AB3B_ARATH
ID AB3B_ARATH Reviewed; 1229 AA.
AC Q9SYI2; O49749;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ABC transporter B family member 3;
DE Short=ABC transporter ABCB.3;
DE Short=AtABCB3;
DE AltName: Full=P-glycoprotein 3;
DE AltName: Full=Putative multidrug resistance protein 3;
GN Name=ABCB3; Synonyms=MDR3, PGP3; OrderedLocusNames=At4g01820;
GN ORFNames=T7B11.8;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Sidler M., Dudler R.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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; Y15990; CAA75922.1; -; Genomic_DNA.
DR EMBL; AC007138; AAD22644.1; -; Genomic_DNA.
DR EMBL; AL161493; CAB80675.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82081.1; -; Genomic_DNA.
DR PIR; D85023; D85023.
DR PIR; T52319; T52319.
DR RefSeq; NP_192091.1; NM_116412.2.
DR AlphaFoldDB; Q9SYI2; -.
DR SMR; Q9SYI2; -.
DR BioGRID; 12248; 1.
DR STRING; 3702.AT4G01820.1; -.
DR iPTMnet; Q9SYI2; -.
DR PaxDb; Q9SYI2; -.
DR PRIDE; Q9SYI2; -.
DR EnsemblPlants; AT4G01820.1; AT4G01820.1; AT4G01820.
DR GeneID; 826951; -.
DR Gramene; AT4G01820.1; AT4G01820.1; AT4G01820.
DR KEGG; ath:AT4G01820; -.
DR Araport; AT4G01820; -.
DR TAIR; locus:2141350; AT4G01820.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_8_1; -.
DR InParanoid; Q9SYI2; -.
DR OMA; CEETIKS; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q9SYI2; -.
DR BioCyc; ARA:AT4G01820-MON; -.
DR PRO; PR:Q9SYI2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SYI2; baseline and differential.
DR Genevisible; Q9SYI2; 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; ISS:TAIR.
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..1229
FT /note="ABC transporter B family member 3"
FT /id="PRO_0000227914"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 172..192
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 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 797..817
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 888..908
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 25..313
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 348..584
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 662..949
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 984..1222
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 594..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383..390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1019..1026
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1073
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 87
FT /note="Q -> E (in Ref. 1; CAA75922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1229 AA; 133234 MW; 613009768A1AA9D5 CRC64;
MEEKTKTVPF YKLFSFSDST DVLLMIVGSI GAIGNGVGFP LMTLLFGDLI DSIGQNQSNK
DIVEIVSKVC LKFVYLGLGT LGAAFLQVAC WMITGERQAA RIRSLYLKTI LRQDIGFFDV
ETSTGEVVGR MSGDTVLILE AMGEKVGKFI QLIATFVGGF VLAFVKGWLL TLVMLVSIPL
LAIAGAAMPI IVTRASSREQ AAYAKASTVV EQTLGSIRTV ASFTGEKQAM KSYREFINLA
YRASVKQGFS MGLGLGVVFF VFFCSYALAI WFGGEMILKK GYTGGEVVNV MVTVVASSMS
LGQTTPCLTA FAAGKAAAYK MFETIERKPS IDAFDLNGKV LEDIRGEIEL RDVCFSYPAR
PMEEVFGGFS LLIPSGATAA LVGESGSGKS SVISLIERFY DPSSGSVLID GVNLKEFQLK
WIRGKIGLVS QEPVLFSSSI MENIGYGKEN ATVEEIQAAA KLANAANFID KLPRGLETLV
GEHGTQLSGG QKQRIAIARA ILKDPRILLL DEATSALDAE SERVVQEALD RVMMSRTTVI
VAHRLSTVRN ADMIAVIHRG KIVEEGSHSE LLKDHEGAYA QLIRLQKIKK EPKRLESSNE
LRDRSINRGS SRNIRTRVHD DDSVSVLGLL GRQENTEISR EQSRNVSITR IAALNKPETT
ILILGTLLGA VNGTIFPIFG ILFAKVIEAF FKPPHDMKRD SRFWSMIFVL LGVASLIVYP
MHTYLFAVAG GRLIQRIRVM CFEKVVHMEV GWFDDPENSS GTIGSRLSAD AALIKTLVGD
SLSLSVKNAA AAVSGLIIAF TASWKLAVII LVMIPLIGIN GYLQIKFIKG FTADAKAKYE
EASQVANDAV GSIRTVASFC AEEKVMEMYK KRCEDTIKSG IKQGLISGVG FGISFFVLYS
VYASCFYVGA RLVKAGRTNF NDVFQVFLAL TMTAIGISQA SSFAPDSSKA KGAAASIFGI
IDGKSMIDSR DESGLVLENV KGDIELCHIS FTYQTRPDVQ IFRDLCFAIR AGQTVALVGE
SGSGKSTVIS LLQRFYDPDS GHITLDRVEL KKLQLKWVRQ QMGLVGQEPV LFNDTIRSNI
AYGKGGDEAS EAEIIAAAEL ANAHGFISSI QQGYDTVVGE RGIQLSGGQK QRVAIARAIV
KEPKILLLDE ATSALDAESE RVVQDALDRV MVNRTTVVVA HRLSTIKNAD VIAVVKNGVI
VEKGTHETLI NIEGGVYASL VQLHISASS
