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ABC transporter B family member 19 (ABC transporter ABCB.19) (AtABCB19) (Multidrug resistance protein 11) (P-glycoprotein 19)

 AB19B_ARATH             Reviewed;        1252 AA.
Q9LJX0; Q8GZ77; Q8H6F5;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 127.
RecName: Full=ABC transporter B family member 19;
Short=ABC transporter ABCB.19;
Short=AtABCB19;
AltName: Full=Multidrug resistance protein 11;
AltName: Full=P-glycoprotein 19;
Name=ABCB19; Synonyms=MDR1, MDR11, PGP19; OrderedLocusNames=At3g28860;
ORFNames=MLD15.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 523-536 AND 941-947,
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH
NPA, AND INDUCTION.
STRAIN=cv. Columbia; TISSUE=Seedling;
PubMed=11701880; DOI=10.1105/tpc.010350;
Noh B., Murphy A.S., Spalding E.P.;
"Multidrug resistance-like genes of Arabidopsis required for auxin
transport and auxin-mediated development.";
Plant Cell 13:2441-2454(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[5]
PROTEIN SEQUENCE OF 36-54; 956-963 AND 1111-1122, AND INTERACTION WITH
NPA.
PubMed=16243904; DOI=10.1105/tpc.105.035816;
Terasaka K., Blakeslee J.J., Titapiwatanakun B., Peer W.A.,
Bandyopadhyay A., Makam S.N., Lee O.R., Richards E.L., Murphy A.S.,
Sato F., Yazaki K.;
"PGP4, an ATP binding cassette P-glycoprotein, catalyzes auxin
transport in Arabidopsis thaliana roots.";
Plant Cell 17:2922-2939(2005).
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11346655; DOI=10.1074/jbc.M103104200;
Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
"The Arabidopsis thaliana ABC protein superfamily, a complete
inventory.";
J. Biol. Chem. 276:30231-30244(2001).
[7]
FUNCTION, AND INTERACTION WITH FKBP42/TWD1.
PubMed=14517332; DOI=10.1091/mbc.E02-10-0698;
Geisler M., Kolukisaoglu H.U., Bouchard R., Billion K., Berger J.,
Saal B., Frangne N., Koncz-Kalman Z., Koncz C., Dudler R.,
Blakeslee J.J., Murphy A.S., Martinoia E., Schulz B.;
"TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like
protein, interacts with Arabidopsis multidrug resistance-like
transporters AtPGP1 and AtPGP19.";
Mol. Biol. Cell 14:4238-4249(2003).
[8]
FUNCTION, AND INDUCTION.
PubMed=15908594; DOI=10.1104/pp.105.061572;
Lin R., Wang H.;
"Two homologous ATP-binding cassette transporter proteins, AtMDR1 and
AtPGP1, regulate Arabidopsis photomorphogenesis and root development
by mediating polar auxin transport.";
Plant Physiol. 138:949-964(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Seedling;
PubMed=17586839; DOI=10.1074/mcp.M700164-MCP200;
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,
Schulze W.X.;
"Temporal analysis of sucrose-induced phosphorylation changes in
plasma membrane proteins of Arabidopsis.";
Mol. Cell. Proteomics 6:1711-1726(2007).
[10]
GENE FAMILY, AND NOMENCLATURE.
PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A.,
Rea P.A., Samuels L., Schulz B., Spalding E.J., Yazaki K.,
Theodoulou F.L.;
"Plant ABC proteins - a unified nomenclature and updated inventory.";
Trends Plant Sci. 13:151-159(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
-!- FUNCTION: Auxin efflux transporter that acts as a negative
regulator of light signaling to promote hypocotyl elongation.
Mediates the accumulation of chlorophyll and anthocyanin, as well
as the expression of genes in response to light. Participates in
auxin efflux and thus regulates the polar auxin basipetal
transport (from auxin-producing leaves to auxin-sensitive tissues,
and from root tips to root elongating zone). Involved in divers
auxin-mediated responses including gravitropism, phototropism and
lateral root formation. {ECO:0000269|PubMed:11701880,
ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:15908594}.
-!- SUBUNIT: Interacts with 1-naphthylphthalamic acid (NPA), and
FKBP42/TWD1. {ECO:0000269|PubMed:11701880,
ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:16243904}.
