ID   DHC2_ALTCI              Reviewed;         581 AA.
AC   A0A0N7D7C9;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Dehydrocurvularin exporter {ECO:0000303|PubMed:26493380};
DE   AltName: Full=Dehydrocurvularin biosynthesis protein 2 {ECO:0000303|PubMed:26493380};
GN   Name=Dhc2 {ECO:0000303|PubMed:26493380};
OS   Alternaria cinerariae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Sonchi.
OX   NCBI_TaxID=216837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=ATCC 11784;
RX   PubMed=26493380; DOI=10.1002/cbic.201500428;
RA   Cochrane R.V., Gao Z., Lambkin G.R., Xu W., Winter J.M., Marcus S.L.,
RA   Tang Y., Vederas J.C.;
RT   "Comparison of 10,11-dehydrocurvularin polyketide synthases from Alternaria
RT   cinerariae and Aspergillus terreus highlights key structural motifs.";
RL   ChemBioChem 16:2479-2483(2015).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 11784;
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Efflux pump that is probably involved in the export of
CC       dehydrocurvularin (PubMed:26493380). {ECO:0000269|PubMed:26493380}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26493380};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KT271471; AKQ49200.1; -; mRNA.
DR   AlphaFoldDB; A0A0N7D7C9; -.
DR   SMR; A0A0N7D7C9; -.
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; -; 1.
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; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..581
FT                   /note="Dehydrocurvularin exporter"
FT                   /id="PRO_0000438395"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        527..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   581 AA;  62369 MW;  72F3D4DBBE500788 CRC64;
     MTDSPSLESN NKSDMDTPRP PASSHDEHDA AESVSEKQDS ATTSPTGKLE PEYLTGLRLG
     LVMFTIFVST ILVSLEIGII ATAIPGITND FRKLDDVGWY GSATFILAAA ASPLWGKLYK
     YLNVKWVYLS AVGIFLVGSI VAAAAPNSVA VIVGRALQGW GASGVLGGTL IVINYVAPPR
     NHPLLIGTWM AVFMMSTILG PVIGGAFTSG VSWRWCFWIN LPVGGPIVVL LLLFLRVPKH
     VKPVPATWKE IILNLDIPGF CLLLVSLVCL TLALQWGGQT KTWDDGSVIA TLVLWILLTI
     GFFIVEWLQG ARAMAPLSIL KQRMTWSNVI FCLVSYAALY QVMFYLPIYF QSIHGQSAVT
     SGVNTLPFLA FFALGAMVSG GAIGKTRYTQ PYELAGALIM TAGMALIYIL DVDSPKAKYI
     GAEVLFGFGI GLCNQVPMTA VQGFSKPDEV ASATGIMVMC QTLSGAYFVA IAQSLFANRM
     LHALNSGSDH LDVALVLGTG ASELQDVFSG DDLTAVIDAY MVGIKDVFAF SLACAAFSVI
     LTALIPFKRL PDHEKKPSKD AMASDEVKAS EEVQQEKKVT V