AB21B_ARATH
ID AB21B_ARATH Reviewed; 1296 AA.
AC Q9M1Q9; A0A1I9LRJ8; F4IX45;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=ABC transporter B family member 21;
DE Short=ABC transporter ABCB.21;
DE Short=AtABCB21;
DE AltName: Full=Multidrug resistance protein 17;
DE AltName: Full=P-glycoprotein 21;
GN Name=ABCB21; Synonyms=MDR17, PGP21; OrderedLocusNames=At3g62150;
GN ORFNames=T17J13.110;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657 AND SER-660, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
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).
RN [6]
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 -!- 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=CAB71875.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138651; CAB71875.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80316.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65205.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65206.1; -; Genomic_DNA.
DR PIR; T48007; T48007.
DR RefSeq; NP_001327192.1; NM_001340143.1.
DR RefSeq; NP_001327193.1; NM_001340142.1.
DR RefSeq; NP_191774.2; NM_116080.3.
DR AlphaFoldDB; Q9M1Q9; -.
DR SMR; Q9M1Q9; -.
DR STRING; 3702.AT3G62150.1; -.
DR TCDB; 3.A.1.201.36; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q9M1Q9; -.
DR PaxDb; Q9M1Q9; -.
DR PRIDE; Q9M1Q9; -.
DR ProteomicsDB; 243270; -.
DR EnsemblPlants; AT3G62150.1; AT3G62150.1; AT3G62150.
DR EnsemblPlants; AT3G62150.2; AT3G62150.2; AT3G62150.
DR EnsemblPlants; AT3G62150.3; AT3G62150.3; AT3G62150.
DR GeneID; 825388; -.
DR Gramene; AT3G62150.1; AT3G62150.1; AT3G62150.
DR Gramene; AT3G62150.2; AT3G62150.2; AT3G62150.
DR Gramene; AT3G62150.3; AT3G62150.3; AT3G62150.
DR KEGG; ath:AT3G62150; -.
DR Araport; AT3G62150; -.
DR TAIR; locus:2097978; AT3G62150.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q9M1Q9; -.
DR OMA; LFMLPMT; -.
DR OrthoDB; 186078at2759; -.
DR BioCyc; ARA:AT3G62150-MON; -.
DR PRO; PR:Q9M1Q9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1Q9; baseline and differential.
DR Genevisible; Q9M1Q9; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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:0010328; F:auxin influx transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0010315; P:auxin export across the plasma membrane; IDA:TAIR.
DR GO; GO:0060919; P:auxin import into cell; IDA: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 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; Glycoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1296
FT /note="ABC transporter B family member 21"
FT /id="PRO_0000227928"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 731..751
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 865..885
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 952..972
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 80..368
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 403..639
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 730..1017
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1052..1289
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 438..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1087..1094
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15308754"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15308754"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1296 AA; 140334 MW; ED16D162A767C3A6 CRC64;
MDSVIESEEG LKVDSPNRAD AETSNSKIHE EDEKELKTES DLKEEKKKTE KNKQEEDEKT
KTVPFHKLFA FADSFDIILM ILGTIGAVGN GLGFPIMTIL FGDVIDVFGQ NQNSSDVSDK
IAKVALKFVY LGLGTLVAAL LQVSGWMISG ERQAGRIRSL YLQTILRQDI AFFDVETNTG
EVVGRMSGDT VLIQDAMGEK VGKAIQLVST FIGGFVIAFT EGWLLTLVMV SSIPLLVMSG
AALAIVISKM ASRGQTSYAK AAVVVEQTVG SIRTVASFTG EKQAISNYNK HLVSAYRAGV
FEGASTGLGL GTLNIVIFCT YALAVWYGGK MILEKGYTGG QVLIIIFAVL TGSMSLGQAS
PCLSAFAAGQ AAAYKMFEAI KRKPEIDASD TTGKVLDDIR GDIELNNVNF SYPARPEEQI
FRGFSLSISS GSTVALVGQS GSGKSTVVSL IERFYDPQSG EVRIDGINLK EFQLKWIRSK
IGLVSQEPVL FTSSIKENIA YGKENATVEE IRKATELANA SKFIDKLPQG LDTMVGEHGT
QLSGGQKQRI AVARAILKDP RILLLDEATS ALDAESERIV QEALDRIMVN RTTVVVAHRL
STVRNADMIA VIHQGKIVEK GSHSELLRDP EGAYSQLIRL QEDTKQTEDS TDEQKLSMES
MKRSSLRKSS LSRSLSKRSS SFSMFGFPAG IDTNNEAIPE KDIKVSTPIK EKKVSFFRVA
ALNKPEIPML ILGSIAAVLN GVILPIFGIL ISSVIKAFFK PPEQLKSDTR FWAIIFMLLG
VASMVVFPAQ TIFFSIAGCK LVQRIRSMCF EKVVRMEVGW FDETENSSGA IGARLSADAA
TVRGLVGDAL AQTVQNLASV TAGLVIAFVA SWQLAFIVLA MLPLIGLNGY IYMKFMVGFS
ADAKRMYEEA SQVANDAVGS IRTVASFCAE EKVMKMYKKK CEGPMRTGIR QGIVSGIGFG
VSFFVLFSSY AASFYAGARL VDDGKTTFDS VFRVFFALTM AAVAISQSSS LSPDSSKASN
AAASIFAVID RESKIDPSDE SGRVLDNVKG DIELRHISFK YPSRPDVQIF QDLCLSIRAG
KTIALVGESG SGKSTVIALL QRFYDPDSGQ ITLDGVEIKT LQLKWLRQQT GLVSQEPVLF
NETIRANIAY GKGGDATETE IVSAAELSNA HGFISGLQQG YDTMVGERGV QLSGGQKQRV
AIARAIVKDP KVLLLDEATS ALDAESERVV QDALDRVMVN RTTVVVAHRL STIKNADVIA
VVKNGVIVEK GKHETLINIK DGVYASLVQL HLSAST
