AP1_EMENI
ID AP1_EMENI Reviewed; 577 AA.
AC Q5AW17; C8VBJ8;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=AP-1-like transcription factor napA {ECO:0000305};
GN Name=napA {ECO:0000303|PubMed:17617701}; ORFNames=ANIA_07513;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION.
RX PubMed=17617701; DOI=10.1271/bbb.70133;
RA Asano Y., Hagiwara D., Yamashino T., Mizuno T.;
RT "Characterization of the bZip-type transcription factor NapA with reference
RT to oxidative stress response in Aspergillus nidulans.";
RL Biosci. Biotechnol. Biochem. 71:1800-1803(2007).
RN [4]
RP FUNCTION.
RX PubMed=18838792; DOI=10.1271/bbb.80001;
RA Hagiwara D., Asano Y., Yamashino T., Mizuno T.;
RT "Characterization of bZip-type transcription factor AtfA with reference to
RT stress responses of conidia of Aspergillus nidulans.";
RL Biosci. Biotechnol. Biochem. 72:2756-2760(2008).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=30863878; DOI=10.1007/s00253-019-09712-3;
RA Bermudez-Garcia E., Pena-Montes C., Martins I., Pais J., Pereira C.S.,
RA Sanchez S., Farres A.;
RT "Regulation of the cutinases expressed by Aspergillus nidulans and
RT evaluation of their role in cutin degradation.";
RL Appl. Microbiol. Biotechnol. 103:3863-3874(2019).
CC -!- FUNCTION: Transcription activator involved in oxidative stress
CC response, specifically during hyphal growth. Regulates the
CC transcription of genes encoding antioxidant enzymes and components of
CC the cellular thiol-reducing pathways including the mycelium-specific
CC catalase catB (but not the conidia-specific catalase catA), thioredoxin
CC reductase trxB and thioredoxin thiO (PubMed:17617701). Preferentially
CC binds to promoters with the core binding site 5'-TTA[CG]TAA-3'.
CC Activity of the transcription factor is controlled through oxidation of
CC specific cysteine residues resulting in the alteration of its
CC subcellular location. Activation by hydroperoxides induces nuclear
CC accumulation and as a result NapA transcriptional activity (By
CC similarity). {ECO:0000250|UniProtKB:P19880,
CC ECO:0000269|PubMed:17617701}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P19880}. Cytoplasm
CC {ECO:0000250|UniProtKB:P19880}. Note=Oxidized napA is found
CC predominantly in the nucleus, while reduced napA is continuously
CC exported to the cytoplasm by CRM1/exportin 1.
CC {ECO:0000250|UniProtKB:P19880}.
CC -!- DOMAIN: NapA contains a C-terminal cysteine rich domain (c-CRD), but
CC lacks the N-terminal CRD (n-CRD) found in the yeast homolog YAP1. It
CC probably also contains embedded in the c-CRD a nuclear export signal,
CC with which the nuclear export protein CRM1 may interact in the absence
CC of inter- or intramolecular disulfide bonds (or otherwise
CC oxidized/modified cysteines) within the c-CRD.
CC {ECO:0000250|UniProtKB:P19880, ECO:0000305|PubMed:17617701}.
CC -!- PTM: Oxidative stress induces conformational changes through oxidation
CC of cysteine residues, masking the nuclear export signal, thus
CC abolishing nuclear export by CRM1/exportin 1.
CC {ECO:0000250|UniProtKB:P19880}.
CC -!- DISRUPTION PHENOTYPE: Decreases the level of cutinase cut4 during
CC oxidative stress. {ECO:0000269|PubMed:30863878}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; BN001304; CBF79538.1; -; Genomic_DNA.
DR RefSeq; XP_680782.1; XM_675690.1.
DR AlphaFoldDB; Q5AW17; -.
DR SMR; Q5AW17; -.
DR STRING; 162425.CADANIAP00000615; -.
DR EnsemblFungi; CBF79538; CBF79538; ANIA_07513.
DR EnsemblFungi; EAA62093; EAA62093; AN7513.2.
DR GeneID; 2869524; -.
DR KEGG; ani:AN7513.2; -.
DR VEuPathDB; FungiDB:AN7513; -.
DR eggNOG; ENOG502RPD7; Eukaryota.
DR HOGENOM; CLU_011807_0_0_1; -.
DR InParanoid; Q5AW17; -.
DR OMA; DFFTPYN; -.
DR OrthoDB; 1198076at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0030436; P:asexual sporulation; IMP:AspGD.
DR GO; GO:0036184; P:asperthecin biosynthetic process; IMP:AspGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:AspGD.
DR GO; GO:1900766; P:emericellin biosynthetic process; IMP:AspGD.
DR GO; GO:1900380; P:negative regulation of asperthecin biosynthetic process; IMP:AspGD.
DR GO; GO:1900835; P:negative regulation of emericellin biosynthetic process; IMP:AspGD.
DR GO; GO:1900760; P:negative regulation of sterigmatocystin biosynthetic process; IMP:AspGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:1900793; P:shamixanthone biosynthetic process; IMP:AspGD.
DR GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
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; Nucleus; Reference proteome.
FT CHAIN 1..577
FT /note="AP-1-like transcription factor napA"
FT /id="PRO_0000441070"
FT DOMAIN 154..217
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 25..178
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 294..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..558
FT /note="c-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT MOTIF 117..124
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 144..151
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 543..550
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT COMPBIAS 25..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 63154 MW; A60818873F3533C3 CRC64;
MADYNSLYQH GLYLSPDQQD LLLAALSSNN PPSKQKQNVQ KPELGTNPTN TPGQASTGSF
NTSPAFDGSH QFDNLNYDES PFLDFNPELE WDFPGSENLI GELPGSATSD DHEVGEKRKD
SNSNGEVNGK KRRESDDKSD DKTSKKPGRK PLTSEPTSKR KAQNRAAQRA FRERKEKHLK
DLEAKVEELQ KASDSANQEN GLLKAQVERL QVELREYRKR LSWVTQGNAL SAINSYPGNA
NRMSGLNNND FMFDFPKFGD LPGGRIFNGS VAKTNQNKKD DTPIPGILRH SALQAANGRA
SSSASPKTVT SNNPATKSPV TADGRLTSHT SSVYNYHQPG QGHDTSTSDS PSSSSDSHQF
LSSSGTSPEP SVQSPDNQAK ESHEGHTCTI DGEKSFCAQL GMACGNINNP IPAVRQRSES
ATNTPNAPSS TDNVPGIDFM AQQNGGQFDP LLFGDWREPQ DAVLSQDFNT FFDDAFPLPD
LGSPSHNLTE VGLGAQQKKS ILEEMDNKEE EEVVPGEDKA QMLSCTKIWD RLQSMEKFRN
GEIDVDNLCS ELRTKARCSE GGVVVNQRDV DDIIGRV
