AP1_CANAL
ID AP1_CANAL Reviewed; 499 AA.
AC Q5AJU7; A0A1D8PJE9; G1UB70;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=AP-1-like transcription factor CAP1 {ECO:0000303|PubMed:9235926};
GN Name=CAP1 {ECO:0000303|PubMed:9235926}; OrderedLocusNames=CAALFM_C302220WA;
GN ORFNames=CaO19.1623, CaO19.9191;
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=9235926; DOI=10.1074/jbc.272.31.19304;
RA Alarco A.-M., Balan I., Talibi D., Mainville N., Raymond M.;
RT "AP1-mediated multidrug resistance in Saccharomyces cerevisiae requires
RT FLR1 encoding a transporter of the major facilitator superfamily.";
RL J. Biol. Chem. 272:19304-19313(1997).
RN [5]
RP DNA-BINDING, DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9922230; DOI=10.1128/jb.181.3.700-708.1999;
RA Alarco A.M., Raymond M.;
RT "The bZip transcription factor Cap1p is involved in multidrug resistance
RT and oxidative stress response in Candida albicans.";
RL J. Bacteriol. 181:700-708(1999).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-477.
RX PubMed=10844651; DOI=10.1046/j.1365-2958.2000.01877.x;
RA Zhang X., De Micheli M., Coleman S.T., Sanglard D., Moye-Rowley W.S.;
RT "Analysis of the oxidative stress regulation of the Candida albicans
RT transcription factor, Cap1p.";
RL Mol. Microbiol. 36:618-629(2000).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=12684384; DOI=10.1128/ec.2.2.351-361.2003;
RA Alonso-Monge R., Navarro-Garcia F., Roman E., Negredo A.I., Eisman B.,
RA Nombela C., Pla J.;
RT "The Hog1 mitogen-activated protein kinase is essential in the oxidative
RT stress response and chlamydospore formation in Candida albicans.";
RL Eukaryot. Cell 2:351-361(2003).
RN [8]
RP INDUCTION.
RX PubMed=12686601; DOI=10.1091/mbc.e02-08-0546;
RA Enjalbert B., Nantel A., Whiteway M.;
RT "Stress-induced gene expression in Candida albicans: absence of a general
RT stress response.";
RL Mol. Biol. Cell 14:1460-1467(2003).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16339733; DOI=10.1128/ec.4.12.2160-2169.2005;
RA Sohn K., Roehm M., Urban C., Saunders N., Rothenstein D., Lottspeich F.,
RA Schroppel K., Brunner H., Rupp S.;
RT "Identification and characterization of Cor33p, a novel protein implicated
RT in tolerance towards oxidative stress in Candida albicans.";
RL Eukaryot. Cell 4:2160-2169(2005).
RN [10]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15813733; DOI=10.1111/j.1365-2958.2005.04557.x;
RA Fradin C., De Groot P., MacCallum D., Schaller M., Klis F., Odds F.C.,
RA Hube B.;
RT "Granulocytes govern the transcriptional response, morphology and
RT proliferation of Candida albicans in human blood.";
RL Mol. Microbiol. 56:397-415(2005).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16102003; DOI=10.1111/j.1365-2958.2005.04771.x;
RA Urban C., Xiong X., Sohn K., Schroppel K., Brunner H., Rupp S.;
RT "The moonlighting protein Tsa1p is implicated in oxidative stress response
RT and in cell wall biogenesis in Candida albicans.";
RL Mol. Microbiol. 57:1318-1341(2005).
RN [12]
RP FUNCTION.
RX PubMed=17159223; DOI=10.1099/mic.0.29277-0;
RA Rognon B., Kozovska Z., Coste A.T., Pardini G., Sanglard D.;
RT "Identification of promoter elements responsible for the regulation of MDR1
RT from Candida albicans, a major facilitator transporter involved in azole
RT resistance.";
RL Microbiology 152:3701-3722(2006).
RN [13]
RP FUNCTION.