-!- INTERACTION:
Q9C6B8:PIN1; NbExp=7; IntAct=EBI-371791, EBI-1541799;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Ubiquitous, mostly in shoot meristems.
{ECO:0000269|PubMed:11701880}.
-!- DEVELOPMENTAL STAGE: In seedlings, confined to hypocotyls in
darkness, but expressed in all tissues except in hypocotyls in
light. In flowers, present in all organs except petals.
{ECO:0000269|PubMed:11701880}.
-!- INDUCTION: By auxin (IAA). Induced by red light, but repressed by
far-red light. {ECO:0000269|PubMed:11701880,
ECO:0000269|PubMed:15908594}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF540384; AAN28720.2; -; mRNA.
EMBL; AP000386; BAB02129.1; -; Genomic_DNA.
EMBL; CP002686; AEE77498.1; -; Genomic_DNA.
EMBL; AK117168; BAC41846.1; -; mRNA.
RefSeq; NP_189528.1; NM_113807.3.
UniGene; At.24939; -.
ProteinModelPortal; Q9LJX0; -.
SMR; Q9LJX0; -.
BioGrid; 7848; 5.
IntAct; Q9LJX0; 3.
MINT; MINT-1701415; -.
STRING; 3702.AT3G28860.1; -.
TCDB; 3.A.1.201.6; the atp-binding cassette (abc) superfamily.
iPTMnet; Q9LJX0; -.
PaxDb; Q9LJX0; -.
EnsemblPlants; AT3G28860.1; AT3G28860.1; AT3G28860.
GeneID; 822519; -.
Gramene; AT3G28860.1; AT3G28860.1; AT3G28860.
KEGG; ath:AT3G28860; -.
Araport; AT3G28860; -.
TAIR; locus:2090734; AT3G28860.
eggNOG; KOG0055; Eukaryota.
eggNOG; COG1132; LUCA.
InParanoid; Q9LJX0; -.
KO; K05658; -.
OMA; VDCKFTY; -.
OrthoDB; EOG093600JM; -.
PhylomeDB; Q9LJX0; -.
BioCyc; ARA:AT3G28860-MONOMER; -.
Reactome; R-ATH-159418; Recycling of bile acids and salts.
Reactome; R-ATH-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-ATH-382556; ABC-family proteins mediated transport.
PRO; PR:Q9LJX0; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q9LJX0; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
GO; GO:0010329; F:auxin efflux transmembrane transporter activity; IDA:TAIR.
GO; GO:0010541; P:acropetal auxin transport; IMP:TAIR.
GO; GO:0043481; P:anthocyanin accumulation in tissues in response to UV light; IMP:TAIR.
GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
GO; GO:0060918; P:auxin transport; IMP:TAIR.
GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0010540; P:basipetal auxin transport; IMP:TAIR.
GO; GO:0090691; P:formation of plant organ boundary; IMP:TAIR.
GO; GO:0048527; P:lateral root development; IMP:TAIR.
GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
GO; GO:0008361; P:regulation of cell size; IMP:TAIR.
GO; GO:0009733; P:response to auxin; IMP:TAIR.
GO; GO:0009637; P:response to blue light; IMP:TAIR.
GO; GO:0010218; P:response to far red light; IMP:TAIR.
GO; GO:0009639; P:response to red or far red light; IMP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0048443; P:stamen development; IGI:TAIR.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Auxin signaling pathway; Cell membrane;
Complete proteome; Direct protein sequencing; Glycoprotein; Membrane;
Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1252 ABC transporter B family member 19.
/FTId=PRO_0000227922.
TRANSMEM 42 62 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 88 108 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 163 183 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 187 207 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 274 294 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 308 328 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 688 708 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 732 752 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 822 842 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 914 934 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 949 969 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
DOMAIN 41 330 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 365 601 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 687 975 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1010 1246 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 400 407 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1045 1052 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 965 1252 Interaction with FKBP42/TWD1.
CARBOHYD 5 5 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 641 641 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 758 758 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 785 785 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 814 814 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 1064 1064 P -> L (in Ref. 1; AAN28720).
{ECO:0000305}.
CONFLICT 1222 1222 G -> E (in Ref. 4; BAC41846).
{ECO:0000305}.
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


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