AB19B_ARATH
ID AB19B_ARATH Reviewed; 1252 AA.
AC Q9LJX0; Q8GZ77; Q8H6F5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ABC transporter B family member 19;
DE Short=ABC transporter ABCB.19;
DE Short=AtABCB19;
DE AltName: Full=Multidrug resistance protein 11;
DE AltName: Full=P-glycoprotein 19;
GN Name=ABCB19; Synonyms=MDR1, MDR11, PGP19; OrderedLocusNames=At3g28860;
GN ORFNames=MLD15.2;
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 [MRNA], PROTEIN SEQUENCE OF 523-536 AND 941-947,
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH NPA,
RP AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=11701880; DOI=10.2307/3871586;
RA Noh B., Murphy A.S., Spalding E.P.;
RT "Multidrug resistance-like genes of Arabidopsis required for auxin
RT transport and auxin-mediated development.";
RL Plant Cell 13:2441-2454(2001).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP PROTEIN SEQUENCE OF 36-54; 956-963 AND 1111-1122, AND INTERACTION WITH NPA.
RX PubMed=16243904; DOI=10.1105/tpc.105.035816;
RA Terasaka K., Blakeslee J.J., Titapiwatanakun B., Peer W.A.,
RA Bandyopadhyay A., Makam S.N., Lee O.R., Richards E.L., Murphy A.S.,
RA Sato F., Yazaki K.;
RT "PGP4, an ATP binding cassette P-glycoprotein, catalyzes auxin transport in
RT Arabidopsis thaliana roots.";
RL Plant Cell 17:2922-2939(2005).
RN [6]
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 [7]
RP FUNCTION, AND INTERACTION WITH FKBP42/TWD1.
RX PubMed=14517332; DOI=10.1091/mbc.e02-10-0698;
RA Geisler M., Kolukisaoglu H.U., Bouchard R., Billion K., Berger J., Saal B.,
RA Frangne N., Koncz-Kalman Z., Koncz C., Dudler R., Blakeslee J.J.,
RA Murphy A.S., Martinoia E., Schulz B.;
RT "TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like
RT protein, interacts with Arabidopsis multidrug resistance-like transporters
RT AtPGP1 and AtPGP19.";
RL Mol. Biol. Cell 14:4238-4249(2003).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=15908594; DOI=10.1104/pp.105.061572;
RA Lin R., Wang H.;
RT "Two homologous ATP-binding cassette transporter proteins, AtMDR1 and
RT AtPGP1, regulate Arabidopsis photomorphogenesis and root development by
RT mediating polar auxin transport.";
RL Plant Physiol. 138:949-964(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [10]
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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Auxin efflux transporter that acts as a negative regulator of
CC light signaling to promote hypocotyl elongation. Mediates the
CC accumulation of chlorophyll and anthocyanin, as well as the expression
CC of genes in response to light. Participates in auxin efflux and thus
CC regulates the polar auxin basipetal transport (from auxin-producing
CC leaves to auxin-sensitive tissues, and from root tips to root
CC elongating zone). Involved in diverse auxin-mediated responses
CC including gravitropism, phototropism and lateral root formation.
CC {ECO:0000269|PubMed:11701880, ECO:0000269|PubMed:14517332,
CC ECO:0000269|PubMed:15908594}.
CC -!- SUBUNIT: Interacts with 1-naphthylphthalamic acid (NPA), and
CC FKBP42/TWD1. {ECO:0000269|PubMed:11701880, ECO:0000269|PubMed:14517332,
CC ECO:0000269|PubMed:16243904}.
CC -!- INTERACTION:
CC Q9LJX0; Q9C6B8: PIN1; NbExp=7; IntAct=EBI-371791, EBI-1541799;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, mostly in shoot meristems.
CC {ECO:0000269|PubMed:11701880}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, confined to hypocotyls in darkness,
CC but expressed in all tissues except in hypocotyls in light. In flowers,
CC present in all organs except petals. {ECO:0000269|PubMed:11701880}.
CC -!- INDUCTION: By auxin (IAA). Induced by red light, but repressed by far-
CC red light. {ECO:0000269|PubMed:11701880, ECO:0000269|PubMed:15908594}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF540384; AAN28720.2; -; mRNA.
DR EMBL; AP000386; BAB02129.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77498.1; -; Genomic_DNA.
DR EMBL; AK117168; BAC41846.1; -; mRNA.
DR RefSeq; NP_189528.1; NM_113807.3.
DR AlphaFoldDB; Q9LJX0; -.
DR SMR; Q9LJX0; -.
DR BioGRID; 7848; 25.
DR IntAct; Q9LJX0; 4.
DR STRING; 3702.AT3G28860.1; -.
DR TCDB; 3.A.1.201.6; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q9LJX0; -.
DR PaxDb; Q9LJX0; -.
DR PRIDE; Q9LJX0; -.
DR ProteomicsDB; 243294; -.