RX PubMed=16545688; DOI=10.1016/j.freeradbiomed.2005.11.019;
RA Wang Y., Cao Y.Y., Jia X.M., Cao Y.B., Gao P.H., Fu X.P., Ying K.,
RA Chen W.S., Jiang Y.Y.;
RT "Cap1p is involved in multiple pathways of oxidative stress response in
RT Candida albicans.";
RL Free Radic. Biol. Med. 40:1201-1209(2006).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17127290; DOI=10.2741/2055;
RA Wang Y., Cao Y.Y., Cao Y.B., Wang D.J., Jia X.M., Fu X.P., Zhang J.D.,
RA Xu Z., Ying K., Chen W.S., Jiang Y.Y.;
RT "Cap1p plays regulation roles in redox, energy metabolism and substance
RT transport: an investigation on Candida albicans under normal culture
RT condition.";
RL Front. Biosci. 12:145-153(2007).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18310903; DOI=10.1248/bpb.31.421;
RA Cao Y., Wang Y., Dai B., Wang B., Zhang H., Zhu Z., Xu Y., Cao Y.,
RA Jiang Y., Zhang G.;
RT "Trehalose is an important mediator of Cap1p oxidative stress response in
RT Candida albicans.";
RL Biol. Pharm. Bull. 31:421-425(2008).
RN [16]
RP FUNCTION, AND PROMOTER-BINDING.
RX PubMed=19395663; DOI=10.1128/ec.00002-09;
RA Znaidi S., Barker K.S., Weber S., Alarco A.M., Liu T.T., Boucher G.,
RA Rogers P.D., Raymond M.;
RT "Identification of the Candida albicans Cap1p regulon.";
RL Eukaryot. Cell 8:806-820(2009).
RN [17]
RP INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19734718;
RA Dai B.D., Cao Y.Y., Huang S., Xu Y.G., Gao P.H., Wang Y., Jiang Y.Y.;
RT "Baicalein induces programmed cell death in Candida albicans.";
RL J. Microbiol. Biotechnol. 19:803-809(2009).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=19888802; DOI=10.3109/13693780802552606;
RA Kelly J., Rowan R., McCann M., Kavanagh K.;
RT "Exposure to caspofungin activates Cap and Hog pathways in Candida
RT albicans.";
RL Med. Mycol. 47:697-706(2009).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19202089; DOI=10.1099/mic.0.023309-0;
RA Alonso-Monge R., Carvaihlo S., Nombela C., Rial E., Pla J.;
RT "The Hog1 MAP kinase controls respiratory metabolism in the fungal pathogen
RT Candida albicans.";
RL Microbiology 155:413-423(2009).
RN [20]
RP FUNCTION.
RX PubMed=19279142; DOI=10.1091/mbc.e08-11-1093;
RA Sellam A., Askew C., Epp E., Lavoie H., Whiteway M., Nantel A.;
RT "Genome-wide mapping of the coactivator Ada2p yields insight into the
RT functional roles of SAGA/ADA complex in Candida albicans.";
RL Mol. Biol. Cell 20:2389-2400(2009).
RN [21]
RP FUNCTION.
RX PubMed=19759180; DOI=10.1091/mbc.e09-01-0002;
RA Rodaki A., Bohovych I.M., Enjalbert B., Young T., Odds F.C., Gow N.A.,
RA Brown A.J.;
RT "Glucose promotes stress resistance in the fungal pathogen Candida
RT albicans.";
RL Mol. Biol. Cell 20:4845-4855(2009).
RN [22]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20337724; DOI=10.1111/j.1567-1364.2010.00613.x;
RA Garcera A., Casas C., Herrero E.;
RT "Expression of Candida albicans glutathione transferases is induced inside
RT phagocytes and upon diverse environmental stresses.";
RL FEMS Yeast Res. 10:422-431(2010).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, OXIDATION STATE, AND INDUCTION.
RX PubMed=20679492; DOI=10.1128/mcb.00313-10;
RA da Silva Dantas A., Patterson M.J., Smith D.A., Maccallum D.M., Erwig L.P.,
RA Morgan B.A., Quinn J.;
RT "Thioredoxin regulates multiple hydrogen peroxide-induced signaling
RT pathways in Candida albicans.";
RL Mol. Cell. Biol. 30:4550-4563(2010).
RN [24]
RP FUNCTION, AND MUTAGENESIS OF CYS-333.
RX PubMed=21343453; DOI=10.1128/aac.01467-10;
RA Mogavero S., Tavanti A., Senesi S., Rogers P.D., Morschhaeuser J.;
RT "Differential requirement of the transcription factor Mcm1 for activation
RT of the Candida albicans multidrug efflux pump MDR1 by its regulators Mrr1
RT and Cap1.";
RL Antimicrob. Agents Chemother. 55:2061-2066(2011).
RN [25]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21402859; DOI=10.1128/aac.01343-10;
RA Schubert S., Barker K.S., Znaidi S., Schneider S., Dierolf F., Dunkel N.,
RA Aid M., Boucher G., Rogers P.D., Raymond M., Morschhaeuser J.;
RT "Regulation of efflux pump expression and drug resistance by the
RT transcription factors Mrr1, Upc2, and Cap1 in Candida albicans.";
RL Antimicrob. Agents Chemother. 55:2212-2223(2011).
