ASAE_ASPFN
ID ASAE_ASPFN Reviewed; 442 AA.
AC B8N0F1;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=MFS transporter asaE {ECO:0000303|PubMed:29674152};
DE AltName: Full=Aspergillic acid biosynthesis cluster protein E {ECO:0000303|PubMed:29674152};
GN Name=asaE {ECO:0000303|PubMed:29674152}; ORFNames=AFLA_023050;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP IDENTIFICATION WITHIN THE CLUSTER, AND INDUCTION.
RX PubMed=23834374; DOI=10.1111/mpp.12056;
RA Dolezal A.L., Obrian G.R., Nielsen D.M., Woloshuk C.P., Boston R.S.,
RA Payne G.A.;
RT "Localization, morphology and transcriptional profile of Aspergillus flavus
RT during seed colonization.";
RL Mol. Plant Pathol. 14:898-909(2013).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=29674152; DOI=10.1016/j.fgb.2018.04.009;
RA Lebar M.D., Cary J.W., Majumdar R., Carter-Wientjes C.H., Mack B.M.,
RA Wei Q., Uka V., De Saeger S., Diana Di Mavungu J.;
RT "Identification and functional analysis of the aspergillic acid gene
RT cluster in Aspergillus flavus.";
RL Fungal Genet. Biol. 116:14-23(2018).
CC -!- FUNCTION: MFS transporter; part of the gene cluster that mediates the
CC biosynthesis of aspergillic acid (PubMed:29674152). Probably involved
CC in aspergillic acid metabolism and transport (PubMed:29674152).
CC {ECO:0000269|PubMed:29674152}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:29674152}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:29674152};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expressed during the earliest stages of maize kernel
CC infection (PubMed:23834374). {ECO:0000269|PubMed:23834374}.
CC -!- DISRUPTION PHENOTYPE: Leads to the production of a mixture of
CC ferriaspergillin analogs with varying combinations of aspergillic acid
CC and hydroxyaspergillic acid (PubMed:29674152).
CC {ECO:0000269|PubMed:29674152}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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DR EMBL; EQ963473; EED55034.1; -; Genomic_DNA.
DR RefSeq; XP_002373816.1; XM_002373775.1.
DR AlphaFoldDB; B8N0F1; -.
DR SMR; B8N0F1; -.
DR EnsemblFungi; EED55034; EED55034; AFLA_023050.
DR VEuPathDB; FungiDB:AFLA_023050; -.
DR eggNOG; KOG2504; Eukaryota.
DR HOGENOM; CLU_001265_1_0_1; -.
DR OMA; GLMDFMF; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..442
FT /note="MFS transporter asaE"
FT /id="PRO_0000444460"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 47346 MW; B93C607F618BC0C1 CRC64;
MDRSRTSSQG RDVLPPRGDE GRISPSLDKE KSPGPEDQPD APPDGGLTAW LVVVGAWCTS
FCSFGWVNSV GIFQNYYESH LLKHLSSSTI SWIPSLQIFF MFAMGPIVGK LYDTFGARYL
IIGGTFFHVF GLMMASISTQ YYQLLLSQGI CSAIGAAAIF QPALSAVSAW FNRKRGIAFA
TLSTGSSVGG VIFPIMVDRL IAKVGFGWSM RISAFMILFL LGIAIVTVKA RRPPPQGPKP
SGVQLLQPFK EPVFIVTLLG YMLLTYGVFI PINYVIVQAV ASGMNADLAS YLVPMLNGAS
LFGRLGAGFM SDRYGRYNIF IVMCIVAGVL VLALWIPATS NAPIIVFATL FGFASGAYVS
LSPALIAQIS PLKEVGYRTG LLFLFASVGG LTTSPIAGAI LQNAGGDYTH MKIFSGVMLL
GGTAFIITAR IVGTGLKLVV KY
