AB7B_ARATH
ID AB7B_ARATH Reviewed; 1248 AA.
AC Q9FHF1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=ABC transporter B family member 7;
DE Short=ABC transporter ABCB.7;
DE Short=AtABCB7;
DE AltName: Full=Multidrug resistance protein 7;
DE AltName: Full=P-glycoprotein 7;
GN Name=ABCB7; Synonyms=MDR7, PGP7; OrderedLocusNames=At5g46540;
GN ORFNames=K11I1.13;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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}.
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; AB019223; BAB10822.1; -; Genomic_DNA.
DR EMBL; AB028605; BAB10822.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED95396.1; -; Genomic_DNA.
DR RefSeq; NP_199466.1; NM_124024.2.
DR AlphaFoldDB; Q9FHF1; -.
DR SMR; Q9FHF1; -.
DR STRING; 3702.AT5G46540.1; -.
DR PaxDb; Q9FHF1; -.
DR PRIDE; Q9FHF1; -.
DR ProteomicsDB; 244615; -.
DR EnsemblPlants; AT5G46540.1; AT5G46540.1; AT5G46540.
DR GeneID; 834697; -.
DR Gramene; AT5G46540.1; AT5G46540.1; AT5G46540.
DR KEGG; ath:AT5G46540; -.
DR Araport; AT5G46540; -.
DR TAIR; locus:2151496; AT5G46540.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q9FHF1; -.
DR OMA; FAIWYGA; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q9FHF1; -.
DR BioCyc; ARA:AT5G46540-MON; -.
DR PRO; PR:Q9FHF1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHF1; baseline and differential.
DR Genevisible; Q9FHF1; AT.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA: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:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 3.
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..1248
FT /note="ABC transporter B family member 7"
FT /id="PRO_0000227918"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 158..175
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 299..321
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 834..854
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 939..959
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 35..322
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 357..593
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 683..970
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1005..1242
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 392..399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1040..1047
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1248 AA; 136112 MW; 6D25B1F93EB7E3F0 CRC64;
MAEKAKKKKN GGGGNQRIAF YKLFTFADRY DIVLMVIGTL SAMANGLTQP FMSILMGQLI
NVFGFSDHDH VFKEVSKVAV KFLYLAAYAG VVSFLQVSCW MVTGERQSTR IRRLYLKTIL
RQDIGFFDTE TNTGEVIGRM SGDTILIQDS MGEKVGKFTQ LVSSFVGGFT VAFIVGMKLT
LALLPCVPLI VGTGGAMTYI MSKKAQRVQL AYTEAGNVVQ QAVGSIRTVV AFTGEKQSMG
KYEKKLEIAY KSMVKQGLYS GLGIGIMMVV VYCTYGFAIW YGARQIIEKG YTGGQVMNVI
TSILTGGMAL GQTLPSLNSF AAGTAAAYKM FETIKRKPKI DAYDMSGEVL EEIKGDIELR
DVYFRYPARP DVQIFVGFSL TVPNGMTVAL VGQSGSGKST VISLIERFYD PESGEVLIDG
IDLKKFQVKW IRSKIGLVSQ EPILFATTIR ENIVYGKKDA SDQEIRTALK LANASNFIDK
LPQGLETMVG EHGTQLSGGQ KQRIAIARAI LKNPKILLLD EATSALDAES ERIVQDALVK
LMLSRTTVVV AHRLTTIRTA DMIAVVQQGK VIEKGTHDEM IKDPEGTYSQ LVRLQEGSKK
EEAIDKEPEK CEMSLEIESS DSQNGIHSGT LTSPSGLPGV ISLDQTEEFH ENISSTKTQT
VKKGKEVSLR RLAHLNKPEI SVLLLGSLAA VIHGIVFPVQ GLLLSRTIRI FFEPSNKLKN
DSLFWALIFV ALGLTDLIVI PLQNYLFAIA GAKLIKRIRS LSFDRVLHQD ISWFDDTKNS
SGVIGARLST DASTVKSIVG DVLGLIMQNM ATIIGAFIIA FTANWLLALM ALLVAPVMFF
QGYYQIKFIT GFGAKARGKY EEASQVASDA VSSIRTVASF CAEDKVMDLY QEKCDEPKQQ
GFKLGLVSGL CYGGSYLALY VIESVCFLGG SWLIQNRRAT FGEFFQVFFA LTLTAVGVTQ
TSTMAPDINK AKDSAASIFD ILDSKPKIDS SSEKGTILPI VHGDIELQHV SFRYPMRPDI
QIFSDLCLTI SSGQTVALVG ESGSGKSTVI SLLERFYDPD SGKILLDQVE IQSLKLSWLR
EQMGLVSQEP VLFNETIGSN IAYGKIGGAT EEEIITAAKA ANVHNFISSL PQGYETSVGE
RGVQLSGGQK QRIAIARAIL KDPKILLLDE ATSALDAESE RVVQDALDQV MVNRTTVVVA
HLLTTIKDAD MIAVVKNGVI AESGRHETLM EISGGAYASL VAFNMSAN