ID HAC1_ASPOR Reviewed; 345 AA.
AC Q1XGE2; Q2U743;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 22-FEB-2023, entry version 84.
DE RecName: Full=Transcriptional activator hacA;
GN Name=hacA; ORFNames=AO090124000074;
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 [MRNA] (ISOFORM I).
RC STRAIN=ATCC 42149 / RIB 40;
RA Maruyama J., Nakajima K., Ohno A., Higuchi Y., Arioka M., Abe K.,
RA Kitamoto K.;
RT "Aspergillus oryzae hacA mRNA under the ER stress condition.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
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=Q1XGE2-1; Sequence=Displayed;
CC Name=U; Synonyms=Uninduced;
CC IsoId=Q1XGE2-2; Sequence=VSP_020902;
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.
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=BAE62622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB246349; BAE93063.1; -; mRNA.
DR EMBL; AP007165; BAE62622.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001823755.2; XM_001823703.2.
DR AlphaFoldDB; Q1XGE2; -.
DR SMR; Q1XGE2; -.
DR STRING; 510516.Q1XGE2; -.
DR OrthoDB; 2681518at2759; -.
DR Proteomes; UP000006564; Chromosome 5.
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 CDD; cd14710; bZIP_HAC1-like; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR044280; Hac1/HY5.
DR PANTHER; PTHR46714; TRANSCRIPTIONAL ACTIVATOR HAC1; 1.
DR PANTHER; PTHR46714:SF6; TRANSCRIPTIONAL ACTIVATOR HAC1; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 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..345
FT /note="Transcriptional activator hacA"
FT /id="PRO_0000252295"
FT DOMAIN 83..146
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..138
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 139..146
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 186..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 218..345
FT /note="VSVAGLEGDGSALPLFDLGSDLKHHSTDDVAAPLSDDDFNRLFHGDSSVEPD
FT SSVFEDGLAFDVLEGGDLSAFPFDSMVNFDSEPVTLEGIEMAHGLPDETTCKTSSVQPG
FT FGASTTRCDGQGIAAGC -> AVLCDLQCPSLDSKEMEAPSHFSTSAQTLNITLQMTLQ
FT LLFLTMTSTAYSTVIHPLNQILLSLKTGLPLMFSKEEIYQHFHLILWLISTPSLSPSKA
FT SRWPTGFRMRLLARLLACNPALARPLRDATGRALQLAVSENFSQGSMSVTDTQRSRWSW
FT ESLLTLSWAIDRLENPRRRRRILHGLRTSQIDRRNNLGKRQRSIRSTWSSNNTETLTSP
FT LTGKDC (in isoform U)"
FT /evidence="ECO:0000305"
FT /id="VSP_020902"
SQ SEQUENCE 345 AA; 37563 MW; BDC0FBCD69CE73B1 CRC64;
MSCDMEKTMS SVDSLPATPA SEVPVLTVSP ADTSLNSADV KTQEVKPEEK KPAKKRKSWG
QELPVPKTNL PPRKRAKTED EKEQRRIERV LRNRAAAQTS RERKRLEMEK LENEKIQMEQ
QNQFLLQRLS QMEAENNRLS QQLAQLAAEV RGSRANTPMP GSPATASPTL TPTLFKQERD
ELPLERIPFP TPSLSDYSPT LKPSTLAESS DVAQHPAVSV AGLEGDGSAL PLFDLGSDLK
HHSTDDVAAP LSDDDFNRLF HGDSSVEPDS SVFEDGLAFD VLEGGDLSAF PFDSMVNFDS
EPVTLEGIEM AHGLPDETTC KTSSVQPGFG ASTTRCDGQG IAAGC
//