RN [26]
RP FUNCTION, AND MUTAGENESIS OF CYS-333.
RX PubMed=22615278; DOI=10.1128/aac.00264-12;
RA Sasse C., Schillig R., Reimund A., Merk J., Morschhauser J.;
RT "Inducible and constitutive activation of two polymorphic promoter alleles
RT of the Candida albicans multidrug efflux pump MDR1.";
RL Antimicrob. Agents Chemother. 56:4490-4494(2012).
RN [27]
RP FUNCTION, OXIDATION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH YBP1.
RX PubMed=23706023; DOI=10.1089/ars.2013.5199;
RA Patterson M.J., McKenzie C.G., Smith D.A., da Silva Dantas A., Sherston S.,
RA Veal E.A., Morgan B.A., MacCallum D.M., Erwig L.P., Quinn J.;
RT "Ybp1 and Gpx3 signaling in Candida albicans govern hydrogen peroxide-
RT induced oxidation of the Cap1 transcription factor and macrophage escape.";
RL Antioxid. Redox Signal. 19:2244-2260(2013).
RN [28]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23517286; DOI=10.1111/febs.12251;
RA Dai B.D., Wang Y., Zhao L.X., Li D.D., Li M.B., Cao Y.B., Jiang Y.Y.;
RT "Cap1p attenuates the apoptosis of Candida albicans.";
RL FEBS J. 280:2633-2643(2013).
RN [29]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23314569; DOI=10.4161/viru.22700;
RA Jain C., Pastor K., Gonzalez A.Y., Lorenz M.C., Rao R.P.;
RT "The role of Candida albicans AP-1 protein against host derived ROS in in
RT vivo models of infection.";
RL Virulence 4:67-76(2013).
RN [30]
RP FUNCTION, AND MUTAGENESIS OF CYS-333.
RX PubMed=24936593; DOI=10.1128/aac.03065-14;
RA Ramirez-Zavala B., Mogavero S., Schoeller E., Sasse C., Rogers P.D.,
RA Morschhaeuser J.;
RT "SAGA/ADA complex subunit Ada2 is required for Cap1- but not Mrr1-mediated
RT upregulation of the Candida albicans multidrug efflux pump MDR1.";
RL Antimicrob. Agents Chemother. 58:5102-5110(2014).
RN [31]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25028425; DOI=10.1128/mbio.01334-14;
RA Kaloriti D., Jacobsen M., Yin Z., Patterson M., Tillmann A., Smith D.A.,
RA Cook E., You T., Grimm M.J., Bohovych I., Grebogi C., Segal B.H., Gow N.A.,
RA Haynes K., Quinn J., Brown A.J.;
RT "Mechanisms underlying the exquisite sensitivity of Candida albicans to
RT combinatorial cationic and oxidative stress that enhances the potent
RT fungicidal activity of phagocytes.";
RL MBio 5:E01334-E01334(2014).
CC -!- FUNCTION: Transcription activator involved in multidrug resistance,
CC oxidative stress response, and redox homeostasis. Preferentially binds
CC to promoters with the core binding site 5'-TTA[CG]TAA-3'. Involved in
CC the oxidative stress response in via multiple pathways, including the
CC cellular antioxidant defense system, carbohydrate metabolism and energy
CC metabolism, protein degradation, ATP-dependent RNA helicase, and
CC resistance pathways. The ability of the major systemic fungal pathogen
CC of humans to sense and respond to reactive oxygen species, such as
CC H(2)O(2) generated by the host immune system, is required for survival
CC in the host and therefore virulence. Regulates the transcription of
CC COR33, GLR1, GTO1, GTT1, GTT1, TRR1, TRX1, SOD1, CAT1, and the
CC transcription regulator TSA1. Participates in the apoptosis by
CC regulating the expression of the glutathione reductase gene and
CC glutathione content. Also plays a role in the peroxide-mediated
CC induction of MDR1 and other drug response genes such as PDR16, MDR1,
CC FLU1, YCF1, and FCR1. Regulates trehalose accumulation which is
CC important for the oxidative stress tolerance. Recruits ADA2 to its
CC target promoters. Activity of CAP1 is controlled through oxidation of
CC specific cysteine residues resulting in the alteration of its
CC subcellular location. Oxidative stress induces nuclear accumulation and
CC as a result CAP1 transcriptional activity. Nuclear export is restored
CC when disulfide bonds are reduced by thioredoxin, whose expression is
CC controlled by CAP1, providing a mechanism for negative autoregulation.
