PATC_ASPCL
ID PATC_ASPCL Reviewed; 549 AA.
AC A1CFL0;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Efflux pump patC {ECO:0000303|PubMed:19383676};
DE AltName: Full=Patulin synthesis protein C {ECO:0000303|PubMed:19383676};
GN Name=patC {ECO:0000303|PubMed:19383676}; ORFNames=ACLA_093580;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=15082620; DOI=10.1093/ije/dyh028;
RG Patulin Clinical Trials Committee, Medical Research Council;
RT "Clinical trial of patulin in the common cold. 1944.";
RL Int. J. Epidemiol. 33:243-246(2004).
RN [3]
RP FUNCTION.
RX PubMed=19383676; DOI=10.1099/mic.0.024836-0;
RA Artigot M.P., Loiseau N., Laffitte J., Mas-Reguieg L., Tadrist S.,
RA Oswald I.P., Puel O.;
RT "Molecular cloning and functional characterization of two CYP619 cytochrome
RT P450s involved in biosynthesis of patulin in Aspergillus clavatus.";
RL Microbiology 155:1738-1747(2009).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=22222931; DOI=10.1016/j.fct.2011.12.022;
RA de Melo F.T., de Oliveira I.M., Greggio S., Dacosta J.C., Guecheva T.N.,
RA Saffi J., Henriques J.A., Rosa R.M.;
RT "DNA damage in organs of mice treated acutely with patulin, a known
RT mycotoxin.";
RL Food Chem. Toxicol. 50:3548-3555(2012).
RN [5]
RP FUNCTION.
RX PubMed=24334092; DOI=10.1016/j.ijfoodmicro.2013.11.020;
RA Snini S.P., Tadrist S., Laffitte J., Jamin E.L., Oswald I.P., Puel O.;
RT "The gene PatG involved in the biosynthesis pathway of patulin, a food-
RT borne mycotoxin, encodes a 6-methylsalicylic acid decarboxylase.";
RL Int. J. Food Microbiol. 171:77-83(2014).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=26619846; DOI=10.1007/s13277-015-4474-z;
RA Boussabbeh M., Ben Salem I., Rjiba-Touati K., Bouyahya C., Neffati F.,
RA Najjar M.F., Bacha H., Abid-Essefi S.;
RT "The potential effect of patulin on mice bearing melanoma cells: an anti-
RT tumour or carcinogenic effect?";
RL Tumor Biol. 37:6285-6295(2016).
CC -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC biosynthesis of patulin, an acetate-derived tetraketide mycotoxin
CC produced by several fungal species that shows antimicrobial properties
CC against several bacteria (PubMed:19383676). May be involved in the
CC secretion of E-ascladiol to be converted to patulin by the secreted
CC patulin synthase patE (By similarity).
CC {ECO:0000250|UniProtKB:A0A075TRA9, ECO:0000269|PubMed:19383676}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane
CC {ECO:0000250|UniProtKB:A0A075TRA9}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:A0A075TRA9}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- BIOTECHNOLOGY: Patulin was originally used as an antibiotic and
CC specifically trialed to be used against the common cold, but it is no
CC longer used for that purpose since it has been shown to induce
CC immunological, neurological and gastrointestinal effects
CC (PubMed:15082620). Genotoxic effects of patulin with dose-dependent
CC increase in DNA strand breaks in brain, liver and kidneys have been
CC detected in mice (PubMed:22222931). However, more recently, it has been
CC proposed that patulin might also have anti-tumor properties
CC (PubMed:26619846). {ECO:0000269|PubMed:15082620,
CC ECO:0000269|PubMed:22222931, ECO:0000269|PubMed:26619846}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; DS027052; EAW11659.1; -; Genomic_DNA.
DR RefSeq; XP_001273085.1; XM_001273084.1.
DR AlphaFoldDB; A1CFL0; -.
DR SMR; A1CFL0; -.
DR EnsemblFungi; EAW11659; EAW11659; ACLA_093580.
DR GeneID; 4704865; -.
DR KEGG; act:ACLA_093580; -.
DR VEuPathDB; FungiDB:ACLA_093580; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_1_1; -.
DR OMA; DVYVMAI; -.
DR OrthoDB; 503593at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; ISS:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0140723; P:patulin biosynthetic process; ISS:GO_Central.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..549
FT /note="Efflux pump patC"
FT /id="PRO_0000437113"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
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 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 59113 MW; 41A31590A6868C6D CRC64;
MAESTAHTSP SLNDKEREVD QGILSDESGP AEEVKETPDQ ERSVQGVRWL LICIAVFSAN
LLYGLDNTIV ADIQGAVAGT FEEYAQLGWL GVGFTLGSVV FILPLGKAYA IFDTKWLFIG
CLTMFAAGSA LCGGAPNMDA IIVGRVWAGA GGAGMYLGNL NLITILTTPK EQPVYVGLVG
LIYGVGCILG PIIGGAFADS SATWRWGFYI NLIIFGIMAP IYVFLLPSLP RPAGEGRSFI
NRLRELDWVG TVLSAGMHVS FILFIVFGGV MWPWTDGRNI ALYVVAAVTL IAFALSQYFC
VLTDKENRLF PGEFLRNPTM IALYVLMACG GAALFVAVYY IPLYFQFVHG DSGIMSAVRL
LPFICFYVAT ILLCGWLMPK TGYYVLWYLL SGIFMVIGSA TMYTVKYDTK VANIYGYSIL
LGLGMATTQA AYAVGPSLVT PDRVAESIQF MNIGQGQSQL LGLAIASAIF QSETLSGLNA
LLAGKGYSQG DIQGAIAGAR STLLTELPAD LKTKALDVIV HSIDDVYVMA IAAGALYVIA
SCFLPWRRF
