| IED ID |
IndEnz0018000997 |
| Enzyme Type ID |
peroxidase000997 |
| Protein Name |
AP-1-like transcription factor CAP1
|
| Gene Name |
CAP1 CAALFM_C302220WA CaO19.1623 CaO19.9191 |
| Organism |
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Fungi
Dikarya
Ascomycota
saccharomyceta
Saccharomycotina (true yeasts)
Saccharomycetes
Saccharomycetales
Debaryomycetaceae
Candida/Lodderomyces clade
Candida
Candida albicans (Yeast)
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
|
| Enzyme Sequence |
MTDIKRNFSDIASPANLDDTKKLHVDSTATTKVGRKPIDTEPKSKRTAQNRAAQRAYRERKERKMKELEDKVRLLEDANVRALTETDFLRAQVDVLKNELAKYTGGSDFSDLNLPTKVGHLSHPNNHHSNVSTGTPHGSMSSSNSVASLDNDKPSSASSVSNNSPGFAFDNPWSKDNIQKLKHQHQQQQQKVPQGVPDLVSGSSSSSTPLNDNLLVTPESLTGLSTSSKYTGQNNVPTNLDFTNQFDEQVDPFCVKLNEACGTKSNPVPKFKRSGSKANTSVTNNSPLAHLVSPESQQYTNSSNIDFMNDPFFNGVGTDYNFNFDSKNGSIQDPLSFLQDDNFDLALAFGDPSPTGNEAEADPISLLTTEESIYDPLTNNSDKLCSTVKADDVNTDFNFNDFVKNSLPEKQEKGKYEPPSTSKTTNNNEEEDKDEVVPAPPQTLKCSEIWDRITSHPKYTELDIDGLCNELKSKAKCSEKGVVINTADVNQLLERSIKH |
| Enzyme Length |
499 |
| Uniprot Accession Number |
Q5AJU7 |
| Absorption |
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| Active Site |
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| Activity Regulation |
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| Binding Site |
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| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
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| Enzyme Function |
FUNCTION: Transcription activator involved in multidrug resistance, oxidative stress response, and redox homeostasis. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Involved in the oxidative stress response in via multiple pathways, including the cellular antioxidant defense system, carbohydrate metabolism and energy metabolism, protein degradation, ATP-dependent RNA helicase, and resistance pathways. The ability of the major systemic fungal pathogen of humans to sense and respond to reactive oxygen species, such as H(2)O(2) generated by the host immune system, is required for survival in the host and therefore virulence. Regulates the transcription of COR33, GLR1, GTO1, GTT1, GTT1, TRR1, TRX1, SOD1, CAT1, and the transcription regulator TSA1. Participates in the apoptosis by regulating the expression of the glutathione reductase gene and glutathione content. Plays also a role in the peroxide-mediated induction of MDR1 and other drug response genes such as PDR16, MDR1, FLU1, YCF1, and FCR1. Regulates trehalose accumulation which is important for the oxidative stress tolerance. Recruits ADA2 to its target promoters. Activity of CAP1 is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress induces nuclear accumulation and as a result CAP1 transcriptional activity. Nuclear export is restored when disulfide bonds are reduced by thioredoxin, whose expression is controlled by CAP1, providing a mechanism for negative autoregulation. {ECO:0000269|PubMed:10844651, ECO:0000269|PubMed:12684384, ECO:0000269|PubMed:16102003, ECO:0000269|PubMed:16339733, ECO:0000269|PubMed:16545688, ECO:0000269|PubMed:17127290, ECO:0000269|PubMed:17159223, ECO:0000269|PubMed:18310903, ECO:0000269|PubMed:19202089, ECO:0000269|PubMed:19279142, ECO:0000269|PubMed:19395663, ECO:0000269|PubMed:19734718, ECO:0000269|PubMed:19759180, ECO:0000269|PubMed:20337724, ECO:0000269|PubMed:20679492, ECO:0000269|PubMed:21343453, ECO:0000269|PubMed:21402859, ECO:0000269|PubMed:22615278, ECO:0000269|PubMed:23314569, ECO:0000269|PubMed:23517286, ECO:0000269|PubMed:23706023, ECO:0000269|PubMed:24936593, ECO:0000269|PubMed:25028425, ECO:0000269|PubMed:9235926, ECO:0000269|PubMed:9922230}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
|
| Features |
Chain (1); Coiled coil (1); Compositional bias (3); Disulfide bond (3); Domain (1); Motif (3); Mutagenesis (2); Region (7) |
| Keywords |
Coiled coil;Cytoplasm;DNA-binding;Disulfide bond;Nucleus;Oxidation;Phosphoprotein;Reference proteome;Stress response;Transcription;Transcription regulation;Virulence |
| Interact With |
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| Induction |
INDUCTION: Induced by oxidative stress and during contact with neutrophils. Expression is also up-regulated by the thioredoxin TRX1 and by treatment with Chinese herbal medicine baicalein. {ECO:0000269|PubMed:12686601, ECO:0000269|PubMed:15813733, ECO:0000269|PubMed:19734718, ECO:0000269|PubMed:20679492}. |
| Subcellular Location |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10844651, ECO:0000269|PubMed:12684384, ECO:0000269|PubMed:19888802, ECO:0000269|PubMed:20679492, ECO:0000269|PubMed:23706023, ECO:0000269|PubMed:25028425}. Cytoplasm {ECO:0000269|PubMed:10844651, ECO:0000269|PubMed:12684384, ECO:0000269|PubMed:19888802, ECO:0000269|PubMed:20679492, ECO:0000269|PubMed:23706023, ECO:0000269|PubMed:25028425}. Note=Oxidized CAP1 is found predominantly in the nucleus, while reduced CAP1 is continuously exported to the cytoplasm. Caspofungin treatment also induces nuclear translocation. {ECO:0000269|PubMed:10844651, ECO:0000269|PubMed:12684384, ECO:0000269|PubMed:19888802, ECO:0000269|PubMed:20679492, ECO:0000269|PubMed:23706023, ECO:0000269|PubMed:25028425}. |
| Modified Residue |
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| Post Translational Modification |
PTM: Upon oxidative stress, is oxidated by the peroxidase GPX3 and stabilized by YBP1 (PubMed:20679492, PubMed:23706023). Oxidative stress induces conformational changes through oxidation of cysteine residues, masking the nuclear export signal, thus abolishing nuclear export by CRM1/exportin 1 (By similarity). {ECO:0000250|UniProtKB:P19880, ECO:0000269|PubMed:20679492, ECO:0000269|PubMed:23706023}.; PTM: Phosphorylated in response to H(2)O(2). {ECO:0000269|PubMed:23706023}. |
| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
MOTIF 20..27; /note=Bipartite nuclear localization signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00768; MOTIF 44..51; /note=Bipartite nuclear localization signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00768; MOTIF 462..469; /note=Nuclear export signal; /evidence=ECO:0000250|UniProtKB:P19880 |
| Gene Encoded By |
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| Mass |
54,998 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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