PMD1_SCHPO
ID PMD1_SCHPO Reviewed; 1362 AA.
AC P36619; O74513;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Leptomycin B resistance protein pmd1;
GN Name=pmd1; ORFNames=SPCC663.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1349418; DOI=10.1111/j.1365-2958.1992.tb01526.x;
RA Nishi K., Yoshida M., Nishimura M., Nishikawa M., Nishiyama M.,
RA Horinouchi S., Beppu T.;
RT "A leptomycin B resistance gene of Schizosaccharomyces pombe encodes a
RT protein similar to the mammalian P-glycoproteins.";
RL Mol. Microbiol. 6:761-769(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: May be a transmembrane transporter of the mating factor,
CC namely P-factor or M-factor. Confers resistance to leptomycin B and to
CC several other antifungal drugs.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; D10695; BAA01537.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20363.1; -; Genomic_DNA.
DR PIR; T41534; T41534.
DR RefSeq; NP_588265.1; NM_001023255.2.
DR AlphaFoldDB; P36619; -.
DR SMR; P36619; -.
DR BioGRID; 275293; 8.
DR STRING; 4896.SPCC663.03.1; -.
DR TCDB; 3.A.1.201.18; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P36619; -.
DR MaxQB; P36619; -.
DR PaxDb; P36619; -.
DR PRIDE; P36619; -.
DR EnsemblFungi; SPCC663.03.1; SPCC663.03.1:pep; SPCC663.03.
DR PomBase; SPCC663.03; pmd1.
DR VEuPathDB; FungiDB:SPCC663.03; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; P36619; -.
DR OMA; LFMLPMT; -.
DR PhylomeDB; P36619; -.
DR Reactome; R-SPO-1369007; Mitochondrial ABC transporters.
DR Reactome; R-SPO-159418; Recycling of bile acids and salts.
DR Reactome; R-SPO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-9754706; Atorvastatin ADME.
DR PRO; PR:P36619; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IMP:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:PomBase.
DR Gene3D; 1.20.1560.10; -; 3.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 2.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1362
FT /note="Leptomycin B resistance protein pmd1"
FT /id="PRO_0000093452"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..115
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 138..162
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 220..237
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 320..346
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 375..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 789..809
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 835..859
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 916..935
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 940..957
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1022..1040
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1054..1072
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1073..1362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 95..385
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 420..665
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 795..1083
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1119..1356
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 748..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 455..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1154..1161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 1334..1335
FT /note="IA -> TC (in Ref. 1; BAA01537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1362 AA; 149632 MW; 2ADF8A8E7B3ACEE8 CRC64;
MSLHSKKSTS TVKDNEHSLD LSIKSIPSNE KNFSTEKSEN EASESHVVDV VKDPFEQYTP
EEQEILYKQI NDTPAKLSGY PRILSYADKW DIMLQLAGTI TGIGAGLGMP LMSLVSGQLA
QAFTDLASGK GASSFQHTVD HFCLYFIYIA IGVFGCSYIY TVTFIIAGER IARRIRQDYL
HAILSQNIGY FDRLGAGEIT TRITTDTNFI QDGLGEKVGL VFFAIATFVS GFVIAFIRHW
KFTLILSSMF PAICGGIGLG VPFITKNTKG QIAVVAESST FVEEVFSNIR NAFAFGTQDI
LAKLYNKYLI TAQRFGINKA IAMGLMVGWM FFVAYGVYGL AFWEGGRLLH AGDLDVSKLI
GCFFAVLIAS YSLANISPKM QSFVSCASAA KKIFDTIDRV SPINAFTPTG DVVKDIKGEI
ELKNIRFVYP TRPEVLVLDN FSLVCPSGKI TALVGASGSG KSTIIGLVER FYDPIGGQVF
LDGKDLRTLN VASLRNQISL VQQEPVLFAT TVFENITYGL PDTIKGTLSK EELERRVYDA
AKLANAYDFI MTLPEQFSTN VGQRGFLMSG GQKQRIAIAR AVISDPKILL LDEATSALDS
KSEVLVQKAL DNASRSRTTI VIAHRLSTIR NADNIVVVNA GKIVEQGSHN ELLDLNGAYA
RLVEAQKLSG GEKDQEMVEE ELEDAPREIP ITSFGDDDED NDMASLEAPM MSHNTDTDTL
NNKLNEKDNV VFEDKTLQHV ASEIVPNLPP ADVGELNEEP KKSKKSKKNN HEINSLTALW
FIHSFVRTMI EIICLLIGIL ASMICGAAYP VQAAVFARFL NIFTDLSSTD FLHKVNVFAV
YWLILAIVQF FAYAISNFAM TYAMEAVLQR IRYHLFRTLL RQDVEFFDRS ENTVGAITTS
LSTKIQSLEG LSGPTLGTFF QILTNIISVT ILSLATGWKL GLVTLSTSPV IITAGYYRVR
ALDQVQEKLS AAYKESAAFA CESTSAIRTV ASLNREENVF AEYCDSLIKP GRESAIASLK
SGLFFSAAQG VTFLINALTF WYGSTLMRKG EYNIVQFYTC FIAIVFGIQQ AGQFFGYSAD
VTKAKAAAGE IKYLSESKPK IDTWSTEGKK VESLQSAAIE FRQVEFSYPT RRHIKVLRGL
NLTVKPGQFV AFVGSSGCGK STTIGLIERF YDCDNGAVLV DGVNVRDYNI NDYRKQIALV
SQEPTLYQGT VRENIVLGAS KDVSEEEMIE ACKKANIHEF ILGLPNGYNT LCGQKGSSLS
GGQKQRIAIA RALIRNPKIL LLDEATSALD SHSEKVVQEA LNAASQGRTT VAIAHRLSSI
QDADCIFVFD GGVIAEAGTH AELVKQRGRY YELVVEQGLN KA
