA:EnsemblFungi.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:EnsemblFungi.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR013910; TF_PAP1.
DR   InterPro; IPR023167; Yap1_redox_dom_sf.
DR   Pfam; PF08601; PAP1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF111430; SSF111430; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..588
FT                   /note="bZip transcription factor GAP1"
FT                   /id="PRO_0000443418"
FT   DOMAIN          25..88
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..51
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          53..60
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          164..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..327
FT                   /note="Transcription activation 1"
FT                   /evidence="ECO:0000250|UniProtKB:P19880"
FT   REGION          253..265
FT                   /note="n-CRD"
FT                   /evidence="ECO:0000250|UniProtKB:P19880"
FT   REGION          376..477
FT                   /note="Transcription activation 2"
FT                   /evidence="ECO:0000250|UniProtKB:P19880"
FT   REGION          487..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..567
FT                   /note="c-CRD"
FT                   /evidence="ECO:0000250|UniProtKB:P19880"
FT   MOTIF           552..559
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:P19880"
FT   COMPBIAS        15..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..524
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  64609 MW;  A3907213D0FF57B4 CRC64;
     MAEVDNGGAQ KSSASRKKRY QELDPETRMK RVAQNRAAQK AFRERKERKM KELERKVVDL
     ENLTKLNEVE TNFLRDQLSI LVKELRKYRP ETKQDHKVLK YLEKHKGGAA GAGNGAATGS
     VSTSTRHTDL AASNANRVSK DSSILPGAKI IRQDLESFNE NRHFNVTGQL TPPGNTSSST
     TANSVAANAK KQSIPHSDSS DSNESKNTWN TDPTSSEDWL DDVMTSHKQI SRGQSGSGID
     FNNFFDEQVS EFCTKLNQAC GTKACPIPQS KSAATTPLPG TSSNGNSNSP MIINDTMGDV
     SLNMQGNEHG NATNNLVTDP AFLSNTWDDM SPASNQHSTG GAPGFGQLGF GDNLLGNDIL
     FSPNSPAYSP SVLGSGRTQE VYRSPAVQKV VEKENESKSV NFPFINSSLA FPGDYDNNFF
     RETTDLNFDD NDQDDNFTNS NDLVNDYFTT NIPDTDNSDS ALIANGLVKE EPSMQTEDTF
     KVQNTNDMLN SSRMKETIDN QNIGEKTTKD DNEDDDEDDE NDNTVVPSRD DGLLRCSEIW
     DRITAHPKYS DIDIDGLCSE LMAKAKCSER GVVINADDVQ VALNKHMS