SAT21_STACB
ID SAT21_STACB Reviewed; 474 AA.
AC A0A084AFH0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=MFS transporter SAT21 {ECO:0000303|PubMed:25015739};
DE AltName: Full=Satratoxin biosynthesis SC3 cluster protein 216 {ECO:0000303|PubMed:25015739};
GN Name=SAT21 {ECO:0000303|PubMed:25015739}; ORFNames=S7711_07411;
OS Stachybotrys chartarum (strain CBS 109288 / IBT 7711) (Toxic black mold)
OS (Stilbospora chartarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1280523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP FUNCTION.
RC STRAIN=CBS 109288 / IBT 7711;
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- FUNCTION: MFS transporter; part of the satratoxin SC3 cluster involved
CC in the biosynthesis of satratoxins, trichothecene mycotoxins that are
CC associated with human food poisonings (PubMed:25015739). Satratoxins
CC are suggested to be made by products of multiple gene clusters (SC1,
CC SC2 and SC3) that encode 21 proteins in all, including polyketide
CC synthases, acetyltransferases, and other enzymes expected to modify the
CC trichothecene skeleton (PubMed:25015739). SC1 encodes 10 proteins, SAT1
CC to SAT10 (PubMed:25015739). The largest are SAT8, which encodes a
CC putative polyketide synthase (PKS) with a conventional non-reducing
CC architecture, and SAT10, a putative protein containing four ankyrin
CC repeats and thus may be involved in protein scaffolding
CC (PubMed:25015739). The putative short-chain reductase SAT3 may assist
CC the PKS in some capacity (PubMed:25015739). SAT6 contains a secretory
CC lipase domain and acts probably as a trichothecene esterase
CC (PubMed:25015739). SAT5 encodes a putative acetyltransferase, and so,
CC with SAT6, may affect endogenous protection from toxicity
CC (PubMed:25015739). The probable transcription factor SAT9 may regulate
CC the expression of the SC1 cluster (PubMed:25015739). SC2 encodes
CC proteins SAT11 to SAT16, the largest of which encodes the putative
CC reducing PKS SAT13 (PubMed:25015739). SAT11 is a cytochrome P450
CC monooxygenase, while SAT14 and SAT16 are probable acetyltransferases
CC (PubMed:25015739). The SC2 cluster may be regulated by the
CC transcription factor SAT15 (PubMed:25015739). SC3 is a small cluster
CC that encodes 5 proteins, SAT17 to SAT21 (PubMed:25015739). SAT21 is a
CC putative MFS-type transporter which may have a role in exporting
CC secondary metabolites (PubMed:25015739). The four other proteins
CC putatively encoded in SC3 include the taurine hydroxylase-like protein
CC SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and
CC the Cys6-type zinc finger SAT20, the latter being probably involved in
CC regulation of SC3 expression (PubMed:25015739).
CC {ECO:0000305|PubMed:25015739}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; KL648755; KEY64049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084AFH0; -.
DR SMR; A0A084AFH0; -.
DR EnsemblFungi; KEY64049; KEY64049; S7711_07411.
DR HOGENOM; CLU_013756_2_1_1; -.
DR OrthoDB; 1458702at2759; -.
DR Proteomes; UP000028045; 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; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..474
FT /note="MFS transporter SAT21"
FT /id="PRO_0000442418"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 220..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 474 AA; 51045 MW; C57E85FE487CD40B CRC64;
MLRNTHLVLP FILYLLFRLS HFLLEVPTVR MIELAACHQH LRLDHGPLNE AACKTPPVQE
HVSLVVGWKM TFDSIPGLMS ILYFGTLADK SGHRAILRLC CVGYLLAILW VLITCLFHQV
FPVELVLLSS LFLFIGGGQL VFAAVITAFV ADLFPPPSRT KFLFLLAAMP HMDKVASPAL
ATKLMEQNLF LPSLVSMAIV VICVALLQMS DVGRETAASK VVGSTSDQTE PFLRSSSNSS
QESGTAAPAI DPEQARGPFR QLKNIICWVH REPVLFICYL CFFLKSNAMA SEAFIFQYLS
EKFGWPLRET TVMRLALSSG AVISTLIICP LANATLHNRG VASARINIGA VHASSIVLVA
SFIMAWQASS STAFIFSMLA AGFGEGLEPA LQGVLAAASQ TKAKGSIFAL MCTCSLLGDM
TGGPLMSALM SIGRGGNGVS DGYCFLASAL VFGAVIVLAH LLWALGAEEM LGED
