ATFB_ASPPU
ID ATFB_ASPPU Reviewed; 318 AA.
AC A0A0F0IP79; F1CLM8;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Basic leucine zipper (bZIP) transcription factor atfB {ECO:0000303|PubMed:21808056};
GN Name=atfB {ECO:0000303|PubMed:21808056}; ORFNames=P875_00075906;
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DNA-BINDING.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=21808056; DOI=10.1074/jbc.m111.253468;
RA Roze L.V., Chanda A., Wee J., Awad D., Linz J.E.;
RT "Stress-related transcription factor AtfB integrates secondary metabolism
RT with oxidative stress response in aspergilli.";
RL J. Biol. Chem. 286:35137-35148(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=23281343; DOI=10.1002/mbo3.63;
RA Hong S.Y., Roze L.V., Wee J., Linz J.E.;
RT "Evidence that a transcription factor regulatory network coordinates
RT oxidative stress response and secondary metabolism in aspergilli.";
RL MicrobiologyOpen 2:144-160(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28926946; DOI=10.3390/toxins9090287;
RA Wee J., Hong S.Y., Roze L.V., Day D.M., Chanda A., Linz J.E.;
RT "The fungal bZIP transcription factor AtfB controls virulence-associated
RT processes in Aspergillus parasiticus.";
RL Toxins 9:0-0(2017).
CC -!- FUNCTION: Transcription factor that acts as a key player in the
CC regulatory circuit that integrates secondary metabolism and cellular
CC response to oxidative stress (PubMed:21808056). Regulates the genes
CC involved in development, stress response, and secondary metabolism
CC through direct binding to their promoters (PubMed:23281343,
CC PubMed:28926946). Particularly involved in the resistance to oxidative
CC stress in asexual conidiospores (PubMed:23281343). Binds aflatoxin gene
CC promoters carrying the cAMP-response element (CRE1) under aflatoxin-
CC inducing conditions (PubMed:21808056, PubMed:23281343).
CC {ECO:0000269|PubMed:21808056, ECO:0000269|PubMed:23281343,
CC ECO:0000269|PubMed:28926946}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- DISRUPTION PHENOTYPE: Leads to a decrease in aflatoxin enzyme levels,
CC down-regulation of aflatoxin accumulation, and impaired conidiospore
CC development (PubMed:28926946). {ECO:0000269|PubMed:28926946}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; HQ396161; ADZ06147.1; -; Genomic_DNA.
DR EMBL; JZEE01000036; KJK68567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0IP79; -.
DR SMR; A0A0F0IP79; -.
DR STRING; 1403190.A0A0F0IP79; -.
DR EnsemblFungi; KJK68567; KJK68567; P875_00075906.
DR Proteomes; UP000033540; 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:1900179; P:positive regulation of aflatoxin biosynthetic process; IDA:GO_Central.
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 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..318
FT /note="Basic leucine zipper (bZIP) transcription factor
FT atfB"
FT /id="PRO_0000444003"
FT DOMAIN 160..223
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 79..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..199
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 202..216
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 247..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 308
FT /note="T -> S (in Ref. 1; ADZ06147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 35873 MW; 81D4FD2F605AFE68 CRC64;
MSVDQTLYSR ARAAMADPTC AGPATFTAAG AFSQPDLMAF SLPEEEPIWG FDTIAPSMAS
WQGKMEQQTF CNPNMERGLK NTHVRNGQPT PPPFDDKKLQ TPMGEMYPVA QYAFNSSPPE
YAPPKHRSSL SEQSQTDGYG VSTRRRKASA VDQSEQQQDR EKREKFLERN RLAASKCRQK
KKEHTKLLET RFREVSSKKG ELESEIEHLR SEVLNLKNEM LRHAQCGDEA IKIHLAQMVR
LITSKDTPNR DLVSPMRSPE QMTASTPHGL SFGFDGPMQL PSEMGSPLDQ RRDSEQSIMT
ESSYTFSTDD SFEELINV
