| IED ID | IndEnz0007000071 |
| Enzyme Type ID | catalase000071 |
| Protein Name |
AP-1-like transcription factor Caffeine resistance protein 3 |
| Gene Name | pap1 caf3 SPAC1783.07c |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MSGQTETLSSTSNIPIAKAEPEQSADFSASHKKRGPVSDRSSRRTSSEEVDLMPNVDDEVDGDVKPKKIGRKNSDQEPSSKRKAQNRAAQRAFRKRKEDHLKALETQVVTLKELHSSTTLENDQLRQKVRQLEEELRILKDGSFTFEMSLPHRNPSLSSLPTTGFSSNFAHMKDGISPQSNLHLSPNSIEKPNMHQNVLHNDRSADNLNHRYQVPPTLVDSNSAQGTLSPETPSSSDSPSNLYLNYPKRKSITHLHHDCSALSNGENGEDVADGKQFCQKLSTACGSIACSMLTKTTPHRASVDILSNLHESTVSPPMADESVQRSSEVSKSIPNVELSLNVNQQFVSPFGGTDSFPLPTDTGLDSLFEPDSAIENSHLKNVVMEPELFQAWREPAESLDKEFFNDEGEIDDVFHNYFHNSNENGDLITNSLHGLDFLENANESFPEQMYPFIKHNKDYISNHPDEVPPDGLPQKGKHDTSSQMPSENEIVPAKERAYLSCPKVWSKIINHPRFESFDIDDLCSKLKNKAKCSSSGVLLDERDVEAALNQFN |
| Enzyme Length | 552 |
| Uniprot Accession Number | Q01663 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Transcription activator involved in multidrug resistance, oxidative stress response, and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes like catalase ctt1 and components of the cellular thiol-reducing pathways, including the thioredoxin system (trx2, trr1), ABC tansporters involved in multidrug resistance like bfr1/hba2 and pmd1 as well as the gene obr1/apt1. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription factor 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 pap1 transcriptional activity. Required for sty1/spc1-confered staurosporine resistance. {ECO:0000269|PubMed:11017199, ECO:0000269|PubMed:1448080, ECO:0000269|PubMed:1899230, ECO:0000269|PubMed:23525001, ECO:0000269|PubMed:9585505}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (3); Disulfide bond (2); Domain (1); Helix (2); Motif (2); Mutagenesis (12); Region (7); Sequence conflict (3) |
| Keywords | 3D-structure;Activator;Cytoplasm;DNA-binding;Direct protein sequencing;Disulfide bond;Nucleus;Reference proteome;Transcription;Transcription regulation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10329722, ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:15165244, ECO:0000269|PubMed:15824112, ECO:0000269|PubMed:9585505}. Cytoplasm {ECO:0000269|PubMed:10329722, ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:15165244, ECO:0000269|PubMed:15824112, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:9585505}. Note=Oxidized pap1 is found predominantly in the nucleus, while reduced pap1 is continuously exported to the cytoplasm by crm1/exportin 1. {ECO:0000269|PubMed:10329722, ECO:0000269|PubMed:9585505}. |
| Modified Residue | |
| Post Translational Modification | PTM: Depending on the oxidative stress inducing agent, pap1 can undergo two distinct conformational changes, both masking the nuclear export signal, thus abolishing nuclear export by crm1/exportin 1. The glutathione-depleting agent diethylmaleate (DEM) leads to the non-reversible modification of at least 2 cysteine residues in the c-CRD. Peroxide stress induces the formation of a tpx1-dependent interdomain disulfide bond between Cys-278 and Cys-501. {ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:15165244, ECO:0000269|PubMed:15824112}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1GD2; |
| Mapped Pubmed ID | 10348908; 10749922; 10954610; 11071922; 11129048; 11350071; 11453251; 12018855; 12063243; 12243351; 12359231; 12442905; 12521308; 12521310; 12787490; 12855726; 12896976; 14503856; 14758541; 15052323; 15135546; 15164362; 15529002; 15650330; 15650694; 15765057; 15865206; 16087744; 16141205; 16175211; 16202243; 16258240; 16258244; 16278445; 16458193; 16554715; 17016471; 17205051; 17473896; 17530441; 17668038; 17725619; 17881729; 18003976; 18235227; 18248428; 18337696; 18665268; 18684775; 18758731; 19264558; 19625445; 19672306; 19940942; 20204527; 20473289; 20537132; 20563653; 21712547; 22245228; 22279963; 22344694; 22561704; 22806344; 22840777; 23209828; 23695302; 23697806; 23861937; 23896534; 24118096; 24521463; 24696293; 24763107; 25483073; 25720772; 26537787; 26567340; 27298342; 27558664; 28410370; 28652406; 29996109; 30181366; 30726745; 32908306; 33225241; 33260998; 33823663; 35079912; 7769002; 7929079; 8569688; 9211790; 9287302; 9532803; |
| Motif | MOTIF 81..88; /note=Nuclear localization signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00768; MOTIF 515..533; /note=Nuclear export signal; /evidence=ECO:0000305|PubMed:10329722 |
| Gene Encoded By | |
| Mass | 61,532 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |