AB29G_ARATH
ID AB29G_ARATH Reviewed; 1416 AA.
AC Q94A18; O04323;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ABC transporter G family member 29;
DE Short=ABC transporter ABCG.29;
DE Short=AtABCG29;
DE AltName: Full=Pleiotropic drug resistance protein 1;
GN Name=ABCG29; Synonyms=PDR1; OrderedLocusNames=At3g16340;
GN ORFNames=MYA6.14, T02O04.17;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
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 [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: May be a general defense protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94A18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94A18-2; Sequence=VSP_018391;
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems, and, to a lower
CC extent, in seedling and inflorescence. {ECO:0000269|PubMed:12430018}.
CC -!- INDUCTION: Repressed by cold/dark treatment.
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}.
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DR EMBL; AB023046; BAB01273.1; -; Genomic_DNA.
DR EMBL; AC001645; AAB63643.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75799.1; -; Genomic_DNA.
DR EMBL; AY050448; AAK91463.1; -; mRNA.
DR EMBL; BK001001; DAA00870.1; -; Genomic_DNA.
DR RefSeq; NP_566543.1; NM_112505.4. [Q94A18-1]
DR AlphaFoldDB; Q94A18; -.
DR SMR; Q94A18; -.
DR BioGRID; 6215; 1.
DR STRING; 3702.AT3G16340.1; -.
DR TCDB; 3.A.1.205.18; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q94A18; -.
DR PaxDb; Q94A18; -.
DR PRIDE; Q94A18; -.
DR ProteomicsDB; 244492; -. [Q94A18-1]
DR EnsemblPlants; AT3G16340.1; AT3G16340.1; AT3G16340. [Q94A18-1]
DR GeneID; 820881; -.
DR Gramene; AT3G16340.1; AT3G16340.1; AT3G16340. [Q94A18-1]
DR KEGG; ath:AT3G16340; -.
DR Araport; AT3G16340; -.
DR TAIR; locus:2094952; AT3G16340.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_6_1; -.
DR InParanoid; Q94A18; -.
DR OMA; LVFNKHS; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; Q94A18; -.
DR PRO; PR:Q94A18; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94A18; baseline and differential.
DR Genevisible; Q94A18; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0015850; P:organic hydroxy compound transport; IDA:TAIR.
DR GO; GO:1901140; P:p-coumaryl alcohol transport; IDA:TAIR.
DR GO; GO:1901141; P:regulation of lignin biosynthetic process; IMP:TAIR.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
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; IPR034001; ABCG_PDR_1.
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 Alternative splicing; ATP-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1416
FT /note="ABC transporter G family member 29"
FT /id="PRO_0000234628"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1160..1180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1198..1218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1246..1266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1273..1293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1303..1323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1331..1351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1385..1405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 147..420
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 498..711
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 814..1067
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1139..1353
FT /note="ABC transmembrane type-2 2"
FT BINDING 180..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 859..866
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT VAR_SEQ 1..1004
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_018391"
FT CONFLICT 1197
FT /note="M -> K (in Ref. 4; AAK91463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1416 AA; 160298 MW; 4EC185458B4CCD3B CRC64;
METLSRSLSK SLGELLASNS NNHFSRRSGS TIDDHDEEAL KWAALEKLPT FARLRTTIIH
PHEDLVDVTK LGVDDRQKFI DSIFKVTEED NEKFLKKFRN RIDRVRIKLP TVEVRFEKVT
IEANCHIGKR ALPTLPNAAL NIAERGLRLL GFNFTKTTKV TILRDVSGII KPSRMTLLLG
PPSSGKTTLL LALAGKLDQS LKVTGRVTYN GHGLEEFVPQ KTSAYISQND VHVGVMTVQE
TLDFSARCQG VGTRYDLLSE LVRREKDAGI LPEPEVDLFM KSIAAGNVKS SLITDYTLRI
LGLDICKDTV VGDEMIRGIS GGQKKRVTTG EMIVGPTKTL FMDEISTGLD SSTTYQIVKC
LQEIVRFTDA TVLMSLLQPA PETFELFDDI ILLSEGQIVY QGPRDHVLTF FETCGFKCPD
RKGTADFLQE VTSRKDQEQY WADSKKPYSY ISVSEFSKRF RTFHVGANLE KDLSVPYDRF
KSHPASLVFK KHSVPKSQLF KVCWDRELLL MKRNAFFYIT KTVQIIIMAL IASTVYLRTE
MGTKNESDGA VYIGALMFSM IVNMFNGFAE LALMIQRLPV FYKQRDLLFH PPWTFSLPTF
LLGIPISIFE SVVWVTITYY MIGFAPELSR FLKHLLVIFL TQQMAGGIFR FIAATCRSMI
LANTGGALVI LLLFLLGGFI VPRGEIPKWW KWAYWVSPMA YTYDALTVNE MLAPRWINQP
SSDNSTSLGL AVLEIFDIFT DPNWYWIGVG GILGFTVLFN ILVTLALTFL NPLEKQQAVV
SKENTEENRA ENGSKSKSID VKRGMVLPFT PLTMSFDNVN YYVDMPKEMK EQGVSKDKLQ
LLKEVTGVFR PGVLTALMGV SGAGKTTLMD VLAGRKTGGY IEGDIRISGF PKRQETFARI
SGYCEQNDIH SPQVTVKESL IYSAFLRLPK EVTKYEKMRF VDEVMELVEL ESLKDAVVGL
PGITGLSTEQ RKRLTIAVEL VANPSIIFMD EPTSGLDARA AAIVMRTVRN TVDTGRTVVC
TIHQPSIDIF EAFDELLLLK RGGQVIYAGP LGQNSHKIIE YFQAIHGVPK IKEKYNPATW
MLEVSSMAAE AKLEIDFAEH YKTSSLYQQN KNLVKELSTP PQGASDLYFS TRFSQSLLGQ
FKSCLWKQWI TYWRTPDYNL ARFFFTLAAA VMLGSIFWKV GTKRENANDL TKVIGAMYAA
VLFVGVNNSS SVQPLIAVER SVFYRERAAE MYSALPYALA QVVCEIPYVL IQTTYYTLII
YAMMCFEWTL AKFFWFYFVS FMSFLYFTYY GMMTVALTPN QQVAAVFAGA FYGLFNLFSG
FVIPRPRIPK WWIWYYWICP VAWTVYGLIV SQYGDVEDTI KVPGMANDPT IKWYIENHYG
YDADFMIPIA TVLVGFTLFF AFMFAFGIRT LNFQQR