DR EnsemblPlants; AT3G28860.1; AT3G28860.1; AT3G28860.
DR GeneID; 822519; -.
DR Gramene; AT3G28860.1; AT3G28860.1; AT3G28860.
DR KEGG; ath:AT3G28860; -.
DR Araport; AT3G28860; -.
DR TAIR; locus:2090734; AT3G28860.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q9LJX0; -.
DR OMA; AFYMQRT; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q9LJX0; -.
DR BioCyc; ARA:AT3G28860-MON; -.
DR PRO; PR:Q9LJX0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJX0; baseline and differential.
DR Genevisible; Q9LJX0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0010329; F:auxin efflux transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0010541; P:acropetal auxin transport; IMP:TAIR.
DR GO; GO:0043481; P:anthocyanin accumulation in tissues in response to UV light; IMP:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0060918; P:auxin transport; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010540; P:basipetal auxin transport; IMP:TAIR.
DR GO; GO:0090691; P:formation of plant organ boundary; IMP:TAIR.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009637; P:response to blue light; IMP:TAIR.
DR GO; GO:0010218; P:response to far red light; IMP:TAIR.
DR GO; GO:0009639; P:response to red or far red light; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048443; P:stamen development; IGI: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 1: Evidence at protein level;
KW ATP-binding; Auxin signaling pathway; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1252
FT /note="ABC transporter B family member 19"
FT /id="PRO_0000227922"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 914..934
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 41..330
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 365..601
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 687..975
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1010..1246
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 965..1252
FT /note="Interaction with FKBP42/TWD1"
FT BINDING 400..407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1045..1052
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
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 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 814
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1064
FT /note="P -> L (in Ref. 1; AAN28720)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="G -> E (in Ref. 4; BAC41846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1252 AA; 136788 MW; 6EB8D5229FBFC7F3 CRC64;
MSETNTTDAK TVPAEAEKKK EQSLPFFKLF SFADKFDYLL MFVGSLGAIV HGSSMPVFFL
LFGQMVNGFG KNQMDLHQMV HEVSRYSLYF VYLGLVVCFS SYAEIACWMY SGERQVAALR
KKYLEAVLKQ DVGFFDTDAR TGDIVFSVST DTLLVQDAIS EKVGNFIHYL STFLAGLVVG
FVSAWKLALL SVAVIPGIAF AGGLYAYTLT GITSKSRESY ANAGVIAEQA IAQVRTVYSY
VGESKALNAY SDAIQYTLKL GYKAGMAKGL GLGCTYGIAC MSWALVFWYA GVFIRNGQTD
GGKAFTAIFS AIVGGMSLGQ SFSNLGAFSK GKAAGYKLME IINQRPTIIQ DPLDGKCLDQ
VHGNIEFKDV TFSYPSRPDV MIFRNFNIFF PSGKTVAVVG GSGSGKSTVV SLIERFYDPN
SGQILLDGVE IKTLQLKFLR EQIGLVNQEP ALFATTILEN ILYGKPDATM VEVEAAASAA
NAHSFITLLP KGYDTQVGER GVQLSGGQKQ RIAIARAMLK DPKILLLDEA TSALDASSES
IVQEALDRVM VGRTTVVVAH RLCTIRNVDS IAVIQQGQVV ETGTHEELIA KSGAYASLIR
FQEMVGTRDF SNPSTRRTRS TRLSHSLSTK SLSLRSGSLR NLSYSYSTGA DGRIEMISNA
ETDRKTRAPE NYFYRLLKLN SPEWPYSIMG AVGSILSGFI GPTFAIVMSN MIEVFYYTDY
DSMERKTKEY VFIYIGAGLY AVGAYLIQHY FFSIMGENLT TRVRRMMLSA ILRNEVGWFD
EDEHNSSLIA ARLATDAADV KSAIAERISV ILQNMTSLLT SFIVAFIVEW RVSLLILGTF
PLLVLANFAQ QLSLKGFAGD TAKAHAKTSM IAGEGVSNIR TVAAFNAQSK ILSLFCHELR
VPQKRSLYRS QTSGFLFGLS QLALYGSEAL ILWYGAHLVS KGVSTFSKVI KVFVVLVITA
NSVAETVSLA PEIIRGGEAV GSVFSVLDRQ TRIDPDDADA DPVETIRGDI EFRHVDFAYP
SRPDVMVFRD FNLRIRAGHS QALVGASGSG KSSVIAMIER FYDPLAGKVM IDGKDIRRLN
LKSLRLKIGL VQQEPALFAA TIFDNIAYGK DGATESEVID AARAANAHGF ISGLPEGYKT
PVGERGVQLS GGQKQRIAIA RAVLKNPTVL LLDEATSALD AESECVLQEA LERLMRGRTT
VVVAHRLSTI RGVDCIGVIQ DGRIVEQGSH SELVSRPEGA YSRLLQLQTH RI
