ID A0A074XZX3_AURPU Unreviewed; 1290 AA.
AC A0A074XZX3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Multidrug efflux transporter AcrB transmembrane domain-containing protein {ECO:0000313|EMBL:KEQ89194.1};
GN ORFNames=M438DRAFT_350636 {ECO:0000313|EMBL:KEQ89194.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ89194.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ89194.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ89194.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the patched family.
CC {ECO:0000256|ARBA:ARBA00005585}.
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DR EMBL; KL584974; KEQ89194.1; -; Genomic_DNA.
DR STRING; 1043002.A0A074XZX3; -.
DR HOGENOM; CLU_002359_0_1_1; -.
DR OrthoDB; 2786103at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015918; P:sterol transport; IEA:UniProt.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR InterPro; IPR032190; NPC1_N.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR PANTHER; PTHR45727; NPC INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1.
DR PANTHER; PTHR45727:SF2; NPC INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1.
DR Pfam; PF16414; NPC1_N; 1.
DR Pfam; PF02460; Patched; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR PROSITE; PS50156; SSD; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:KEQ89194.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1290
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001703887"
FT TRANSMEM 284..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 614..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 651..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 681..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 758..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1088..1111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1117..1140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1147..1169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1189..1218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1230..1253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 609..783
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1290 AA; 140349 MW; 4B13F6F1D25AD883 CRC64;
MRITRSWLAV AGLSLLSASA EKHQTAFGLS VDATADASAP DGFTHKHEAG RCAIRGHCGK
QGFFGSELPC PDNGLAEEPS ADTRKTLMSI CGDKWAEGPV CCTDEQLGAL SSNLKRAESI
IGACPACKDN FFNLFCTFTC SPDQSLFVNV TNIAPKGDKL LVTELDQLIS EDYGSAFYSS
CKDVKFGATG GKAMDLIGGG AKNYTQFLKF LGDKKPFGSP FQINFPVPNE ADFPGMEPGS
DKAHPCNSTD ERYRCACVDC AASCPELPSV KEAHECKVGV LPCLSFAVII VYSVFLFLLI
LAVSGHVAYA KHTKSRNERL RLLQDASPSD DEDEGDIVHQ AGLLEKPTRS YPLNTVCDRI
FSRLGRTAAT FPAITISSSV IIVALLSLGW MRFTVETDPV KLWVSPDSEA AKEKAFFDKS
FGPFFRAEQA FLVNDTLPTG PGPVLSYDTL NWWFDVENRI RRMKSIDGGY TLDDVCYKPT
GDACVVQSLT GYFGGDFQGI DPDLWQEDLE ACADTPVNCL PDFQQPLNPR YLFGGYNNSV
IDSTAVVVTW AVTNHAEDTF ELERAMDWEE SLKGLLLTVQ DEASERGLRL SFNTEISLEQ
ELNKSTNTDA KIVAVSYLIM FLYASIALGA TTLTVRDVLR NPANALVQSK FMLGVVGILI
VLMSVSASVG LFAAAGVKAT LIIAEVIPFL VLAVGVDNIF LIVHEFERVN ISHADEPVSE
RIAKALGRMG PSILLSATTE TVAFALGAAV GMPAVRNFAA YAAGAVFINA ILQVTMFISV
LALNQKRVEA GRADCFPFIK VKGADSNSMA IAGMPGLAGI EEEGALQRFI RKTYAPALLG
KKTKTAVITI FLGFFTIGLA LLPGVELGLD QRIAIPSDSY LIKYFDDLYD YFEAGPPVYF
VTKDLNATAR VHQQEICGRF STCEEFSLAN ILEQERKRPE ISYIADATAS WIDDFFFWLN
PSLEECCVDG SHTCFENRNP PWNVTLHGMP EGQEFVSYLQ RWLESPTTSE CPLAGKAAYG
DALVVDNSSL SIPASHFRTS HTPMHSQSDF IAAYKSARRI AKDITSHTGV EVFPYSKFYI
FFDQYVSIVR LSGALIGGAL GFILVLSSVL LGSLATGLVV TVTVGMTVVD IIGTISLAGV
SLNAVSLVNL IICVGISVEF CAHIARAFSV PSPSLLERCH SFRGKDARAW AALVNVGASV
FSGITVTKLL GVFVLAFTRS KIFEIYYFRV WLALVIWAAL HALVFLPVAL SFFGGVGYAD
PDVDGGLEQD LASRRYRAMM PDEEYYSDEY
//
