UniProt functional annotation for Q01663



	UniProt functional annotation for Q01663

UniProt code: Q01663.

Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.

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}.

Subunit: Homodimer (PubMed:11017199). The reduced form of pap1 interacts in the nucleus with the nuclear export protein crm1, and in the cytoplasm with the peroxiredoxin tpx1 (PubMed:12100563, PubMed:24316080). {ECO:0000269|PubMed:11017199, ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:24316080}.

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}.

Domain: Contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD (Cys-259, Cys-278, Cys-285 and Cys-290) and c-CRD (Cys-501, Cys-523 and Cys-532), respectively. Cys-259 and Cys-290 are not conserved in orthologs in other yeast species. A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein crm1/exportin 1 interacts only in the absence of disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or between the c-CRD and the n-CRD. {ECO:0000269|PubMed:12100563, ECO:0000269|PubMed:23525001}.

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}.

Similarity: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.



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}.


Subunit:		Homodimer (PubMed:11017199). The reduced form of pap1 interacts in the nucleus with the nuclear export protein crm1, and in the cytoplasm with the peroxiredoxin tpx1 (PubMed:12100563, PubMed:24316080). {ECO:0000269\|PubMed:11017199, ECO:0000269\|PubMed:12100563, ECO:0000269\|PubMed:24316080}.
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}.
Domain:		Contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD (Cys-259, Cys-278, Cys-285 and Cys-290) and c-CRD (Cys-501, Cys-523 and Cys-532), respectively. Cys-259 and Cys-290 are not conserved in orthologs in other yeast species. A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein crm1/exportin 1 interacts only in the absence of disulfide bonds (or otherwise oxidized cysteines) within the c-CRD or between the c-CRD and the n-CRD. {ECO:0000269\|PubMed:12100563, ECO:0000269\|PubMed:23525001}.
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}.
Similarity:		Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.