CC {ECO:0000269|PubMed:10844651, ECO:0000269|PubMed:12684384,
CC ECO:0000269|PubMed:16102003, ECO:0000269|PubMed:16339733,
CC ECO:0000269|PubMed:16545688, ECO:0000269|PubMed:17127290,
CC ECO:0000269|PubMed:17159223, ECO:0000269|PubMed:18310903,
CC ECO:0000269|PubMed:19202089, ECO:0000269|PubMed:19279142,
CC ECO:0000269|PubMed:19395663, ECO:0000269|PubMed:19734718,
CC ECO:0000269|PubMed:19759180, ECO:0000269|PubMed:20337724,
CC ECO:0000269|PubMed:20679492, ECO:0000269|PubMed:21343453,
CC ECO:0000269|PubMed:21402859, ECO:0000269|PubMed:22615278,
CC ECO:0000269|PubMed:23314569, ECO:0000269|PubMed:23517286,
CC ECO:0000269|PubMed:23706023, ECO:0000269|PubMed:24936593,
CC ECO:0000269|PubMed:25028425, ECO:0000269|PubMed:9235926,
CC ECO:0000269|PubMed:9922230}.
CC -!- SUBUNIT: Interacts with YBP1. {ECO:0000269|PubMed:23706023}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10844651,
CC ECO:0000269|PubMed:12684384, ECO:0000269|PubMed:19888802,
CC ECO:0000269|PubMed:20679492, ECO:0000269|PubMed:23706023,
CC ECO:0000269|PubMed:25028425}. Cytoplasm {ECO:0000269|PubMed:10844651,
CC ECO:0000269|PubMed:12684384, ECO:0000269|PubMed:19888802,
CC ECO:0000269|PubMed:20679492, ECO:0000269|PubMed:23706023,
CC ECO:0000269|PubMed:25028425}. Note=Oxidized CAP1 is found predominantly
CC in the nucleus, while reduced CAP1 is continuously exported to the
CC cytoplasm. Caspofungin treatment also induces nuclear translocation.
CC {ECO:0000269|PubMed:10844651, ECO:0000269|PubMed:12684384,
CC ECO:0000269|PubMed:19888802, ECO:0000269|PubMed:20679492,
CC ECO:0000269|PubMed:23706023, ECO:0000269|PubMed:25028425}.
CC -!- INDUCTION: Induced by oxidative stress and during contact with
CC neutrophils. Expression is also up-regulated by the thioredoxin TRX1
CC and by treatment with Chinese herbal medicine baicalein.
CC {ECO:0000269|PubMed:12686601, ECO:0000269|PubMed:15813733,
CC ECO:0000269|PubMed:19734718, ECO:0000269|PubMed:20679492}.
CC -!- DOMAIN: Contains two cysteine rich domains (CRD), referred to as the
CC N- and C-terminal CRD's, n-CRD (Cys-254 and Cys-261) and c-CRD (Cys-
CC 446, Cys-468 and Cys-477), respectively. A nuclear export signal is
CC embedded in the c-CRD, with which the nuclear export protein
CC CRM1/exportin 1 interacts only in the absence of disulfide bonds (or
CC otherwise oxidized cysteines) within the c-CRD or between the c-CRD and
CC the n-CRD. {ECO:0000250|UniProtKB:P19880}.
CC -!- PTM: Upon oxidative stress, is oxidated by the peroxidase GPX3 and
CC stabilized by YBP1 (PubMed:20679492, PubMed:23706023). Oxidative stress
CC induces conformational changes through oxidation of cysteine residues,
CC masking the nuclear export signal, thus abolishing nuclear export by
CC CRM1/exportin 1 (By similarity). {ECO:0000250|UniProtKB:P19880,
CC ECO:0000269|PubMed:20679492, ECO:0000269|PubMed:23706023}.
CC -!- PTM: Phosphorylated in response to H(2)O(2).
CC {ECO:0000269|PubMed:23706023}.
CC -!- DISRUPTION PHENOTYPE: Causes hypersensitivity to cadmium, 4-
CC nitroquinoline N-oxide, 1,10-phenanthroline, and hydrogen peroxide.
