AB9B_ARATH
ID AB9B_ARATH Reviewed; 1236 AA.
AC Q9M0M2; F4JQQ3; Q9SVW6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=ABC transporter B family member 9;
DE Short=ABC transporter ABCB.9;
DE Short=AtABCB9;
DE AltName: Full=Multidrug resistance protein 9;
DE AltName: Full=P-glycoprotein 9;
GN Name=ABCB9; Synonyms=MDR9, PGP9; OrderedLocusNames=At4g18050;
GN ORFNames=F15J5.20;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB53646.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB53646.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB78807.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78807.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL110123; CAB53646.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161547; CAB78807.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83988.1; -; Genomic_DNA.
DR PIR; H85202; H85202.
DR PIR; T14805; T14805.
DR RefSeq; NP_193539.6; NM_117915.7.
DR AlphaFoldDB; Q9M0M2; -.
DR SMR; Q9M0M2; -.
DR STRING; 3702.AT4G18050.1; -.
DR PaxDb; Q9M0M2; -.
DR PRIDE; Q9M0M2; -.
DR ProteomicsDB; 244632; -.
DR EnsemblPlants; AT4G18050.1; AT4G18050.1; AT4G18050.
DR GeneID; 827530; -.
DR Gramene; AT4G18050.1; AT4G18050.1; AT4G18050.
DR KEGG; ath:AT4G18050; -.
DR Araport; AT4G18050; -.
DR TAIR; locus:2117656; AT4G18050.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q9M0M2; -.
DR OMA; RSDANFW; -.
DR PRO; PR:Q9M0M2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0M2; baseline and differential.
DR Genevisible; Q9M0M2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; -; 2.
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 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..1236
FT /note="ABC transporter B family member 9"
FT /id="PRO_0000227920"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 785..805
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 806..826
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 902..922
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 927..947
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 33..320
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 355..591
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 686..958
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 993..1230
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 593..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1028..1035
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1082
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 746
FT /note="Q -> P (in Ref. 1; CAB53646/CAB78807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1236 AA; 134366 MW; 998787871DDC4489 CRC64;
MEEKSSKKND GGNQKVSFFK LFSFADKTDV VLMTVGTIAA AGNGLTQPFM TLIFGQLINA
FGTTDPDHMV REVWKVAVKF IYLAVYSCVV AFLQVSCWMV TGERQSATIR GLYLKTILRQ
DIGYFDTETN TGEVIGRMSG DTILIQDAMG EKVGKFTQLL CTFLGGFAIA FYKGPLLAGV
LCSCIPLIVI AGAAMSLIMS KMAGRGQVAY AEAGNVVEQT VGAIRTVVAF TGEKQATEKY
ESKLEIAYKT VVQQGLISGF GLGTMLAVIF CSYGLAVWYG AKLIMEKGYN GGQVINVIFA
VLTGGMSLGQ TSPSLNAFAA GRAAAFKMFE TIKRSPKIDA YDMSGSVLED IRGDIELKDV
YFRYPARPDV QIFAGFSLFV PNGKTVALVG QSGSGKSTVI SLIERFYDPE SGQVLIDNID
LKKLQLKWIR SKIGLVSQEP VLFATTIKEN IAYGKEDATD QEIRTAIELA NAAKFIDKLP
QGLDTMVGEH GTQMSGGQKQ RLAIARAILK NPKILLLDEA TSALDAESER IVQDALVNLM
SNRTTVVVAH RLTTIRTADV IAVVHQGKIV EKGTHDEMIQ DPEGAYSQLV RLQEGSKEEA
TESERPETSL DVERSGSLRL SSAMRRSVSR NSSSSRHSFS LASNMFFPGV NVNQTDEMED
EENNVRHKKV SLKRLAHLNK PEIPVLVLGS IAAMVHGTVF PIFGLLLSSS INMFYEPAKI
LKKDSHFWAL IYIALGLTNF VMIPVQNYFF GIAGGKLIKR IRSMCFDKVV HQEISWFDDT
ANSRSLVGDA LALIVQNIAT VTTGLIIAFT ANWILALIVL ALSPFIVIQG YAQTKFLTGF
SADAKAMYEE ASQVANDAVS SIRTVASFCA EEKVMDLYQQ KCDGPKKNGV RLGLLSGAGF
GFSFFFLYCI NCVCFVSGAG LIQIGKATFG EVFKVFFALT IMAIGVSQTS AMAPDSNKAK
DSAASIFDIL DSTPKIDSSS DEGTTLQNVN GDIEFRHVSF RYPMRPDVQI FRDLCLTIPS
GKTVALVGES GSGKSTVISM IERFYNPDSG KILIDQVEIQ TFKLSWLRQQ MGLVSQEPIL
FNETIRSNIA YGKTGGATEE EIIAAAKAAN AHNFISSLPQ GYDTSVGERG VQLSGGQKQR
IAIARAILKD PKILLLDEAT SALDAESERV VQDALDRVMV NRTTVVVAHR LTTIKNADVI
AVVKNGVIAE KGRHETLMKI SGGAYASLVT LHMSAN
