AB17B_ARATH
ID AB17B_ARATH Reviewed; 1240 AA.
AC Q9LSJ6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ABC transporter B family member 17;
DE Short=ABC transporter ABCB.17;
DE Short=AtABCB17;
DE AltName: Full=P-glycoprotein 17;
DE AltName: Full=Putative multidrug resistance protein 19;
GN Name=ABCB17; Synonyms=MDR19, PGP17; OrderedLocusNames=At3g28380;
GN ORFNames=MFJ20.6;
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; BAB02854.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77439.1; -; Genomic_DNA.
DR RefSeq; NP_189479.1; NM_113758.2.
DR AlphaFoldDB; Q9LSJ6; -.
DR SMR; Q9LSJ6; -.
DR BioGRID; 7796; 1.
DR STRING; 3702.AT3G28380.1; -.
DR PaxDb; Q9LSJ6; -.
DR PRIDE; Q9LSJ6; -.
DR EnsemblPlants; AT3G28380.1; AT3G28380.1; AT3G28380.
DR GeneID; 822467; -.
DR Gramene; AT3G28380.1; AT3G28380.1; AT3G28380.
DR KEGG; ath:AT3G28380; -.
DR Araport; AT3G28380; -.
DR TAIR; locus:2088927; AT3G28380.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q9LSJ6; -.
DR OMA; VAWERIL; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q9LSJ6; -.
DR BioCyc; ARA:AT3G28380-MON; -.
DR PRO; PR:Q9LSJ6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSJ6; baseline and differential.
DR Genevisible; Q9LSJ6; AT.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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 17"
FT /id="PRO_0000227930"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 81..101
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 793..815
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 896..919
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 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 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 642
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; 136062 MW; B063D89077179AB6 CRC64;
MGKEDEKESG RDKMKSFGSI RSIFMHADGV DWILMALGLI GAVGDGFITP VVVFIFNTLL
NNLGTSSSNN KTFMQTISKN VVALLYVACG SWVICFLEGY CWTRTGERQA ARMREKYLRA
VLRQDVGYFD LHVTSTSDVI TSISSDSLVI QDFLSEKLPN FLMNASAFVA SYIVSFILMW
RLTIVGFPFI ILLLVPGLMY GRALVSISRK IHEQYNEAGS IAEQAISSVR TVYAFGSENK
MIGKFSTALR GSVKLGLRQG LAKGITIGSN GVTHAIWAFL TWYGSRLVMN HGSKGGTVFV
VISCITYGGV SLGQSLSNLK YFSEAFVAWE RILEVIKRVP DIDSNKKEGQ ILERMKGEVE
FNHVKFTYLS RPETTIFDDL CLKIPAGKTV ALVGGSGSGK STVISLLQRF YDPIAGEILI
DGVSIDKLQV NWLRSQMGLV SQEPVLFATS ITENILFGKE DASLDEVVEA AKASNAHTFI
SQFPLGYKTQ VGERGVQMSG GQKQRIAIAR AIIKSPKILL LDEATSALDS ESERVVQESL
DNASIGRTTI VIAHRLSTIR NADVICVIHN GQIVETGSHE ELLKRIDGQY TSLVSLQQME
NEESNVNINV SVTKDQVMSL SKDFKYSQHN SIGSTSSSIV TNVSDLIPND NQPLVPSFTR
LMVMNRPEWK HALYGCLSAA LVGVLQPVSA YSAGSVISVF FLTSHDQIKE KTRIYVLLFV
GLAIFSFLVN ISQHYGFAYM GEYLTKRIRE QMLSKILTFE VNWFDIDDNS SGAICSRLAK
DANVVRSMVG DRMSLLVQTI SAVIIACIIG LVIAWRLAIV MISVQPLIVV CFYTQRVLLK
SLSEKASKAQ DESSKLAAEA VSNIRTITAF SSQERIIKLL KKVQEGPRRE SVHRSWLAGI
VLGTSRSLIT CTSALNFWYG GRLIADGKIV SKAFFEIFLI FVTTGRVIAD AGTMTTDLAR
GLDAVGSVFA VLDRCTTIEP KNPDGYVAEK IKGQITFLNV DFAYPTRPDV VIFENFSIEI
DEGKSTAIVG TSGSGKSTII GLIERFYDPL KGTVKIDGRD IRSYHLRSLR KYISLVSQEP
MLFAGTIREN IMYGGTSDKI DESEIIEAAK AANAHDFITS LSNGYDTNCG DKGVQLSGGQ
KQRIAIARAV LKNPSVLLLD EATSALDSKS ERVVQDALER VMVGRTSIMI AHRLSTIQNC
DMIVVLGKGK IVESGTHSSL LEKGPTGTYF SLAGIQRTLC