AB35G_ARATH
ID AB35G_ARATH Reviewed; 1442 AA.
AC Q7PC86; Q9XI48;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=ABC transporter G family member 35;
DE Short=ABC transporter ABCG.35;
DE Short=AtABCG35;
DE AltName: Full=Pleiotropic drug resistance protein 7;
GN Name=ABCG35; Synonyms=PDR7; OrderedLocusNames=At1g15210; ORFNames=F9L1.15;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [4]
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 [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 -!- 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: Ubiquitous with higher levels in roots.
CC {ECO:0000269|PubMed:12430018}.
CC -!- INDUCTION: Induced by cycloheximide (CHX) and 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39650.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007591; AAD39650.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29285.1; -; Genomic_DNA.
DR EMBL; BK001006; DAA00875.1; -; Genomic_DNA.
DR PIR; B86286; B86286.
DR RefSeq; NP_172973.1; NM_101389.3.
DR AlphaFoldDB; Q7PC86; -.
DR SMR; Q7PC86; -.
DR BioGRID; 23327; 4.
DR STRING; 3702.AT1G15210.1; -.
DR iPTMnet; Q7PC86; -.
DR PaxDb; Q7PC86; -.
DR PRIDE; Q7PC86; -.
DR ProteomicsDB; 243271; -.
DR EnsemblPlants; AT1G15210.1; AT1G15210.1; AT1G15210.
DR GeneID; 838087; -.
DR Gramene; AT1G15210.1; AT1G15210.1; AT1G15210.
DR KEGG; ath:AT1G15210; -.
DR Araport; AT1G15210; -.
DR TAIR; locus:2037703; AT1G15210.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q7PC86; -.
DR OMA; YFPVGYF; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; Q7PC86; -.
DR PRO; PR:Q7PC86; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7PC86; baseline and differential.
DR Genevisible; Q7PC86; 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 GO; GO:0003729; F:mRNA binding; IDA: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; 3.
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..1442
FT /note="ABC transporter G family member 35"
FT /id="PRO_0000234634"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1186..1206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1218..1238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1272..1292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1299..1319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1329..1349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1357..1377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1414..1434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 169..442
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 520..733
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 840..1092
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1165..1379
FT /note="ABC transmembrane type-2 2"
FT BINDING 202..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 885..892
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1442 AA; 162570 MW; 1C6686FB567E3F57 CRC64;
MDYDPAHAMS RGGSMRQTIS RSVSKASRNM EDIFNTSSRR TKSVNEDEEA LKWASIEKLP
TYNRLRTSLM PELGEDDVYG NQILNKAVDV TKLDGEERQK FIDMVFKVAE QDNERILTKL
RNRIDRVGIQ LPTVEVRYDH LTVKADCYTG DRSLPSLLNA VRNMGEAALG MIGIRLAKKA
QLTILKDVSG IVKPSRMTLL LGPPSSGKTT LLLALAGKLD KSLDVSGEVT YNGYRLNEFV
PIKTSAYISQ NDLHVGIMTV KETLDFSARC QGVGTRYDLL NELARREKDA GIFPEADVDL
FMKASAAQGV KSSLITDYTL KILGLDICKD TIVGDDMMRG ISGGQKKRVT TGEMIVGPTK
TLFMDEISTG LDSSTTFQIV KCLQQIVHLT EATVLISLLQ PAPETFDLFD DIILLSEGQI
VYQGPRDHIL EFFESFGFKC PERKGTADFL QEVTSKKDQE QYWVDPNRPY RYIPVSEFAS
SFKKFHVGSK LSNELSVPYD KSKSHKAALM FDKYSIKKTE LLKSCWDKEW MLMKRNSFFY
VFKTVQIIII AAITSTLYLR TEMHTRNEID ANIYVGSLLF AMIVNMFNGL AEMAMTIQRL
PVFYKQRDLL FHPPWTYTLP TFLLGIPISI FESTAWMVVT YYSIGYAPDA ERFFKQFLII
FLIQQMAAGI FRFIASTCRT MTIANTGGVL VLLVVFLTGG FLLPRSEIPV WWRWAYWISP
LSYAFNAITV NELFAPRWMN KMSGNSTTRL GTSVLNIWDV FDDKNWYWIG VGGLLGFTVI
FNGFFTLALT YLDPLGKAQA ILPKEEDEEA KGKAGSNKET EMESVSAKKG MVLPFTPLAM
SFDDVKYFVD MPAEMREQGV QETRLQLLKG VTSAFRPGVL TALMGVSGAG KTTLMDVLAG
RKTGGYIEGD VRVSGFPKKQ ETFARISGYC EQTDIHSPQV TVRESLIFSA FLRLAKEVSK
EDKLMFVDQV MELVELVDLR DAIVGLPGVT GLSTEQRKRL TIAVELVANP SIIFMDEPTS
GLDARAAAIV MRAVRNTVDT GRTVVCTIHQ PSIDIFEAFD ELLLMKRGGH VIYSGPLGRN
SHKVVEYFES FPGVPKIPEK YNPATWMLEA SSLAAELKLG VDFAELYKAS ALCQRNKALV
QELSVPPQGA TDLYFATQFS QNTWGQFKSC LWKQWWTYWR SPDYNLVRFI FTLATSLMIG
SVFWQIGGKR SNVQDLTMVI GAIYAAVVFV GINNCSTVQP MVAVERTVFY REKAAGMYSA
IPYAISQVTC ELPYVLIQTT YYSLIIYSMV GFEWKASKFL WFIFINYFSF LYWTYYGMMT
VSLTPNQQVA SIFASAFYGI FNLFSGFFIP RPKIPKWWVW YYWICPVAWT IYGLITSQYG
DVETPIALLG GAPGLTVKQY IKDQYGFESD YMGPVAGVLV GFTVFFAFIF AFCIKTLNFQ
SR
