AP1_ASPFU
ID AP1_ASPFU Reviewed; 615 AA.
AC Q4WMH0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=AP-1-like transcription factor yap1 {ECO:0000303|PubMed:17921349};
DE AltName: Full=BZIP domain-containing transcription factor yap1 {ECO:0000303|PubMed:17921349};
GN Name=yap1 {ECO:0000303|PubMed:17921349}; ORFNames=AFUA_6G09930;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17921349; DOI=10.1128/ec.00267-07;
RA Lessing F., Kniemeyer O., Wozniok I., Loeffler J., Kurzai O., Haertl A.,
RA Brakhage A.A.;
RT "The Aspergillus fumigatus transcriptional regulator AfYap1 represents the
RT major regulator for defense against reactive oxygen intermediates but is
RT dispensable for pathogenicity in an intranasal mouse infection model.";
RL Eukaryot. Cell 6:2290-2302(2007).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18608886; DOI=10.1080/13693780802054215;
RA Qiao J., Kontoyiannis D.P., Calderone R., Li D., Ma Y., Wan Z., Li R.,
RA Liu W.;
RT "Afyap1, encoding a bZip transcriptional factor of Aspergillus fumigatus,
RT contributes to oxidative stress response but is not essential to the
RT virulence of this pathogen in mice immunosuppressed by cyclophosphamide and
RT triamcinolone.";
RL Med. Mycol. 46:773-782(2008).
RN [4]
RP FUNCTION.
RX PubMed=18651311; DOI=10.1080/13693780802169138;
RA Kniemeyer O., Lessing F., Brakhage A.A.;
RT "Proteome analysis for pathogenicity and new diagnostic markers for
RT Aspergillus fumigatus.";
RL Med. Mycol. 47:S248-S254(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20376564; DOI=10.1007/s11046-010-9309-2;
RA Qiao J., Liu W., Li R.;
RT "Truncated Afyap1 attenuates antifungal susceptibility of Aspergillus
RT fumigatus to voriconazole and confers adaptation of the fungus to oxidative
RT stress.";
RL Mycopathologia 170:155-160(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27748436; DOI=10.1038/srep35306;
RA Sheridan K.J., Lechner B.E., Keeffe G.O., Keller M.A., Werner E.R.,
RA Lindner H., Jones G.W., Haas H., Doyle S.;
RT "Ergothioneine biosynthesis and functionality in the opportunistic fungal
RT pathogen, Aspergillus fumigatus.";
RL Sci. Rep. 6:35306-35306(2016).
CC -!- FUNCTION: Transcription activator involved in oxidative stress response
CC and redox homeostasis (PubMed:17921349, PubMed:18608886,
CC PubMed:18651311, PubMed:20376564, PubMed:27748436). Regulates the
CC transcription of genes encoding antioxidant enzymes and components of
CC the cellular thiol-reducing pathways, including thioredoxin peroxidase
CC (aspF3), cytochrome peroxidase, and the protein AFUA_3G00730, which
CC appears to belong to the glutathione S-transferase family
CC (PubMed:17921349, PubMed:18651311). Proteins of the protein degradation
CC pathway are also regulated by yap1, as well the p-nitroreductase family
CC protein AFUA_5G09910 (PubMed:17921349). May be involved in antifungal
CC resistance to voriconazole (PubMed:20376564).
CC {ECO:0000269|PubMed:17921349, ECO:0000269|PubMed:18608886,
CC ECO:0000269|PubMed:18651311, ECO:0000269|PubMed:20376564,
CC ECO:0000269|PubMed:27748436}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17921349}. Cytoplasm
CC {ECO:0000269|PubMed:17921349}. 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:0000269|PubMed:17921349}.
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 -!- DISRUPTION PHENOTYPE: Leads to increased sensitivity against H(2)O(2)
CC and menadione (PubMed:17921349, PubMed:27748436). Attenuates antifungal
CC susceptibility to voriconazole (PubMed:20376564). Does not show
CC attenuated virulence in a murine model of Aspergillus infection
CC (PubMed:17921349, PubMed:18608886). {ECO:0000269|PubMed:17921349,
CC ECO:0000269|PubMed:18608886, ECO:0000269|PubMed:20376564,
CC ECO:0000269|PubMed:27748436}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL88844.1; -; Genomic_DNA.
DR RefSeq; XP_750882.1; XM_745789.1.
DR AlphaFoldDB; Q4WMH0; -.
DR SMR; Q4WMH0; -.
DR STRING; 746128.CADAFUBP00007403; -.
DR EnsemblFungi; EAL88844; EAL88844; AFUA_6G09930.
DR GeneID; 3508187; -.
DR KEGG; afm:AFUA_6G09930; -.
DR VEuPathDB; FungiDB:Afu6g09930; -.
DR eggNOG; ENOG502RPD7; Eukaryota.
DR HOGENOM; CLU_011807_0_0_1; -.
DR InParanoid; Q4WMH0; -.
DR OMA; DFFTPYN; -.
DR OrthoDB; 1198076at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:AspGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; DNA-binding; Nucleus; Oxidation;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..615
FT /note="AP-1-like transcription factor yap1"
FT /id="PRO_0000449499"
FT DOMAIN 157..220
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 27..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..183
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 185..192
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 214..364
FT /note="Transcription activation 1"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 270..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..301
FT /note="n-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 409..508
FT /note="Transcription activation 2"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 562..595
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 580..587
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT COMPBIAS 27..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 562..595
FT /note="In nuclear retained form; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT DISULFID 562..586
FT /note="In nuclear retained form; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT DISULFID 586..595
FT /note="In nuclear retained form; alternate"
FT /evidence="ECO:0000250|UniProtKB:P19880"
SQ SEQUENCE 615 AA; 66744 MW; BC70317C093C5EBB CRC64;
MADYNTLYQQ GLYLSPDQQD LLLAALSSNN PTQKQQTVTH NSEANQNLNH TPGHASSGSF
SVSPPSGLDG SVNQSTTFGY EDSPYLDLNP DFDLDFLGNE SLIGDLPPSL PSTEDYEPGD
KRKDIDGQVN DKEDSGKKRR ESDEKAAKKP GRKPLTSEPT SKRKAQNRAA QRAFRERKEK
HLKDLEAKVE ELQKASDNAN QENGLLRAQV ERLQLELKEY RKRLSWVTST SGLSPVNAIP
GAYSKGMYGL NNNEFMFDFP KFGDLPGSHL FTNTQTSKSN QNKAKDNPTA TPRSEAQVPG
VLNRNDLKIS SPNGLSNGPS PAKSTPSGQT PNSQTSTRPG SGTLNGAVDN NGAARGYQVN
SSYSASTKQA THDTPSSDSP SSSSDSHQSQ LLSSNGTSPE PSLHSPAVKA TESSTPHACT
YTTINGEESF CAQLSMACGN INNPIPAVRQ NSESASNTPS HANSSDKALG LDFFAQQNGG
QFDPVLFGDW REPQDAILSQ DFGTFFDDAF PLPDLGSPSH NFSEATKQPA APKKDLIAEI
DSKLDEDEEV VPGEDKSQML TCNKIWDRLQ SMEKFRNGEI DVDNLCSELR TKARCSEGGV
VVNQKDVEDI MGRVK
