ID   ATAA_ASPTN              Reviewed;         449 AA.
AC   Q0CS59;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=MFS acetylaranotin efflux transporter ataA {ECO:0000303|PubMed:23586797};
DE   AltName: Full=Acetylaranotin biosynthesis cluster protein A {ECO:0000303|PubMed:23586797};
GN   Name=ataA {ECO:0000303|PubMed:23586797}; ORFNames=ATEG_03475;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23586797; DOI=10.1021/ja3123653;
RA   Guo C.J., Yeh H.H., Chiang Y.M., Sanchez J.F., Chang S.L., Bruno K.S.,
RA   Wang C.C.;
RT   "Biosynthetic pathway for the epipolythiodioxopiperazine acetylaranotin in
RT   Aspergillus terreus revealed by genome-based deletion analysis.";
RL   J. Am. Chem. Soc. 135:7205-7213(2013).
CC   -!- FUNCTION: Efflux pump that may provide the dual role of acetylaranotin
CC       export and self-protection by allowing the fungus to evade the harmful
CC       effect of its own acetylaranotin production (PubMed:23586797).
CC       {ECO:0000305|PubMed:23586797}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Reduces strongly the production of acetylaranotin
CC       (PubMed:23586797). {ECO:0000269|PubMed:23586797}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH476597; EAU36749.1; -; Genomic_DNA.
DR   RefSeq; XP_001212653.1; XM_001212653.1.
DR   AlphaFoldDB; Q0CS59; -.
DR   STRING; 341663.Q0CS59; -.
DR   EnsemblFungi; EAU36749; EAU36749; ATEG_03475.
DR   GeneID; 4317583; -.
DR   VEuPathDB; FungiDB:ATEG_03475; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_000960_22_1_1; -.
DR   OMA; SITADMA; -.
DR   OrthoDB; 627633at2759; -.
DR   Proteomes; UP000007963; 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   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..449
FT                   /note="MFS acetylaranotin efflux transporter ataA"
FT                   /id="PRO_0000440662"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   449 AA;  48068 MW;  5E8BCC216D84E56A CRC64;
     MRRVTSVYVW LTVVVKDNTI IATAIPRITD QFKALEDVGW YGSSYLLVTC MFQLIFGKLY
     GYFPIKWVFL AAIIIFEIGS AVCGAAPTSD AFILEMVVST YLPEPFDHVL SAGSFYINLP
     IGAVVIVVLL QFLHVPNTVP VEASSKTLFQ HMDPLGVVTF LPAIVCLLLA LQWGGTTFPW
     ANGRIIALFV LAGVLLIAFL AIQRKRQDNA MVPPRIITMH PVAFSSLFMT LFAGAYFTII
     YYLPIWFQAI KNASAVNSGI MCLPLMLSMV IFSFVAGGGV TATGNPVPFF YIATVLAAAG
     AGLMTTFEVH TGHPKWIGYQ VLLGSGVGMG IQLPIIAVQA VLPAADIPVG TAILTFCQTF
     GGAIFVSVAQ AVFANRLQTG LLRAVPGVSP GLVQEVGATN LDTVIDAQHM GAVKVVYNDA
     LVSAWYLAVA LFSVAVLGAV GMSTKRKSA