PDR1_PETHY
ID PDR1_PETHY Reviewed; 1452 AA.
AC H6WS94;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Pleiotropic drug resistance protein 1 {ECO:0000303|PubMed:22398443};
DE AltName: Full=ABC transporter G family PDR1 {ECO:0000305};
DE AltName: Full=Strigolactone transporter {ECO:0000305};
GN Name=PDR1 {ECO:0000303|PubMed:22398443};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. W115;
RX PubMed=22398443; DOI=10.1038/nature10873;
RA Kretzschmar T., Kohlen W., Sasse J., Borghi L., Schlegel M.,
RA Bachelier J.B., Reinhardt D., Bours R., Bouwmeester H.J., Martinoia E.;
RT "A petunia ABC protein controls strigolactone-dependent symbiotic
RT signalling and branching.";
RL Nature 483:341-344(2012).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25683808; DOI=10.1016/j.cub.2015.01.015;
RA Sasse J., Simon S., Guebeli C., Liu G.W., Cheng X., Friml J.,
RA Bouwmeester H., Martinoia E., Borghi L.;
RT "Asymmetric localizations of the ABC transporter PaPDR1 trace paths of
RT directional strigolactone transport.";
RL Curr. Biol. 25:647-655(2015).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27040840; DOI=10.1007/s00425-016-2503-9;
RA Borghi L., Liu G.W., Emonet A., Kretzschmar T., Martinoia E.;
RT "The importance of strigolactone transport regulation for symbiotic
RT signaling and shoot branching.";
RL Planta 243:1351-1360(2016).
CC -!- FUNCTION: Cellular strigolactone (SL) transporter required for the
CC exudation of SL from the root to the soil (PubMed:22398443,
CC PubMed:25683808, PubMed:27040840). The presence of SL in the vicinity
CC of the roots is required for development of symbiotic interactions with
CC arbuscular mycorrhizal fungi (AMF) (PubMed:22398443, PubMed:27040840).
CC Transports SL in the above ground tissues and is required for the
CC control of shoot branching (PubMed:22398443, PubMed:27040840). SL
CC regulates plant shoot architecture by inhibiting the outgrowth of
CC axillary buds (PubMed:22398443, PubMed:27040840). Involved in the
CC regulation of shootward and outward directional strigolactone transport
CC in roots (PubMed:25683808). Due to its polar localization in root
CC cells, mediates directional shootward strigolactone transport, as well
CC as localized outward directional transport for exudation to the soil
CC (PubMed:25683808). {ECO:0000269|PubMed:22398443,
CC ECO:0000269|PubMed:25683808, ECO:0000269|PubMed:27040840}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22398443,
CC ECO:0000269|PubMed:25683808, ECO:0000269|PubMed:27040840}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane
CC (PubMed:22398443, PubMed:25683808, PubMed:27040840). Exhibits
CC asymmetric localization in different root tissues (PubMed:25683808). In
CC root tips, localizes at the apical membrane of hypodermal cells
CC (PubMed:25683808). In the hypodermal passage cells localizes in the
CC outer-lateral membrane (PubMed:25683808). {ECO:0000269|PubMed:22398443,
CC ECO:0000269|PubMed:25683808, ECO:0000269|PubMed:27040840}.
CC -!- TISSUE SPECIFICITY: Expressed in root hypodermal passage cells
CC (PubMed:22398443, PubMed:25683808). Expressed in stem tissues,
CC particularly the vasculature and nodes adjacent to leaf axils
CC (PubMed:22398443). {ECO:0000269|PubMed:22398443,
CC ECO:0000269|PubMed:25683808}.
CC -!- INDUCTION: Induced in roots by auxin, phosphate starvation, treatment
CC with the synthetic strigolactone analog GR24, and colonization by the
CC arbuscular mycorrhizal fungus Glomus intraradices.
CC {ECO:0000269|PubMed:22398443}.
CC -!- DISRUPTION PHENOTYPE: Enhanced branching phenotype (PubMed:22398443).
CC Defective in strigolactone exudation from roots, and reduced symbiotic
CC interactions with arbuscular mycorrhizal fungi (AMF) (PubMed:22398443).
CC {ECO:0000269|PubMed:22398443}.
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; JQ292813; AFA43816.1; -; mRNA.
DR AlphaFoldDB; H6WS94; -.
DR SMR; H6WS94; -.
