PDR1_SCHPO
ID PDR1_SCHPO Reviewed; 1396 AA.
AC Q9C0Y5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ATP-binding cassette transporter pdr1;
DE Short=ABC transporter pdr1;
GN Name=pdr1; ORFNames=SPAPB24D3.09c;
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 [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).
RN [2]
RP IDENTIFICATION AS AN ABC TRANSPORTER, AND SUBCELLULAR LOCATION.
RX PubMed=16849797; DOI=10.1099/mic.0.28952-0;
RA Iwaki T., Giga-Hama Y., Takegawa K.;
RT "A survey of all 11 ABC transporters in fission yeast: two novel ABC
RT transporters are required for red pigment accumulation in a
RT Schizosaccharomyces pombe adenine biosynthetic mutant.";
RL Microbiology 152:2309-2321(2006).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16849797}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16849797}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAC36905.1; -; Genomic_DNA.
DR RefSeq; NP_593995.1; NM_001019421.2.
DR AlphaFoldDB; Q9C0Y5; -.
DR SMR; Q9C0Y5; -.
DR BioGRID; 279785; 12.
DR STRING; 4896.SPAPB24D3.09c.1; -.
DR iPTMnet; Q9C0Y5; -.
DR MaxQB; Q9C0Y5; -.
DR PaxDb; Q9C0Y5; -.
DR EnsemblFungi; SPAPB24D3.09c.1; SPAPB24D3.09c.1:pep; SPAPB24D3.09c.
DR GeneID; 2543363; -.
DR KEGG; spo:SPAPB24D3.09c; -.
DR PomBase; SPAPB24D3.09c; pdr1.
DR VEuPathDB; FungiDB:SPAPB24D3.09c; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q9C0Y5; -.
DR OMA; KHIPFLS; -.
DR PhylomeDB; Q9C0Y5; -.
DR PRO; PR:Q9C0Y5; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISM:PomBase.
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; 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; PF00005; ABC_tran; 2.
DR Pfam; PF06422; PDR_CDR; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Endoplasmic reticulum; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1396
FT /note="ATP-binding cassette transporter pdr1"
FT /id="PRO_0000362140"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1095..1115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1166..1186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1208..1228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1245..1265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1361..1381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 73..320
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 412..622
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 758..1001
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1071..1286
FT /note="ABC transmembrane type-2 2"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 794..801
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1396 AA; 159319 MW; B4CA19755056AD75 CRC64;
MSEQEKGKGD LDDPNSKNTK CPDKFEQKVE EYLEVLNELH LTGRTSGFCM RNFTVEGAFN
PKFQIRSFFA QLLHPINIIF RTGPKRDIIP LVKGFDGYLQ PGSSLLVLGH EGSGGSTLLK
ALCGIVEENE RLNGSLHYDG LDYKIAHSQF KADLSYCGEG HSKVATITVR RLLEFVCSCR
LPASKYDHPR SHYIRRICEI IRDAFDLGDF YNHRILRVFN SGDQIKVDVA QTMCARPLIQ
CWDNNMRDFD SISVIDILSR IKVLSHKLGT TLVAIVSQAS DRIFHMFDMV TLMYEGEQIF
YGPTSRLKPY FLDLGFIPAK HSTTVEFVTS LTYPEMRIIN KKHQGFIPST PAEFRECWLR
SEDYAKLIKF MDRYEENHSD IHAFKDAKFD QTRLQKFLRW LNSNPCLIPY RLQVFATAKV
TFFQYLHDYS YIATFVFTYV FQALMLGSLF YNLRNESSEL YSRGSVLSNA IVFTAIQTMS
EVDIIFLKKS LFKEHRVQSL YHPSAALMGS SLVEFPMRIV VVTMYDIIVY FLSDLKRNAR
SFFIFYLFTI VITFCMSAVF RFIALLSTTA EIAALIGGIG ALVLIIFCGA VMPVQYIGWW
FRWIAYANPV NYGYESIMLN EFDGREIPCS LMAPAPDTAP IENNFCLATA GRTGTSIVSG
YQYLQVVYQY KADFLWRNCG IILGFAIFIL ASSLILANFI RYDRESVHIP EFQKRKSYSQ
VASSFLIEPQ DKPPSQTEPD NKKVDVSTTL STNDNLVLCW RDLNFTVVTK TSKKQILTNV
SGYLKKNTLT ALLGENKSGK SVLLRILSQR GIAGSVEGEI TLSGLKNPKN LRKRIGYVRK
NPLFISEYTV RETLRLHAAL RQSKQRSLSE QYAYVEYVID FLGLGEVADF IVGDMGKGLS
LYHKRLLSIA VELSARPGSI LLLDEPANGL DSQSAWMLVC ILQKLARSGL SILCSVSQPS
SRILELFDMM LILDLNGNTV YYDTMGRDLS KLVNYFKRIH GTNEHSKDTA DFVLHCIQFL
KQGPEFDYAG AWASTNTHKQ IIEHVNFIMD NPELTDDDFP NETRFMTSFF FQIYKISMRN
FVAYWRDSSL LRARVAFNIV AGLIIGFSFY KQGVGVEETQ NKMFSAYMLT VASTSTMNGL
QPKFIYFRSI YEQYEQNTAI YSRTAFIIAF FLVEAVINCC FATLFFFGWY YPSGFYEFNH
NIPFYGGFAW LMLMIFTLYY TTLGIGIATI SPSIGTASII SGTAFVFIQY FNGMIQLPGV
IVGFWKWMDA LSPYKYFLEG MIGGVLHDAP ITCEKFEIHY VDPPPNYSCG EYFSSFLNSS
GHGIVYNPEA YSSCQYCPYK NADELMVGFG YHYNHKWRNF CIMIGYTAFN LGAAIALYYI
IHKTPWKRLA ARFVPD
