AB15B_ARATH
ID AB15B_ARATH Reviewed; 1240 AA.
AC Q9LHD1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ABC transporter B family member 15;
DE Short=ABC transporter ABCB.15;
DE Short=AtABCB15;
DE AltName: Full=Multidrug resistance protein 13;
DE AltName: Full=P-glycoprotein 15;
GN Name=ABCB15; Synonyms=MDR13, PGP15; OrderedLocusNames=At3g28345;
GN ORFNames=MZF16.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
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; AP002051; BAB02627.1; -; Genomic_DNA.
DR EMBL; AB026644; BAB02627.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE77436.1; -; Genomic_DNA.
DR RefSeq; NP_189475.1; NM_113754.3.
DR AlphaFoldDB; Q9LHD1; -.
DR SMR; Q9LHD1; -.
DR BioGRID; 7792; 2.
DR STRING; 3702.AT3G28345.1; -.
DR TCDB; 3.A.1.201.34; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q9LHD1; -.
DR PaxDb; Q9LHD1; -.
DR PRIDE; Q9LHD1; -.
DR ProteomicsDB; 244578; -.
DR EnsemblPlants; AT3G28345.1; AT3G28345.1; AT3G28345.
DR GeneID; 822463; -.
DR Gramene; AT3G28345.1; AT3G28345.1; AT3G28345.
DR KEGG; ath:AT3G28345; -.
DR Araport; AT3G28345; -.
DR TAIR; locus:2088897; AT3G28345.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q9LHD1; -.
DR OMA; CMALCFW; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q9LHD1; -.
DR BioCyc; ARA:AT3G28345-MON; -.
DR PRO; PR:Q9LHD1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHD1; baseline and differential.
DR Genevisible; Q9LHD1; AT.
DR GO; GO:0016021; C:integral component of membrane; IBA: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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
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; 1.
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 ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1240
FT /note="ABC transporter B family member 15"
FT /id="PRO_0000227924"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 681..701
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 794..813
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 817..839
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 35..324
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 359..595
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 672..960
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 995..1233
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 617..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394..401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1030..1037
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1240 AA; 135641 MW; F00F17EBD4709173 CRC64;
MGKEEEKESG RNKMNCFGSV RSIFMHADGV DWLLMGLGLI GAVGDGFTTP LVLLITSKLM
NNIGGSSFNT DTFMQSISKN SVALLYVACG SWVVCFLEGY CWTRTGERQT ARMREKYLRA
VLRQDVGYFD LHVTSTSDVI TSVSSDSFVI QDVLSEKLPN FLMSASTFVG SYIVGFILLW
RLAIVGLPFI VLLVIPGLMY GRALISISRK IREEYNEAGF VAEQAISSVR TVYAFSGERK
TISKFSTALQ GSVKLGIKQG LAKGITIGSN GITFAMWGFM SWYGSRMVMY HGAQGGTVFA
VAAAIAIGGV SLGGGLSNLK YFFEAASVGE RIMEVINRVP KIDSDNPDGH KLEKIRGEVE
FKNVKFVYPS RLETSIFDDF CLRVPSGKTV ALVGGSGSGK STVISLLQRF YDPLAGEILI
DGVSIDKLQV KWLRSQMGLV SQEPALFATT IKENILFGKE DASMDDVVEA AKASNAHNFI
SQLPNGYETQ VGERGVQMSG GQKQRIAIAR AIIKSPTILL LDEATSALDS ESERVVQEAL
ENASIGRTTI LIAHRLSTIR NADVISVVKN GHIVETGSHD ELMENIDGQY STLVHLQQIE
KQDINVSVKI GPISDPSKDI RNSSRVSTLS RSSSANSVTG PSTIKNLSED NKPQLPSFKR
LLAMNLPEWK QALYGCISAT LFGAIQPAYA YSLGSMVSVY FLTSHDEIKE KTRIYALSFV
GLAVLSFLIN ISQHYNFAYM GEYLTKRIRE RMLSKVLTFE VGWFDRDENS SGAICSRLAK
DANVVRSLVG DRMALVVQTV SAVTIAFTMG LVIAWRLALV MIAVQPVIIV CFYTRRVLLK
SMSKKAIKAQ DESSKLAAEA VSNVRTITAF SSQERIMKML EKAQESPRRE SIRQSWFAGF
GLAMSQSLTS CTWALDFWYG GRLIQDGYIT AKALFETFMI LVSTGRVIAD AGSMTTDLAK
GSDAVGSVFA VLDRYTSIDP EDPDGYETER ITGQVEFLDV DFSYPTRPDV IIFKNFSIKI
EEGKSTAIVG PSGSGKSTII GLIERFYDPL KGIVKIDGRD IRSYHLRSLR RHIALVSQEP
TLFAGTIREN IIYGGVSDKI DEAEIIEAAK AANAHDFITS LTEGYDTYCG DRGVQLSGGQ
KQRIAIARAV LKNPSVLLLD EATSALDSQS ERVVQDALER VMVGRTSVVI AHRLSTIQNC
DAIAVLDKGK LVERGTHSSL LSKGPTGIYF SLVSLQTTSG
