IED ID | IndEnz0018000208 |
Enzyme Type ID | peroxidase000208 |
Protein Name |
AP-1-like transcription factor yap1 BZIP domain-containing transcription factor yap1 |
Gene Name | yap1 AFUA_6G09930 |
Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Enzyme Sequence | MADYNTLYQQGLYLSPDQQDLLLAALSSNNPTQKQQTVTHNSEANQNLNHTPGHASSGSFSVSPPSGLDGSVNQSTTFGYEDSPYLDLNPDFDLDFLGNESLIGDLPPSLPSTEDYEPGDKRKDIDGQVNDKEDSGKKRRESDEKAAKKPGRKPLTSEPTSKRKAQNRAAQRAFRERKEKHLKDLEAKVEELQKASDNANQENGLLRAQVERLQLELKEYRKRLSWVTSTSGLSPVNAIPGAYSKGMYGLNNNEFMFDFPKFGDLPGSHLFTNTQTSKSNQNKAKDNPTATPRSEAQVPGVLNRNDLKISSPNGLSNGPSPAKSTPSGQTPNSQTSTRPGSGTLNGAVDNNGAARGYQVNSSYSASTKQATHDTPSSDSPSSSSDSHQSQLLSSNGTSPEPSLHSPAVKATESSTPHACTYTTINGEESFCAQLSMACGNINNPIPAVRQNSESASNTPSHANSSDKALGLDFFAQQNGGQFDPVLFGDWREPQDAILSQDFGTFFDDAFPLPDLGSPSHNFSEATKQPAAPKKDLIAEIDSKLDEDEEVVPGEDKSQMLTCNKIWDRLQSMEKFRNGEIDVDNLCSELRTKARCSEGGVVVNQKDVEDIMGRVK |
Enzyme Length | 615 |
Uniprot Accession Number | Q4WMH0 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Transcription activator involved in oxidative stress response and redox homeostasis (PubMed:17921349, PubMed:18608886, PubMed:18651311, PubMed:20376564, PubMed:27748436). Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including thioredoxin peroxidase (aspF3), cytochrome peroxidase, and the protein AFUA_3G00730, which appears to belong to the glutathione S-transferase family (PubMed:17921349, PubMed:18651311). Proteins of the protein degradation pathway are also regulated by yap1, as well the p-nitroreductase family protein AFUA_5G09910 (PubMed:17921349). May be involved in antifungal resistance to voriconazole (PubMed:20376564). {ECO:0000269|PubMed:17921349, ECO:0000269|PubMed:18608886, ECO:0000269|PubMed:18651311, ECO:0000269|PubMed:20376564, ECO:0000269|PubMed:27748436}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Compositional bias (2); Disulfide bond (3); Domain (1); Motif (3); Region (9) |
Keywords | Cytoplasm;DNA-binding;Disulfide bond;Nucleus;Oxidation;Reference proteome;Transcription;Transcription regulation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17921349}. Cytoplasm {ECO:0000269|PubMed:17921349}. Note=The nuclear localization is oxidative stress-dependent and oxidized yap1 is found predominantly in the nucleus, while reduced yap1 is continuously exported to the cytoplasm. {ECO:0000269|PubMed:17921349}. |
Modified Residue | |
Post Translational Modification | PTM: Depending on the oxidative stress inducing agent, yap1 can undergo two distinct conformational changes, both involving disulfide bond formation, and both masking the nuclear export signal, thus abolishing nuclear export. {ECO:0000250|UniProtKB:P19880}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 35..42; /note=Bipartite nuclear localization signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00768; MOTIF 68..75; /note=Bipartite nuclear localization signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00768; MOTIF 580..587; /note=Nuclear export signal; /evidence=ECO:0000250|UniProtKB:P19880 |
Gene Encoded By | |
Mass | 66,744 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |