AB18B_ARATH
ID AB18B_ARATH Reviewed; 1225 AA.
AC Q9LSJ5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ABC transporter B family member 18;
DE Short=ABC transporter ABCB.18;
DE Short=AtABCB18;
DE AltName: Full=P-glycoprotein 18;
DE AltName: Full=Putative multidrug resistance protein 20;
GN Name=ABCB18; Synonyms=MDR20, PGP18; OrderedLocusNames=At3g28390;
GN ORFNames=MFJ20.7;
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=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 [2]
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 [3]
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 [4]
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; AB026644; BAB02855.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77440.1; -; Genomic_DNA.
DR RefSeq; NP_189480.1; NM_113759.1.
DR AlphaFoldDB; Q9LSJ5; -.
DR SMR; Q9LSJ5; -.
DR BioGRID; 7797; 1.
DR STRING; 3702.AT3G28390.1; -.
DR PaxDb; Q9LSJ5; -.
DR PRIDE; Q9LSJ5; -.
DR EnsemblPlants; AT3G28390.1; AT3G28390.1; AT3G28390.
DR GeneID; 822468; -.
DR Gramene; AT3G28390.1; AT3G28390.1; AT3G28390.
DR KEGG; ath:AT3G28390; -.
DR Araport; AT3G28390; -.
DR TAIR; locus:2088942; AT3G28390.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q9LSJ5; -.
DR OMA; FIIACSY; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q9LSJ5; -.
DR BioCyc; ARA:AT3G28390-MON; -.
DR PRO; PR:Q9LSJ5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSJ5; differential.
DR Genevisible; Q9LSJ5; 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..1225
FT /note="ABC transporter B family member 18"
FT /id="PRO_0000227931"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 780..800
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 23..312
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 347..583
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 657..945
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 980..1218
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 382..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1015..1022
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1225 AA; 134303 MW; DCB4E5D590F4D782 CRC64;
MMKSFGSIRS IFMHADGVDW MLMALGLIGA VGDGFITPII FFICSKLLNN VGGSSFDDET
FMQTVAKNAV ALVYVACASW VICFIEGYCW TRTGERQAAK MREKYLKAVL RQDVGYFDLH
VTSTSDVITS VSSDSLVIQD FLSEKLPNFL MNTSAFVASY IVGFLLLWRL TIVGFPFIIL
LLIPGLMYGR ALIRISMKIR EEYNEAGSIA EQVISSVRTV YAFGSEKKMI EKFSTALQGS
VKLGLRQGLA KGIAIGSNGI TYAIWGFLTW YGSRMVMNHG SKGGTVSSVI VCVTFGGTSL
GQSLSNLKYF SEAFVVGERI MKVINRVPGI DSDNLEGQIL EKTRGEVEFN HVKFTYPSRP
ETPIFDDLCL RVPSGKTVAL VGGSGSGKST VISLLQRFYD PIAGEILIDG LPINKLQVKW
LRSQMGLVSQ EPVLFATSIK ENILFGKEDA SMDEVVEAAK ASNAHSFISQ FPNSYQTQVG
ERGVQLSGGQ KQRIAIARAI IKSPIILLLD EATSALDSES ERVVQEALDN ASIGRTTIVI
AHRLSTIRNA DVICVVHNGR IIETGSHEEL LEKLDGQYTS LVRLQQVDNK ESDHISVEEG
QASSLSKDLK YSPKEFIHST SSNIVRDFPN LSPKDGKSLV PSFKRLMSMN RPEWKHALYG
CLGAALFGAV QPIYSYSSGS MVSVYFLASH DQIKEKTRIY VLLFVGLALF TFLSNISQHY
GFAYMGEYLT KRIRERMLGK ILTFEVNWFD KDENSSGAIC SRLAKDANMV RSLVGDRMSL
LVQTISAVSI TCAIGLVISW RFSIVMMSVQ PVIVVCFYTQ RVLLKSMSRN AIKGQDESSK
LAAEAVSNIR TITAFSSQER IINLLKMVQE GPRKDSARQS WLAGIMLGTS QSLITCVSAL
NFWYGGKLIA DGKMMSKEFL EIFLIFASTG RVIAEAGTMT KDLVKGSDAV ASVFAVLDRN
TTIEPENPDG YVPKKVKGQI SFSNVDFAYP TRPDVIIFQN FSIDIEDGKS TAIVGPSGSG
KSTIISLIER FYDPLKGIVK IDGRDIRSCH LRSLRQHIAL VSQEPTLFAG TIRENIMYGG
ASNKIDESEI IEAAKAANAH DFITSLSNGY DTCCGDRGVQ LSGGQKQRIA IARAVLKNPS
VLLLDEATSA LDSQSESVVQ DALERLMVGR TSVVIAHRLS TIQKCDTIAV LENGAVVECG
NHSSLLAKGP KGAYFSLVSL QRTLF