PATM_ASPCL
ID PATM_ASPCL Reviewed; 1397 AA.
AC A1CFM0;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=ABC transporter patM {ECO:0000303|PubMed:19383676};
DE AltName: Full=Patulin synthesis protein M {ECO:0000303|PubMed:19383676};
GN Name=patM {ECO:0000303|PubMed:19383676}; ORFNames=ACLA_093680;
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: ABC transporter; 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 (Probable). May be involved in the secretion
CC of E-ascladiol to be converted to patulin by the secreted patulin
CC synthase patE (By similarity). {ECO:0000250|UniProtKB:B6RAL1,
CC ECO:0000305|PubMed:19383676}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:B6RAL1};
CC Multi-pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:B6RAL1}; Multi-pass membrane protein
CC {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 ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; DS027052; EAW11669.1; -; Genomic_DNA.
DR RefSeq; XP_001273095.1; XM_001273094.1.
DR AlphaFoldDB; A1CFM0; -.
DR SMR; A1CFM0; -.
DR PRIDE; A1CFM0; -.
DR EnsemblFungi; EAW11669; EAW11669; ACLA_093680.
DR GeneID; 4704857; -.
DR KEGG; act:ACLA_093680; -.
DR VEuPathDB; FungiDB:ACLA_093680; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR OMA; YFPVGYF; -.
DR OrthoDB; 324553at2759; -.
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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140723; P:patulin biosynthetic process; ISS:GO_Central.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT CHAIN 1..1397
FT /note="ABC transporter patM"
FT /id="PRO_0000437121"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1135..1155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1181..1201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1223..1243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1249..1269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1372..1392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 102..346
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 779..1016
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 811..818
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1397 AA; 156194 MW; 943FB6B976B61217 CRC64;
MDMLRNRPVK GSLDHDPQLS ADGTNTPAAS DGSDQRSDVI EKTAQLSEPI ADSIRRFFEI
RKLDGPDGTG VVFENISVEG SGTGAQAAPT ISSAARSAFG VLSPLQHRLA GQFSRPILSG
FSGTIDAGEM LLVIGKPGSG CTTFLKTLSY MWDEYKDVHG DLTIGGHPIQ ESMVKRPQDI
VFCAESDDHF PTLTVAETLR FAIRARCGPE ASATEVDMMV AQLAKLVGLS QVMNTKVGDA
YIRGVSGGER RRVSLAEALA TCARLICLDN PTHGLDSSTA LEFIETMREW TSQSRCVTAM
SVYQASDAIM PYFDKVLVIN SGRQVFYGRI GDAKAYFERL GFECLPTTTL SDFLNSMSAD
PEVRRVQDGK QHLVPRTSEE FEAVFHASTF YQDLQRSLET AKVEARTNPR PLVKARAFSL
PLHHQIWYCA YRQFRIVTSD YSLWAVEPAT IIVQSLVLGT LFRDQKRATQ SLFIFASALF
YSVLVPALQS MAEFGNGFAQ RPLILKQKRY RICRPIAYAL GLVTTDVVWK IAAICYNIPL
YFLTGFQRTA GNFFTWFCIV YLEHLALSMF FRSVAIFSPN MHRAVLPVGI FFNMYVLYTG
LYIPAPQMQV WLGWLRYLNP LYYAFESVMV NEFRDLSYQC SPSDLVPSGL GYTDMANQVC
AVLGSRSGEE SLSGMSYLEA QYGFGRSHLW RNVGINAAFF VFFALCSGIG MERLKTPAGR
LATVFYKGRP SIRNSQADSE SGAVHDDVPP DVSRQLSGDQ HHLNANSERD KNHTLAWTGL
CLDIETKDGT RRLLDNLNGW VKSGQLKALM GVSGAGKTTL LNTLAGRSSI GTLTGTLALN
GQLLPKFFRS RMGYVQQQDI HLPTQSVREA LQMTARLRRD ESIPLEEKNA YVEKVIEWLD
MEDIAEALVG VPGAGLNLEQ RKRVSIGVEM ASKPEILFLD EPTSGLDGQS AFSIVRLLRR
LADSGQAIVC TIHQPAAELV EQFDELYLLS RGGKLVYDGP LGTHCDKAIE YFEQHSRACG
QGENPAEYFL DAIGAGSRKE VQADWVGLWQ QSQQSKDRER AEKALVPAEG QAPLAPARRS
LYAVPFHVQL WVVVQRTWLY YWREPDYAMS KLWMSVGNAL LNSLTYLQSP NTQRGAYNRV
FSAFMSLIVG PPLGLQVQPR FVTLRDIFVH REREGFTYHW LAFVFAGIIV ELPYTFLTSL
VYWLLWYFPV GYFRTAPRAG YSFLMYELFA VFATSLAQMC ASLMPNIEAA FAANGFFFMF
CNTFAGTLSP KPVTPSGWRW YYKVSPLFYL GEGVTVDVLQ DLPLRCAESE VSIFQPPNGT
TCGQYAANFL QQATGFLLNT DSLSDCQYCR YRDGQSYYQQ YGYDFANRYP NIGIFIGFIA
FNFTMVLVMT YLTKIRR
