ID   HAC1_HYPJE              Reviewed;         451 AA.
AC   Q8TFF3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Transcriptional activator hac1;
GN   Name=hac1;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND INDUCTION.
RC   STRAIN=ATCC 56765 / Rut C-30;
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).
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=Q8TFF3-1; Sequence=Displayed;
CC       Name=U; Synonyms=Uninduced;
CC         IsoId=Q8TFF3-2; Sequence=VSP_020904;
CC   -!- INDUCTION: By the unfolded protein response pathway. Accumulation of
CC       unfolded proteins in the ER leads to splicing of the hac1 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}.
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DR   EMBL; AJ413272; CAC88374.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TFF3; -.
DR   SMR; Q8TFF3; -.
DR   OMA; PMIKFED; -.
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   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; DNA-binding; Nucleus; Transcription;
KW   Transcription regulation; Unfolded protein response.
FT   CHAIN           1..451
FT                   /note="Transcriptional activator hac1"
FT                   /id="PRO_0000252297"
FT   DOMAIN          118..181
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..140
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          146..153
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          228..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         296..451
FT                   /note="VSIGGDAAVPVFSDDAGANCLGLDPVHQDDGPFSIGHSFGLSAALDADRYLL
FT                   ESQLLASPNASTVDDDYLAGDSAACFTNPLPSDYDFDINDFLTDDANHAAYDIVAASNY
FT                   AAADRELDLEIHDPENQIPSRHSIQQPQSGASSHGCDDGGIAVGV -> EMLCDPQCQS
FT                   VEMPLSLSSQTTPAQTALAWTLFIRMMVLSASAILSACQRPLMQIAISSKANFSLRPTP
FT                   QLLTTIIWLVTLPPASRILSPPTTTSTSTTSSQTTQTTPPMTLWQRATMPLRTASSTSR
FT                   STTLRIRSLRDILSSSPSLARPLMDATMAALRLVSEGRDDRGGIPASESCATRGDCELE
FT                   RCLRSVTLPSREVLITLWWAVKVEERRIRLRQHKKQAAALDPEKRASLADKKNRQQQQQ
FT                   QHQYQIPSFSK (in isoform U)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_020904"
SQ   SEQUENCE   451 AA;  49278 MW;  600F10E471EA3AD3 CRC64;
     MAFQQSSPLV KFEASPAESF LSAPGDNFTS LFADSTPSTL NPRDMMTPDS VADIDSRLSV
     IPESQDAEDD ESHSTSATAP STSEKKPVKK RKSWGQVLPE PKTNLPPRKR AKTEDEKEQR
     RVERVLRNRR AAQSSRERKR LEVEALEKRN KELETLLINV QKTNLILVEE LNRFRRSSGV
     VTRSSSPLDS LQDSITLSQQ LFGSRDGQTM SNPEQSLMDQ IMRSAANPTV NPASLSPSLP
     PISDKEFQTK EEDEEQADED EEMEQTWHET KEAAAAKEKN SKQSRVSTDS TQRPAVSIGG
     DAAVPVFSDD AGANCLGLDP VHQDDGPFSI GHSFGLSAAL DADRYLLESQ LLASPNASTV
     DDDYLAGDSA ACFTNPLPSD YDFDINDFLT DDANHAAYDI VAASNYAAAD RELDLEIHDP
     ENQIPSRHSI QQPQSGASSH GCDDGGIAVG V