AB27B_ARATH
ID AB27B_ARATH Reviewed; 644 AA.
AC Q0WML0; Q8RY45; Q9FID4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ABC transporter B family member 27;
DE Short=ABC transporter ABCB.27;
DE Short=AtABCB27;
DE AltName: Full=Aluminum tolerance-related ATP-binding cassette transporter;
DE AltName: Full=Antigen peptide transporter-like 2;
DE AltName: Full=Transporter associated with antigen processing-like protein 2;
DE Short=AtTAP2;
GN Name=ABCB27; Synonyms=ALS1, TAP2; OrderedLocusNames=At5g39040;
GN ORFNames=MXF12.50;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLU-261, LACK OF INDUCTION BY
RP ALUMINUM, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=17171374; DOI=10.1007/s00425-006-0452-4;
RA Larsen P.B., Cancel J., Rounds M., Ochoa V.;
RT "Arabidopsis ALS1 encodes a root tip and stele localized half type ABC
RT transporter required for root growth in an aluminum toxic environment.";
RL Planta 225:1447-1458(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [7]
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 -!- FUNCTION: Probably involved in redistribution of internalized aluminum.
CC May mediate vacuolar sequestration of a metal complex.
CC {ECO:0000269|PubMed:17171374}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17151019,
CC ECO:0000269|PubMed:17171374}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:17171374}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissue of roots, leaves,
CC stems and flowers, in the distal portion of the root tip, in leaf
CC hyathodes and in anther filaments, pistils and flower receptacles.
CC {ECO:0000269|PubMed:17171374}.
CC -!- INDUCTION: Not induces by aluminum treatment.
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=BAB10828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY078410; AAL85486.1; -; mRNA.
DR EMBL; DQ469798; ABG37923.1; -; mRNA.
DR EMBL; AB016892; BAB10828.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94390.1; -; Genomic_DNA.
DR EMBL; AK229810; BAF01641.1; -; mRNA.
DR RefSeq; NP_198720.2; NM_123266.8.
DR AlphaFoldDB; Q0WML0; -.
DR SMR; Q0WML0; -.
DR BioGRID; 19147; 11.
DR IntAct; Q0WML0; 11.
DR STRING; 3702.AT5G39040.1; -.
DR TCDB; 3.A.1.201.8; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q0WML0; -.
DR PaxDb; Q0WML0; -.
DR PRIDE; Q0WML0; -.
DR ProteomicsDB; 244365; -.
DR EnsemblPlants; AT5G39040.1; AT5G39040.1; AT5G39040.
DR GeneID; 833896; -.
DR Gramene; AT5G39040.1; AT5G39040.1; AT5G39040.
DR KEGG; ath:AT5G39040; -.
DR Araport; AT5G39040; -.
DR TAIR; locus:2177162; AT5G39040.
DR eggNOG; KOG0058; Eukaryota.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; Q0WML0; -.
DR OMA; FNTLQMG; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; Q0WML0; -.
DR PRO; PR:Q0WML0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WML0; baseline and differential.
DR Genevisible; Q0WML0; AT.
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:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; 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:0010044; P:response to aluminum ion; IMP:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..644
FT /note="ABC transporter B family member 27"
FT /id="PRO_0000300103"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 71..362
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 396..633
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 431..438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 261
FT /note="E->K: In als1-1; loss of aluminum tolerance."
FT /evidence="ECO:0000269|PubMed:17171374"
FT CONFLICT 47
FT /note="H -> Y (in Ref. 1; AAL85486)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="D -> N (in Ref. 1; AAL85486)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 69104 MW; 5A29C0CF8AC19884 CRC64;
MGNKKLLTGG SSKTHGSGSS YRDPLLQNQE DKPKANGSEN GLNDLEHGVV EAANVGFGRV
FALAKPDAGK LVIGTIALLI GSTTNLLVPK FGGMIIDIVS RDVKTPEQQT ESLIAVRNAV
VIILLIVVIG SICTALRAWL FNSASERVVA RLRKDLFRHL MHQEIAFYDV TKTGELLSRL
SEDTQIIKNA ATTNLSEALR NVTTALIGVG FMFTSSWKLT LLALVVVPVI SVAVKQFGRY
LRELSHTTQA AAAVAASIAE ESFGAVRTVR SFAKESYMVS QYSKKVDETL KLGLKQAVLV
GLFFGGLNAA FTLSVITVVS YGAYLTIYGS MTVGALTSFI LYSLTVGSSV SSLSSLYTTA
MKAAGASRRV FQILDRVSSM SSSGDKCPVG NPDGDVELND VWFAYPSRPS HMILKGISLR
LTPGSKVALV GPSGGGKTTI ANLIERFYDP LKGKILLNGV SLMEISHQYL HKQISIVSQE
PILFNCSVEE NIAYGFDGEA SFTDIENAAK MANAHEFIEA FPDKYNTVVG ERGLRLSGGQ
KQRIAIARAL LTNPSVLLLD EATSALDAES EYLVQDAMDS LMAGRTVLVI AHRLSTVKTA
DCVAVISDGE VAEKGTHDEL LSLNGIYTNL VKRQLQSSSS VTTL
