AP1_ASPOR
ID AP1_ASPOR Reviewed; 563 AA.
AC Q2UMT9;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=AP-1-like transcription factor yap1 {ECO:0000303|PubMed:31366149};
DE AltName: Full=BZIP domain-containing transcription factor yap1 {ECO:0000303|PubMed:31366149};
GN Name=yap1 {ECO:0000303|PubMed:31366149}; ORFNames=AO090001000627;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, AND INDUCTION.
RX PubMed=31366149; DOI=10.3390/microorganisms7080225;
RA Shao H., Tu Y., Wang Y., Jiang C., Ma L., Hu Z., Wang J., Zeng B., He B.;
RT "Oxidative stress response of Aspergillus oryzae induced by hydrogen
RT peroxide and menadione sodium bisulfite.";
RL Microorganisms 7:0-0(2019).
CC -!- FUNCTION: Transcription activator involved in oxidative stress response
CC and redox homeostasis (PubMed:31366149). Regulates the transcription of
CC genes encoding antioxidant enzymes and components of the cellular
CC thiol-reducing pathways (By similarity). {ECO:0000250|UniProtKB:Q4WMH0,
CC ECO:0000269|PubMed:31366149}.
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 -!- INDUCTION: Expression is enhanced upon oxidative stress stimuli.
CC {ECO:0000269|PubMed:31366149}.
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; AP007154; BAE57126.1; -; Genomic_DNA.
DR RefSeq; XP_001819128.1; XM_001819076.2.
DR AlphaFoldDB; Q2UMT9; -.
DR SMR; Q2UMT9; -.
DR STRING; 510516.Q2UMT9; -.
DR EnsemblFungi; BAE57126; BAE57126; AO090001000627.
DR GeneID; 5991099; -.
DR KEGG; aor:AO090001000627; -.
DR VEuPathDB; FungiDB:AO090001000627; -.
DR HOGENOM; CLU_011807_0_0_1; -.
DR OMA; DFFTPYN; -.
DR Proteomes; UP000006564; Chromosome 2.
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; 1.
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 2: Evidence at transcript level;
KW Cytoplasm; Disulfide bond; DNA-binding; Nucleus; Oxidation;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..563
FT /note="AP-1-like transcription factor yap1"
FT /id="PRO_0000449501"
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..380
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..459
FT /note="Transcription activation 2"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 394..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..543
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 528..535
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..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 510..543
FT /note="In nuclear retained form; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT DISULFID 510..534
FT /note="In nuclear retained form; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT DISULFID 534..543
FT /note="In nuclear retained form; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19880"
SQ SEQUENCE 563 AA; 61681 MW; 5CBE090EBC44DA2D 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 STIDAVRGKS ESVSNTPSQP NNNYEQTPGP
GLDLLAQQNG GQFDPVLFGD WREPQDAILS QDFGTFFDDA FPLPDLGSPS HNFNEVANPQ
PPKKDLIAEI DNKLDEEVVP GEDKSQMLSC TKIWDRLQSM EKFRNGEIDV DNLCSELRTK
ARCSEGGVVV NQKDVEDIMG RVK
