AP1_ASPFN
ID AP1_ASPFN Reviewed; 584 AA.
AC B8NNN3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=AP-1-like transcription factor yap1 {ECO:0000303|PubMed:30126960};
DE AltName: Full=BZIP domain-containing transcription factor yap1 {ECO:0000303|PubMed:30126960};
GN Name=yap1 {ECO:0000303|PubMed:30126960}; ORFNames=AFLA_129340;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF LEU-558.
RX PubMed=30126960; DOI=10.1128/aac.01216-18;
RA Ukai Y., Kuroiwa M., Kurihara N., Naruse H., Homma T., Maki H., Naito A.;
RT "Contributions of yap1 mutation and subsequent atrF upregulation to
RT voriconazole resistance in Aspergillus flavus.";
RL Antimicrob. Agents Chemother. 62:0-0(2018).
CC -!- FUNCTION: Transcription activator involved in oxidative stress response
CC and redox homeostasis (By similarity). Regulates the transcription of
CC genes encoding antioxidant enzymes and components of the cellular
CC thiol-reducing pathways (By similarity). May be involved in antifungal
CC resistance to voriconazole (PubMed:30126960).
CC {ECO:0000250|UniProtKB:Q4WMH0, ECO:0000269|PubMed:30126960}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q4WMH0}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q4WMH0}. Note=The nuclear localization is
CC oxidative stress-dependent and oxidized yap1 is found predominantly in
CC the nucleus, while reduced yap1 is continuously exported to the
CC cytoplasm. {ECO:0000250|UniProtKB:Q4WMH0}.
CC -!- DOMAIN: Contains two cysteine rich domains (CRD), referred to as the
CC N- and C-terminal CRD's, n-CRD and c-CRD, respectively. A nuclear
CC export signal is embedded in the c-CRD, with which the nuclear export
CC proteins interact only in the absence of disulfide bonds (or otherwise
CC oxidized cysteines) within the c-CRD or between the c-CRD and the n-
CC CRD. {ECO:0000250|UniProtKB:P19880}.
CC -!- PTM: Depending on the oxidative stress inducing agent, yap1 can undergo
CC two distinct conformational changes, both involving disulfide bond
CC formation, and both masking the nuclear export signal, thus abolishing
CC nuclear export. {ECO:0000250|UniProtKB:P19880}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; EQ963481; EED48711.1; -; Genomic_DNA.
DR RefSeq; XP_002382127.1; XM_002382086.1.
DR AlphaFoldDB; B8NNN3; -.
DR SMR; B8NNN3; -.
DR STRING; 5059.CADAFLAP00009992; -.
DR EnsemblFungi; EED48711; EED48711; AFLA_129340.
DR VEuPathDB; FungiDB:AFLA_129340; -.
DR eggNOG; ENOG502RPD7; Eukaryota.
DR HOGENOM; CLU_011807_0_0_1; -.
DR OMA; DFFTPYN; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013910; TF_PAP1.
DR InterPro; IPR023167; Yap1_redox_dom_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF08601; PAP1; 2.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF111430; SSF111430; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; DNA-binding; Nucleus; Transcription;
KW Transcription regulation.
FT CHAIN 1..584
FT /note="AP-1-like transcription factor yap1"
FT /id="PRO_0000449500"
FT DOMAIN 154..217
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 23..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..180
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 182..189
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 211..332
FT /note="Transcription activation 1"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 267..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..296
FT /note="n-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 377..480
FT /note="Transcription activation 2"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 418..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..564
FT /note="c-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT MOTIF 35..42
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 68..75
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 549..556
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT COMPBIAS 23..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 531..564
FT /note="In nuclear retained form; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT DISULFID 531..555
FT /note="In nuclear retained form; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT DISULFID 555..564
FT /note="In nuclear retained form; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT MUTAGEN 558
FT /note="L->W: Leads to the up-regulation of the expression
FT of atrF and subsequent resistance to voriconazole."
FT /evidence="ECO:0000269|PubMed:30126960"
SQ SEQUENCE 584 AA; 63771 MW; 94EEA497F5EF38F8 CRC64;
MADYNTLYHQ GLYLSPDQQD LLLAALSSNQ PPQKQQNDKQ RSQAKTDPDS TPGNMSSGSF
SMSPGFNKTH PGSGGLGYGD DESPFLDFNP ELDFDFPGSE NLIGDLPGSL PSEEHEVGEK
RKDMSDNENE ESGKKRRESD DKAAKKPGRK PLTSEPTSKR KAQNRAAQRA FRERKEKHLK
DLETKVDELQ KASDDANQEN GLLRAQVERL QVELREYRKR LSWLTTGSGI SAMSAIPSAH
SRNLYGLNNN DFMFDFPKFG DLPGGHIFNG PLTKSNQNKP RDGSSPATSD SQVPGVMTRE
TLNGSNNRGM PTAKAANGVS NNPSPKVPSV YNIRQSASSH DSSNSCSPSS SSDSHQSQML
SSNGTSPEPS SNSPATKLND SVQNHHACTY STIDGEASFC AQLGMACGNI NNPIPAVRGK
SESVSNTPSQ PNNNYEQTPG PGLDLLAQQN GGQFDPVLFG DWREPQDAIL SQDFGTFFDD
AFPLPDLGSP SHNFNEVANP QPPKKDLIAE IDNKLDEEVV PGEDKSQMLS CTKIWDRLQS
MEKFRNGEID VDNLCSELRT KARCSEGGVV VNQKDVEDIM GRVK
