AB34G_ARATH
ID AB34G_ARATH Reviewed; 1453 AA.
AC Q7PC87; Q56YS3; Q9SJR6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ABC transporter G family member 34;
DE Short=ABC transporter ABCG.34;
DE Short=AtABCG34;
DE AltName: Full=Pleiotropic drug resistance protein 6;
GN Name=ABCG34; Synonyms=PDR6; OrderedLocusNames=At2g36380; ORFNames=F1O11.1;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1173-1453.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12430018; DOI=10.1007/s00425-002-0889-z;
RA van den Brule S., Smart C.C.;
RT "The plant PDR family of ABC transporters.";
RL Planta 216:95-106(2002).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16506311; DOI=10.1016/j.febslet.2005.12.043;
RA Crouzet J., Trombik T., Fraysse A.S., Boutry M.;
RT "Organization and function of the plant pleiotropic drug resistance ABC
RT transporter family.";
RL FEBS Lett. 580:1123-1130(2006).
RN [6]
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: May be a general defense protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots at low levels.
CC {ECO:0000269|PubMed:12430018}.
CC -!- INDUCTION: Induced by cold/dark treatment, 2,4-D, epibrassinolide
CC (EBR), sodium chloride (NaCl) and cadmium (Cd).
CC {ECO:0000269|PubMed:12430018}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24623.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15320.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD93879.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006919; AAD24623.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006921; AAM15320.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09246.1; -; Genomic_DNA.
DR EMBL; AK221248; BAD93879.1; ALT_INIT; mRNA.
DR EMBL; BK001005; DAA00874.1; -; Genomic_DNA.
DR PIR; A84780; A84780.
DR RefSeq; NP_181179.2; NM_129195.6.
DR AlphaFoldDB; Q7PC87; -.
DR SMR; Q7PC87; -.
DR BioGRID; 3555; 3.
DR STRING; 3702.AT2G36380.1; -.
DR TCDB; 3.A.1.205.23; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q7PC87; -.
DR PaxDb; Q7PC87; -.
DR PRIDE; Q7PC87; -.
DR ProteomicsDB; 244512; -.
DR EnsemblPlants; AT2G36380.1; AT2G36380.1; AT2G36380.
DR GeneID; 818211; -.
DR Gramene; AT2G36380.1; AT2G36380.1; AT2G36380.
DR KEGG; ath:AT2G36380; -.
DR Araport; AT2G36380; -.
DR TAIR; locus:2044893; AT2G36380.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_6_1; -.
DR InParanoid; Q7PC87; -.
DR OMA; SIFHWQD; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; Q7PC87; -.
DR PRO; PR:Q7PC87; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q7PC87; baseline and differential.
DR Genevisible; Q7PC87; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013581; PDR_assoc.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF08370; PDR_assoc; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1453
FT /note="ABC transporter G family member 34"
FT /id="PRO_0000234633"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1196..1216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1230..1250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1289..1309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1311..1331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1341..1361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1366..1386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1422..1442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 173..446
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 524..737
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 852..1105
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1177..1391
FT /note="ABC transmembrane type-2 2"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 897..904
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1453 AA; 164206 MW; 5545559518DC1F76 CRC64;
MLGRDEDLVR TMSGRGSLGS TSHRSLAGAA SKSFRDVFAP PTDDVFGRSD RREEDDVELR
WAALERLPTY DRLRKGMLPQ TMVNGKIGLE DVDVTNLAPK EKKHLMEMIL KFVEEDNEKF
LRRLRERTDR VGIEVPKIEV RYENLSVEGD VRSASRALPT LFNVTLNTIE SILGLFHLLP
SKKRKIEILK DISGIIKPSR MTLLLGPPSS GKTTLLQALA GKLDDTLQMS GRITYCGHEF
REFVPQKTCA YISQHDLHFG EMTVRESLDF SGRCLGVGTR YQLLTELSRR EREAGIKPDP
EIDAFMKSIA ISGQETSLVT DYVLKLLGLD ICADTLVGDV MRRGISGGQR KRLTTGEMLV
GPATALFMDE ISTGLDSSTT FQICKFMRQL VHIADVTMVI SLLQPAPETF ELFDDIILLS
EGQIVYQGSR DNVLEFFEYM GFKCPERKGI ADFLQEVTSK KDQEQYWNRR EHPYSYVSVH
DFSSGFNSFH AGQQLASEFR VPYDKAKTHP AALVTQKYGI SNKDLFKACF DREWLLMKRN
SFVYVFKTVQ ITIMSLIAMT VYFRTEMHVG TVQDGQKFYG ALFFSLINLM FNGMAELAFT
VMRLPVFFKQ RDFLFYPPWA FALPGFLLKI PLSLIESVIW IALTYYTIGF APSAARFFRQ
LLAYFCVNQM ALSLFRFLGA LGRTEVIANS GGTLALLVVF VLGGFIISKD DIPSWLTWCY
YTSPMMYGQT ALVINEFLDE RWGSPNNDTR INAKTVGEVL LKSRGFFTEP YWFWICIGAL
LGFTVLFNFC YIIALMYLNP LGNSKATTVV EEGKDKHKGS HSGTGGSVVE LTSTSSHGPK
KGMVLPFQPL SLAFNNVNYY VDMPAEMKAQ GVEGDRLQLL RDVGGAFRPG VLTALVGVSG
AGKTTLMDVL AGRKTGGYVE GSINISGYPK NQATFARVSG YCEQNDIHSP HVTVYESLIY
SAWLRLSADI DTKTREMFVE EVMELVELKP LRNSIVGLPG VDGLSTEQRK RLTIAVELVA
NPSIIFMDEP TSGLDARAAA IVMRTVRNTV DTGRTVVCTI HQPSIDIFES FDELLLMKRG
GQVIYAGTLG HHSQKLVEYF EAIEGVPKIK DGYNPATWML DVTTPSMESQ MSVDFAQIFV
NSSVNRRNQE LIKELSTPPP GSNDLYFRTK YAQPFSTQTK ACFWKMYWSN WRYPQYNAIR
FLMTVVIGVL FGLLFWQTGT KIEKEQDLNN FFGAMYAAVL FLGATNAATV QPAVAIERTV
FYREKAAGMY SAIPYAISQV AVEIMYNTIQ TGVYTLILYS MIGYDWTVVK FFWFYYYMLT
CFVYFTLYGM MLVALTPNYQ IAGICLSFFL SFWNLFSGFL IPRPQIPIWW RWYYWASPVA
WTLYGIITSQ VGDRDSIVHI TGVGDMSLKT LLKNGFGFDY DFLPVVAVVH IAWILIFLFA
FAYGIKFLNF QRR