DR TCDB; 3.A.1.205.17; the atp-binding cassette (abc) superfamily.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009914; P:hormone transport; IMP:UniProtKB.
DR GO; GO:2000032; P:regulation of secondary shoot formation; IMP:UniProtKB.
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; 1.
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; Cell membrane; Membrane; Nucleotide-binding; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1452
FT /note="Pleiotropic drug resistance protein 1"
FT /id="PRO_0000447562"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1199..1219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1239..1259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1287..1307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1314..1334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1344..1364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1375..1395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1421..1441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 152..425
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 504..716
FT /note="ABC transmembrane type-2 1"
FT /evidence="ECO:0000255"
FT DOMAIN 855..1107
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1180..1394
FT /note="ABC transmembrane type-2 2"
FT /evidence="ECO:0000255"
FT REGION 808..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 900..907
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1452 AA; 164698 MW; 878360A66E7FB70E CRC64;
MEGGEELFRV SSARLSSSNV WRNSAMDVFS RSSREADDEE ALKWAALEKL PTYLRIRRGI
LTEEEGQSRE VDITKLDLVE RRNLLERLIK ITDEDNEKFL LKLKERIDRV GLDLPTIEVR
FEHLSVDAEA RVGSRALPTV FNFTVNILED FLNYLHILPN RKQPLPILHD VSGIIKPGRM
TLLLGPPSSG KTTLLLALAG KLDKDLKVSG RVTYNGHDMN EFVAQRSSAY ISQYDLHIGE
MTVRETLAFS ARCQGVGAKY EILAELSRRE KEANIKPDPD VDIFMKAAWN EGQEANVVTD
YTLKILGLEI CADTIVGDEM VRGISGGQRK RLTTGEMMVG PARALFMDEI STGLDSSTTY
QIVNSIRQSI HILQGTAVIS LLQPAPETYD LFDDIILLSD GQIVYQGPRE NVLEFFEYMG
FICPERKGVA DFLQEVTSRK DQEQYWARRE ESYKFITVRE FSEAFQAFHI GRKLGDELAV
PFDKSKSHPA ALTTKRYGVS KKELLKACTA REYLLMKRNS FVYIFKMIQL TLMASITMTL
FLPTEMHRNT TIDGAVFLGA LFYALIMIMF NGFSELALSI MKLPSFYKHR DLLFFPPWAY
ALPTWILKIP ITLVEVAIWV CMTYYVIGFE ADVGRFFKQL LLLICVNQMA SGLFRLMGAL
GRNIIVANTF GSFVLLTVLV MGGFVLSRDD VKKWWIWGYW ISPMMYAQNA IAVNEFLGKS
WAHVPPNSTS TETLGVSFLK SRGIFPDARW YWIGAGALIG YVFLFNFLFA VALAYLNPFG
KPQAVLSEET VAERNASKRG EVIELSSLGK SSSEKGNDVR RSASSRSMSS RVGSITAADL
SKRRGMILPF EPLSITFDDI RYAVDMPQEM KAQGFTEDRL ELLRGVSGAF RPGVLTALMG
VSGAGKTTLM DVLAGRKTGG YIDGTISISG YPKQQETFAR IAGYCEQTDI HSPHVTVYES
LQFSAWLRLP REVDTATRKM FIEEVMELIE LIPLRDALVG LPGVNGLSTE QRKRLTVAVE
LVANPSIIFM DEPTSGLDAR AAAIVMRTVR NTVDTGRTVV CTIHQPSIDI FDAFDELLLL
KRGGEEIYVG PLGRQSSHLI KYFEGIDGVP KIKDGYNPAT WMLEITSVAQ EGALGNDFTE
LYKNSELYRR NKALIKELSV PASCSKDLYF PTKYSQSFFT QCMACFWKQH WSYWRNPPYT
AVRIMFTFFI ALMFGTIFWD LGSRRERQQD LLNAIGSMYI AVLFLGVQNA TTVQPVIAIE
RTVFYRERAA GMYSAMPYAF GQVMIELPYL FLQTIIYGVI VYAMIGFEWT VAKFFWYLFF
MYFTLLYFTL YGMMTVAVTP NQSIAAIISS AFYAVWNLFC GFIVPKTRMP VWWRWYYYIC
PISWTLYGLI ASQFGDIQDR LDTNETVEQF IENFFDFKHD FVGYVALILV GISVLFLFIF
AFSIKTFNFQ KR
