ID   HAC1_EMENI              Reviewed;         350 AA.
AC   Q8TFU8; C8VRK0; Q5AQN3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Transcriptional activator hacA;
GN   Name=hacA; ORFNames=AN9397;
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 [GENOMIC DNA], ALTERNATIVE SPLICING, AND INDUCTION.
RC   STRAIN=FGSC 26;
RX   PubMed=12581366; DOI=10.1046/j.1365-2958.2003.03363.x;
RA   Saloheimo M.L.A., Valkonen M., Penttilae M.E.;
RT   "Activation mechanisms of the HAC1-mediated unfolded protein response in
RT   filamentous fungi.";
RL   Mol. Microbiol. 47:1149-1161(2003).
RN   [2]
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   [3]
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).
CC   -!- FUNCTION: Transcriptional activator involved in the unfolded protein
CC       response (UPR) pathway. Recognizes and binds to the UPR element (UPRE)
CC       in the promoter of UPR-regulated genes. Increases the synthesis of
CC       endoplasmic reticulum-resident proteins required for protein folding as
CC       well as components of the secretory pathway (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Splicing occurs by a non-spliceosomal, regulated splicing
CC         mechanism when UPR is induced.;
CC       Name=I; Synonyms=Induced;
CC         IsoId=Q8TFU8-1; Sequence=Displayed;
CC       Name=U; Synonyms=Uninduced;
CC         IsoId=Q8TFU8-2; Sequence=VSP_020903;
CC   -!- INDUCTION: By the unfolded protein response pathway. Accumulation of
CC       unfolded proteins in the ER leads to splicing of the hacA precursor
CC       mRNA to produce the mature form. {ECO:0000269|PubMed:12581366}.
CC   -!- MISCELLANEOUS: [Isoform I]: Induced and active isoform.
CC   -!- MISCELLANEOUS: [Isoform U]: Probably not translated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA66464.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ413273; CAC88375.1; -; Genomic_DNA.
DR   EMBL; AACD01000172; EAA66464.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF87535.1; -; Genomic_DNA.
DR   RefSeq; XP_682666.1; XM_677574.1.
DR   AlphaFoldDB; Q8TFU8; -.
DR   SMR; Q8TFU8; -.
DR   STRING; 162425.CADANIAP00001184; -.
DR   EnsemblFungi; CBF87535; CBF87535; ANIA_09397. [Q8TFU8-2]
DR   EnsemblFungi; EAA66464; EAA66464; AN9397.2.
DR   GeneID; 2867859; -.
DR   KEGG; ani:AN9397.2; -.
DR   eggNOG; ENOG502S526; Eukaryota.
DR   HOGENOM; CLU_035741_0_0_1; -.
DR   InParanoid; Q8TFU8; -.
DR   OMA; TMAWAID; -.
DR   OrthoDB; 815295at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR044280; Hac1/HY5.
DR   PANTHER; PTHR46714; PTHR46714; 1.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Unfolded protein response.
FT   CHAIN           1..350
FT                   /note="Transcriptional activator hacA"
FT                   /id="PRO_0000252296"
FT   DOMAIN          87..150
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..142
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          143..150
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          152..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         222..350
FT                   /note="VSVGGLEGDESALTLFDLGASIKHEPTHDLTAPLSDDDFRRLFNGDSSLESD
FT                   SSLLEDGFAFDVLDSGDLSAFPFDSMVDFDTEPVTLEDLEQTNGLSDSASCKAASLQPS
FT                   HGASTSRCDGQGIAAGSA -> AMLCDLQCQSAGSKEMKVPSRFSTSEPALSMSLHMTL
FT                   QLLFLTMTSAAYSTVIHPLSQILHSLKTGSPLTFSTQEIYQHFHLILWLILTPSLSPSK
FT                   ISSKPTAFRIQLLARLLACNPAMARPLRDATGRALQLAVRERFSTEDRLVPDVVEGRWS
FT                   WESLLTLASAINLLEKPERRRRTLRGLDSLKRGRRIDSGKRYRVIRSSRSSTSPREALT
FT                   SRRKGL (in isoform U)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_020903"
FT   CONFLICT        41
FT                   /note="Q -> R (in Ref. 1; CAC88375)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   350 AA;  38164 MW;  BFB62AD097D706F9 CRC64;
     MKSADRFSPV KMEDAFANSL PTTPSLEVPV LTVSPADTSL QTKNVVAQTK PEEKKPAKKR
     KSWGQELPVP KTNLPPRKRA KTEDEKEQRR IERVLRNRAA AQTSRERKRL EMEKLESEKI
     DMEQQNQFLL QRLAQMEAEN NRLSQQVAQL SAEVRGSRHS TPTSSSPASV SPTLTPTLFK
     QEGDEVPLDR IPFPTPSVTD YSPTLKPSSL AESPDLTQHP AVSVGGLEGD ESALTLFDLG
     ASIKHEPTHD LTAPLSDDDF RRLFNGDSSL ESDSSLLEDG FAFDVLDSGD LSAFPFDSMV
     DFDTEPVTLE DLEQTNGLSD SASCKAASLQ PSHGASTSRC DGQGIAAGSA