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Protein

AP-1-like transcription factor

Gene

pap1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

GO - Biological processi

  • cellular response to caffeine Source: PomBase
  • cellular response to hydrogen peroxide Source: PomBase
  • cellular response to oxidative stress Source: PomBase
  • positive regulation of transcription from RNA polymerase II promoter Source: PomBase
  • positive regulation of transcription from RNA polymerase II promoter in response to heat stress Source: PomBase
  • positive regulation of transcription from RNA polymerase II promoter in response to increased salt Source: PomBase
  • positive regulation of transcription from RNA polymerase II promoter in response to menadione Source: PomBase
  • positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: PomBase
  • regulation of transcription from RNA polymerase II promoter Source: PomBase

Keywordsi

Molecular functionActivator, DNA-binding
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1-like transcription factor
Alternative name(s):
Caffeine resistance protein 3
Gene namesi
Name:pap1
Synonyms:caf3
ORF Names:SPAC1783.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1783.07c.
PomBaseiSPAC1783.07c. pap1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi259C → S: No effect. 1 Publication1
Mutagenesisi278C → A: Constitutively cytoplasmic. 2 Publications1
Mutagenesisi285C → S: Constitutively cytoplasmic. 1 Publication1
Mutagenesisi501C → A: Constitutively cytoplasmic. 2 Publications1
Mutagenesisi517F → A: Impairs nuclear export; when associated with A-519. 1 Publication1
Mutagenesisi519I → A: Weakens nuclear export. Impairs nuclear export; when associated with A-517. 1 Publication1
Mutagenesisi522L → A: Impairs nuclear export. 1 Publication1
Mutagenesisi523C → A: No effect. 1 Publication1
Mutagenesisi523C → S: Impairs nuclear export; when associated with S-532. 1 Publication1
Mutagenesisi526L → A: Impairs nuclear export. 1 Publication1
Mutagenesisi532C → S: Weakens nuclear export. Impairs nuclear export; when associated with S-523. 1 Publication1
Mutagenesisi532C → T: Constitutively cytoplasmic. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000765321 – 552AP-1-like transcription factorAdd BLAST552

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi278 ↔ 501In nuclear retained form2 Publications
Disulfide bondi285 ↔ 532In nuclear retained formBy similarity

Post-translational modificationi

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-501.3 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ01663.
PRIDEiQ01663.

PTM databases

iPTMnetiQ01663.

Interactioni

Subunit structurei

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).3 Publications

Protein-protein interaction databases

BioGridi278616. 63 interactors.
IntActiQ01663. 1 interactor.
MINTiMINT-4693342.
STRINGi4896.SPAC1783.07c.1.

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi80 – 125Combined sources46
Helixi128 – 138Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GD2X-ray2.00E/F/G/H/I/J71-140[»]
ProteinModelPortaliQ01663.
SMRiQ01663.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01663.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 139bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni81 – 102Basic motifPROSITE-ProRule annotationAdd BLAST22
Regioni104 – 111Leucine-zipperPROSITE-ProRule annotation8
Regioni259 – 290n-CRD1 PublicationAdd BLAST32
Regioni501 – 532c-CRD1 PublicationAdd BLAST32

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi81 – 88Nuclear localization signalPROSITE-ProRule annotation8
Motifi515 – 533Nuclear export signal1 PublicationAdd BLAST19

Domaini

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.2 Publications

Sequence similaritiesi

Belongs to the bZIP family. YAP subfamily.Curated

Phylogenomic databases

InParanoidiQ01663.
KOiK09043.
OMAiQFDPQLF.
OrthoDBiEOG092C4KCZ.
PhylomeDBiQ01663.

Family and domain databases

Gene3Di1.10.238.100. 1 hit.
InterProiView protein in InterPro
IPR004827. bZIP.
IPR013910. TF_PAP1.
IPR023167. Yap1_redox_dom.
PfamiView protein in Pfam
PF00170. bZIP_1. 1 hit.
PF08601. PAP1. 1 hit.
SMARTiView protein in SMART
SM00338. BRLZ. 1 hit.
SUPFAMiSSF111430. SSF111430. 1 hit.
PROSITEiView protein in PROSITE
PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q01663-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGQTETLSS TSNIPIAKAE PEQSADFSAS HKKRGPVSDR SSRRTSSEEV
60 70 80 90 100
DLMPNVDDEV DGDVKPKKIG RKNSDQEPSS KRKAQNRAAQ RAFRKRKEDH
110 120 130 140 150
LKALETQVVT LKELHSSTTL ENDQLRQKVR QLEEELRILK DGSFTFEMSL
160 170 180 190 200
PHRNPSLSSL PTTGFSSNFA HMKDGISPQS NLHLSPNSIE KPNMHQNVLH
210 220 230 240 250
NDRSADNLNH RYQVPPTLVD SNSAQGTLSP ETPSSSDSPS NLYLNYPKRK
260 270 280 290 300
SITHLHHDCS ALSNGENGED VADGKQFCQK LSTACGSIAC SMLTKTTPHR
310 320 330 340 350
ASVDILSNLH ESTVSPPMAD ESVQRSSEVS KSIPNVELSL NVNQQFVSPF
360 370 380 390 400
GGTDSFPLPT DTGLDSLFEP DSAIENSHLK NVVMEPELFQ AWREPAESLD
410 420 430 440 450
KEFFNDEGEI DDVFHNYFHN SNENGDLITN SLHGLDFLEN ANESFPEQMY
460 470 480 490 500
PFIKHNKDYI SNHPDEVPPD GLPQKGKHDT SSQMPSENEI VPAKERAYLS
510 520 530 540 550
CPKVWSKIIN HPRFESFDID DLCSKLKNKA KCSSSGVLLD ERDVEAALNQ

FN
Length:552
Mass (Da):61,532
Last modified:August 14, 2001 - v2
Checksum:iD9E7FEA0A286B4BE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti166S → P in CAA40363 (PubMed:1899230).Curated1
Sequence conflicti280 – 281KL → NV in CAA40363 (PubMed:1899230).Curated2
Sequence conflicti543 – 552DVEAALNQFN → RC in CAA40363 (PubMed:1899230).Curated10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57078 Genomic DNA. Translation: CAA40363.1.
CU329670 Genomic DNA. Translation: CAB66170.1.
AB027778 Genomic DNA. Translation: BAA87082.1.
PIRiS15664.
T50109.
RefSeqiNP_593662.1. NM_001019094.2.

Genome annotation databases

EnsemblFungiiSPAC1783.07c.1; SPAC1783.07c.1:pep; SPAC1783.07c.
GeneIDi2542140.
KEGGispo:SPAC1783.07c.

Entry informationi

Entry nameiAP1_SCHPO
AccessioniPrimary (citable) accession number: Q01663
Secondary accession number(s): Q9US23, Q9UU69
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: August 14, 2001
Last modified: October 25, 2017
This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families