AFLR_ASPPU
ID AFLR_ASPPU Reviewed; 444 AA.
AC Q6UEG8;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Aflatoxin biosynthesis regulatory protein {ECO:0000305};
DE AltName: Full=Aflatoxin biosynthesis protein R {ECO:0000303|PubMed:15006741};
GN Name=aflR {ECO:0000303|PubMed:15006741};
GN Synonyms=apa-2 {ECO:0000303|PubMed:8250554};
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], AND FUNCTION.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=8250554; DOI=10.1128/aem.59.10.3273-3279.1993;
RA Chang P.-K., Cary J.W., Bhatnagar D., Cleveland T.E., Bennett J.W.,
RA Linz J.E., Woloshuk C.P., Payne G.A.;
RT "Cloning of the Aspergillus parasiticus apa-2 gene associated with the
RT regulation of aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 59:3273-3279(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND NOMENCLATURE.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=15006741; DOI=10.1128/aem.70.3.1253-1262.2004;
RA Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D., Cleveland T.E.,
RA Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
RT "Clustered pathway genes in aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 70:1253-1262(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=15094053; DOI=10.1016/s0014-5793(04)00327-8;
RA Yu J., Bhatnagar D., Cleveland T.E.;
RT "Completed sequence of aflatoxin pathway gene cluster in Aspergillus
RT parasiticus.";
RL FEBS Lett. 564:126-130(2004).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=7793958; DOI=10.1128/aem.61.6.2372-2377.1995;
RA Chang P.K., Ehrlich K.C., Yu J., Bhatnagar D., Cleveland T.E.;
RT "Increased expression of Aspergillus parasiticus aflR, encoding a sequence-
RT specific DNA-binding protein, relieves nitrate inhibition of aflatoxin
RT biosynthesis.";
RL Appl. Environ. Microbiol. 61:2372-2377(1995).
RN [6]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=10216264; DOI=10.1016/s0378-1119(99)00075-x;
RA Ehrlich K.C., Montalbano B.G., Cary J.W.;
RT "Binding of the C6-zinc cluster protein, AFLR, to the promoters of
RT aflatoxin pathway biosynthesis genes in Aspergillus parasiticus.";
RL Gene 230:249-257(1999).
RN [7]
RP FUNCTION.
RX PubMed=11913765; DOI=10.1023/a:1015211915310;
RA Chang P.K., Bennett J.W., Cotty P.J.;
RT "Association of aflatoxin biosynthesis and sclerotial development in
RT Aspergillus parasiticus.";
RL Mycopathologia 153:41-48(2002).
RN [8]
RP FUNCTION, INTERACTION WITH AFLS, AND MUTAGENESIS OF ARG-427; ARG-429 AND
RP ARG-431.
RX PubMed=12655397; DOI=10.1007/s00438-003-0809-3;
RA Chang P.K.;
RT "The Aspergillus parasiticus protein AFLJ interacts with the aflatoxin
RT pathway-specific regulator AFLR.";
RL Mol. Genet. Genomics 268:711-719(2003).
RN [9]
RP INDUCTION.
RX PubMed=15294809; DOI=10.1128/aem.70.8.4733-4739.2004;
RA Calvo A.M., Bok J., Brooks W., Keller N.P.;
RT "veA is required for toxin and sclerotial production in Aspergillus
RT parasiticus.";
RL Appl. Environ. Microbiol. 70:4733-4739(2004).
RN [10]
RP FUNCTION, AND INTERACTION WITH AFLS.
RX PubMed=15054098; DOI=10.1074/jbc.m400075200;
RA Roze L.V., Miller M.J., Rarick M., Mahanti N., Linz J.E.;
RT "A novel cAMP-response element, CRE1, modulates expression of nor-1 in
RT Aspergillus parasiticus.";
RL J. Biol. Chem. 279:27428-27439(2004).
RN [11]
RP FUNCTION.
RX PubMed=15746358; DOI=10.1128/aem.71.3.1539-1545.2005;
RA Miller M.J., Roze L.V., Trail F., Linz J.E.;
RT "Role of cis-acting sites NorL, a TATA box, and AflR1 in nor-1
RT transcriptional activation in Aspergillus parasiticus.";
RL Appl. Environ. Microbiol. 71:1539-1545(2005).
RN [12]
RP FUNCTION.
RX PubMed=23605486; DOI=10.1007/s12550-010-0062-7;
RA Schmidt-Heydt M., Ruefer C.E., Abdel-Hadi A., Magan N., Geisen R.;
RT "The production of aflatoxin B1 or G 1 by Aspergillus parasiticus at
RT various combinations of temperature and water activity is related to the
RT ratio of aflS to aflR expression.";
RL Mycotoxin Res. 26:241-246(2010).
RN [13]
RP INDUCTION.
RX PubMed=23113196;
RA Jahanshiri Z., Shams-Ghahfarokhi M., Allameh A., Razzaghi-Abyaneh M.;
RT "Effect of curcumin on Aspergillus parasiticus growth and expression of
RT major genes involved in the early and late stages of aflatoxin
RT biosynthesis.";
RL Iran. J. Public Health 41:72-79(2012).
RN [14]
RP FUNCTION, INTERACTION WITH AFLS, AND SUBCELLULAR LOCATION.
