ID   ATFC_BOMMO              Reviewed;         236 AA.
AC   Q9GPH3;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Activating transcription factor of chaperone {ECO:0000303|PubMed:15530439};
GN   Name=ATFC {ECO:0000303|PubMed:15530439};
GN   Synonyms=ATF {ECO:0000312|EMBL:AAG45935.1};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAG45935.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX   PubMed=15530439; DOI=10.1016/j.bbrc.2004.10.069;
RA   Goo T.W., Yun E.Y., Choi K.H., Kim S.H., Nho S.K., Kang S.W., Kwon O.Y.;
RT   "ATFC is a novel transducer for the unfolded protein response in Bombyx
RT   mori BM5 cells.";
RL   Biochem. Biophys. Res. Commun. 325:626-631(2004).
CC   -!- FUNCTION: Transcriptional activator that acts in the unfolded protein
CC       response (UPR) pathway. Acts during endoplasmic reticulum (ER) stress
CC       by activating UPR target genes via direct binding to the UPR element
CC       (UPRE) (5'-GGAACTGGACAGCGTGTCGAAA-3'). Activates expression of ER
CC       chaperones ERP72 and PDI. {ECO:0000269|PubMed:15530439}.
CC   -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250|UniProtKB:P18846}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- INDUCTION: By ER stress-inducing agents tunicamycin, DTT, the calcium
CC       ionophore A23187, antimycin, monensin and H(2)O(2).
CC       {ECO:0000269|PubMed:15530439}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000255}.
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DR   EMBL; AF325210; AAG45935.1; -; mRNA.
DR   RefSeq; NP_001037041.1; NM_001043576.1.
DR   AlphaFoldDB; Q9GPH3; -.
DR   SMR; Q9GPH3; -.
DR   GeneID; 692594; -.
DR   KEGG; bmor:692594; -.
DR   CTD; 692594; -.
DR   InParanoid; Q9GPH3; -.
DR   OrthoDB; 1117408at2759; -.
DR   Proteomes; UP000005204; 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:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF00170; bZIP_1; 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; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Unfolded protein response.
FT   CHAIN           1..236
FT                   /note="Activating transcription factor of chaperone"
FT                   /id="PRO_0000390498"
FT   DOMAIN          165..228
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          117..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..187
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          193..228
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        121..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   236 AA;  26127 MW;  183E61B84776C409 CRC64;
     MSCRAMVSPP SRTARAGAVL ASSPFVTSQP TEELLREFET VYGAVELTHL TPPQSPPGPA
     TQLLLSYAQQ AQCTALAPPA PLAPPQEAWQ IVAPVPVNQL PEGYECDLDA VEELVRHRAS
     QLASPQHSSS SANASPRSSP PPSPRSSSTD EDWSAPSRLK TRPVDDRRSR KKEQNKNAAT
     RYRQKKKAEV EVLLKEEQTL RQRHTELGEK CSDLQREIRY LKALMRDLFK AKGLIK