CC Abolishes the peroxide-mediated induction of COR33, TSA1, and many
CC other genes involved in oxidative stress response. Inhibits trehalose
CC accumulation upon exposure to oxidative stress. Shows significantly
CC reduced viability when exposed to whole blood or polymorphonuclear
CC cells, as well as to the Chinese herbal medicine baicalein. Leads also
CC to decreased virulence in a Caenorhabditis elegans model. Increases
CC apoptosis upon apoptotic stimulation. {ECO:0000269|PubMed:12684384,
CC ECO:0000269|PubMed:15813733, ECO:0000269|PubMed:16102003,
CC ECO:0000269|PubMed:16339733, ECO:0000269|PubMed:17127290,
CC ECO:0000269|PubMed:18310903, ECO:0000269|PubMed:19202089,
CC ECO:0000269|PubMed:19734718, ECO:0000269|PubMed:20337724,
CC ECO:0000269|PubMed:21402859, ECO:0000269|PubMed:23314569,
CC ECO:0000269|PubMed:23517286, ECO:0000269|PubMed:9922230}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; CP017625; AOW28259.1; -; Genomic_DNA.
DR RefSeq; XP_721702.2; XM_716609.2.
DR AlphaFoldDB; Q5AJU7; -.
DR SMR; Q5AJU7; -.
DR STRING; 237561.Q5AJU7; -.
DR PRIDE; Q5AJU7; -.
DR EnsemblFungi; KHC79748; KHC79748; W5Q_02727.
DR EnsemblFungi; KHC80164; KHC80164; W5Q_02712.
DR EnsemblFungi; KHC87691; KHC87691; I503_02718.
DR GeneID; 3636640; -.
DR KEGG; cal:CAALFM_C302220WA; -.
DR CGD; CAL0000176112; CAP1.
DR VEuPathDB; FungiDB:C3_02220W_A; -.
DR eggNOG; ENOG502RPD7; Eukaryota.
DR HOGENOM; CLU_032750_0_0_1; -.
DR OMA; ANADYMN; -.
DR OrthoDB; 1198076at2759; -.
DR PHI-base; PHI:3805; -.
DR PRO; PR:Q5AJU7; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IDA:CGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:CGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IMP:CGD.
DR GO; GO:0071276; P:cellular response to cadmium ion; IMP:CGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0042783; P:evasion of host immune response; IMP:CGD.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:CGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:CGD.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013910; TF_PAP1.
DR InterPro; IPR023167; Yap1_redox_dom_sf.
DR Pfam; PF00170; bZIP_1; 1.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Disulfide bond; DNA-binding; Nucleus; Oxidation;
KW Phosphoprotein; Reference proteome; Stress response; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..499
FT /note="AP-1-like transcription factor CAP1"
FT /id="PRO_0000431934"
FT DOMAIN 40..103
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..66
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 68..75
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 104..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..261
FT /note="n-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 408..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..477
FT /note="c-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT COILED 49..105
FT /evidence="ECO:0000255"
FT MOTIF 20..27
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 44..51
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 462..469
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT COMPBIAS 36..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 254..446
FT /note="In nuclear retained form"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT DISULFID 261..477
FT /note="In nuclear retained form"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT DISULFID 446
FT /note="Interchain (with C-43 in GPX3); transient"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT MUTAGEN 333
FT /note="Missing: Leads to hyper-activity and constitutive
FT expression of MDR1."
FT /evidence="ECO:0000269|PubMed:21343453,
FT ECO:0000269|PubMed:22615278, ECO:0000269|PubMed:24936593"
FT MUTAGEN 477
FT /note="C->A: Leads to constitutive nuclear localization."
FT /evidence="ECO:0000269|PubMed:10844651"
SQ SEQUENCE 499 AA; 54998 MW; F1928209A7647F71 CRC64;
MTDIKRNFSD IASPANLDDT KKLHVDSTAT TKVGRKPIDT EPKSKRTAQN RAAQRAYRER
KERKMKELED KVRLLEDANV RALTETDFLR AQVDVLKNEL AKYTGGSDFS DLNLPTKVGH
LSHPNNHHSN VSTGTPHGSM SSSNSVASLD NDKPSSASSV SNNSPGFAFD NPWSKDNIQK
LKHQHQQQQQ KVPQGVPDLV SGSSSSSTPL NDNLLVTPES LTGLSTSSKY TGQNNVPTNL
DFTNQFDEQV DPFCVKLNEA CGTKSNPVPK FKRSGSKANT SVTNNSPLAH LVSPESQQYT
NSSNIDFMND PFFNGVGTDY NFNFDSKNGS IQDPLSFLQD DNFDLALAFG DPSPTGNEAE
ADPISLLTTE ESIYDPLTNN SDKLCSTVKA DDVNTDFNFN DFVKNSLPEK QEKGKYEPPS
TSKTTNNNEE EDKDEVVPAP PQTLKCSEIW DRITSHPKYT ELDIDGLCNE LKSKAKCSEK
GVVINTADVN QLLERSIKH