RX PubMed=23342682; DOI=10.3390/toxins4121582;
RA Ehrlich K.C., Mack B.M., Wei Q., Li P., Roze L.V., Dazzo F., Cary J.W.,
RA Bhatnagar D., Linz J.E.;
RT "Association with AflR in endosomes reveals new functions for AflJ in
RT aflatoxin biosynthesis.";
RL Toxins 4:1582-1600(2012).
RN [15]
RP INDUCTION.
RX PubMed=25741015; DOI=10.1099/mic.0.000070;
RA Verheecke C., Liboz T., Anson P., Diaz R., Mathieu F.;
RT "Reduction of aflatoxin production by Aspergillus flavus and Aspergillus
RT parasiticus in interaction with Streptomyces.";
RL Microbiology 161:967-972(2015).
CC -!- FUNCTION: Transcription factor involved in regulation of the aflatoxin
CC biosynthesis gene cluster (PubMed:8250554, PubMed:15006741,
CC PubMed:7793958, PubMed:11913765, PubMed:12655397, PubMed:15054098,
CC PubMed:23605486, PubMed:23342682). Binds with its co-regulator aflS to
CC AFLR1 elements (5'-TCGSWNNSCGR-3') present in the promoters of the
CC aflatoxin cluster genes (PubMed:10216264, PubMed:15746358). The ratio
CC of the expression data between aflS:aflR plays a crucial role in the
CC regulation of aflatoxins production (PubMed:23605486). A high ratio,
CC produced at a range between 17 and 30 degrees Celsius, corresponds with
CC the production profile of aflatoxin G1 biosynthesis (PubMed:23605486).
CC A low ratio, produced over 30 degrees Celsius, is related to aflatoxin
CC B1 biosynthesis (PubMed:23605486). {ECO:0000269|PubMed:10216264,
CC ECO:0000269|PubMed:11913765, ECO:0000269|PubMed:12655397,
CC ECO:0000269|PubMed:15006741, ECO:0000269|PubMed:15054098,
CC ECO:0000269|PubMed:15746358, ECO:0000269|PubMed:23342682,
CC ECO:0000269|PubMed:23605486, ECO:0000269|PubMed:7793958,
CC ECO:0000269|PubMed:8250554}.
CC -!- SUBUNIT: Interacts with its co-regulator aflS (PubMed:12655397,
CC PubMed:15054098, PubMed:23342682). {ECO:0000269|PubMed:12655397,
CC ECO:0000269|PubMed:15054098, ECO:0000269|PubMed:23342682}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23342682}. Endosome
CC {ECO:0000269|PubMed:23342682}.
CC -!- INDUCTION: Expression is positively regulated by the developmental and
CC secondary metabolism regulator veA (PubMed:15294809). Expression is
CC repressed during Streptomyces-Aspergillus interactions
CC (PubMed:25741015). Expression is also repressed by curcumin
CC (PubMed:23113196). {ECO:0000269|PubMed:15294809,
CC ECO:0000269|PubMed:23113196, ECO:0000269|PubMed:25741015}.
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DR EMBL; AY371490; AAS66018.1; -; Genomic_DNA.
DR EMBL; JZEE01000729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q6UEG8; -.
DR SMR; Q6UEG8; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:InterPro.
DR GO; GO:1900179; P:positive regulation of aflatoxin biosynthetic process; IDA:GO_Central.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR013700; AflR.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF08493; AflR; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Endosome; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..444
FT /note="Aflatoxin biosynthesis regulatory protein"
FT /id="PRO_0000438338"
FT DNA_BIND 29..56
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 427
FT /note="R->L: Abolishes interaction with aflS; when
FT associated with L-429 and L-431."
FT /evidence="ECO:0000269|PubMed:12655397"
FT MUTAGEN 429
FT /note="R->L: Abolishes interaction with aflS; when
FT associated with L-427 and L-431."
FT /evidence="ECO:0000269|PubMed:12655397"
FT MUTAGEN 431
FT /note="R->L: Abolishes interaction with aflS; when
FT associated with L-427 and L-429."
FT /evidence="ECO:0000269|PubMed:12655397"
SQ SEQUENCE 444 AA; 47258 MW; AF68C90B1CC0A006 CRC64;
MVDHISPRAS PGPIRSSQTR RARKLRDSCT SCASSKVRCT KEKPACARCI ERGLACQYMV
SKRMGRNPRA PSPLDSTRRP SESLPSAGSE QGLPAHNTYS TPHAHTQAHT HAHSHPQPHP
QSHPQSNQPP HALPTPNGSS SVSAIFSHQS PPPLVETQGL GGDLAGQAQS TLSSLTVDSE
FGGSLQSMEH GNHADFLAES TGSLFDAFLE VGTPMIDPFL ESAPLPPFQA RYCCFSLALQ
TLTCLFPHAP LGCQLRLTDG EDSSCNLMTT DMVISGNKKA TDAVRKILGC SCAQDGYLLS
MVVLIVLKVL GWYAAAAGTQ CTSTAAGGET NSGSCSNSPA TVSSGCLTEE RVLHHPSMVG
EDCVDEEDQP RVAAQLVLSE LHRVQSLANL LAKRLQEGGD DAAGIPAHHP ASPFSLLGFS
GLEANLRHRL RAVSSDIIDY LHRE
