PDR1_TOBAC
ID PDR1_TOBAC Reviewed; 1434 AA.
AC Q76CU2; Q8LP45;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Pleiotropic drug resistance protein 1;
DE AltName: Full=NtPDR1;
GN Name=PDR1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RC STRAIN=cv. Bright Yellow 2;
RX PubMed=11997039; DOI=10.1016/s0014-5793(02)02697-2;
RA Sasabe M., Toyoda K., Shiraishi T., Inagaki Y., Ichinose Y.;
RT "cDNA cloning and characterization of tobacco ABC transporter: NtPDR1 is a
RT novel elicitor-responsive gene.";
RL FEBS Lett. 518:164-168(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Bright Yellow 2;
RX PubMed=14973342; DOI=10.1266/ggs.78.409;
RA Schenke D., Sasabe M., Toyoda K., Inagaki Y., Shiraishi T., Ichinose Y.;
RT "Genomic structure of the NtPDR1 gene, harboring the two miniature
RT inverted-repeat transposable elements, NtToya1 and NtStowaway101.";
RL Genes Genet. Syst. 78:409-418(2003).
RN [3]
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).
CC -!- FUNCTION: May be a general defense protein.
CC {ECO:0000269|PubMed:11997039}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: By the phytohormone methyl jasmonate (MeJA), defense
CC elicitors (INF1 elicitin of P.infestans, flagellin of P.syringae and
CC yeast extract), and protein phosphatase inhibitor (cantharidin).
CC Repressed by protein kinase inhibitor (K252a) and cycloheximide.
CC {ECO:0000269|PubMed:11997039}.
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; AB075550; BAB92011.1; -; mRNA.
DR EMBL; AB109388; BAD07483.1; -; Genomic_DNA.
DR RefSeq; NP_001312599.1; NM_001325670.1.
DR RefSeq; XP_016478140.1; XM_016622654.1.
DR AlphaFoldDB; Q76CU2; -.
DR SMR; Q76CU2; -.
DR GeneID; 107799533; -.
DR KEGG; nta:107799533; -.
DR OMA; NGARRCE; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; Q76CU2; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1434
FT /note="Pleiotropic drug resistance protein 1"
FT /id="PRO_0000234655"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1181..1201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1221..1241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1269..1289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1296..1316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1326..1346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1357..1377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1406..1426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 161..434
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 512..725
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 837..1089
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1162..1376
FT /note="ABC transmembrane type-2 2"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 882..889
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 810
FT /note="T -> P (in Ref. 1; BAB92011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1434 AA; 161683 MW; 041F2DCDD4D3239A CRC64;
MEPANLSNLR GSSLRGSTRG SLRANSNSIW RNNGVEIFSR SSRDEDDEEA LKWAALEKLP
TFDRLRKGLL FGSQGAAAEV DINDLGFQER KNLLERLVKV ADEDNEKFLL KLKNRIDRVG
IDLPTIEVRY EHLNIDADAY VGSRSLPTFM NFMTNFVETL LNSLHILSSR KRQLTILKDI
SGIIKPCRMT LLLGPPSSGK TTLLLALAGK LDPALKVTGK VSYNGHELHE FVPQRTAAYI
SQHDLHIGEM TVRETLEFSA RCQGVGSRFE MLAELSRREK AANIKPDADI DIYMKAAATE
GQEANVVTDY VLKILGLDIC ADTMVGDDMI RGISGGQKKR VTTGEMLVGP SKALFMDEIS
TGLDSSTTYS IVNSLRQSVQ ILKGTAVISL LQPAPETYNL FDDIILLSDG YIVYQGPRDD
VLEFFESMGF KCPQRKGVAD FLQEVTSKKD QQQYWSKRNE PYRFITSKEF AEAYQSFHVG
RKLGDELATP FDKTKCHPAA LTNEKYGIGK KELLKVCTER ELLLMKRNSF VYMFKFSQLT
IMALITMTLF FRTEMPRDTT DDGGIYAGAL FFVVIMIMFN GMSELAMTIF KLPVFYKQRD
LLFFPSWAYA IPSWILKIPV TLVEVGLWVI LTYYVIGFDP NITRFLKQFL LLIVVNQMAS
GMFRFIGAVG RTMGVASTFG SFALLLQFAL GGFVLSRDDV KSWWIWGYWI SPMMYSVNSI
LVNEFDGKKW NHIVPGGNET LGSTVVKSRG FFPEAYWYWI GVGALVGFTV VFNFCYSLAL
AYLNPFDKPQ AVLPEDGENA ENGEVSSQIT STDGGDSISE SQNNKKGMVL PFEPHSITFD
DVVYSVDMPQ EMKEQGAGED RLVLLKGVSG AFRPGVLTAL MGVSGAGKTT LMDVLAGRKT
GGYIDGEIKI SGYPKKQETF ARISGYCEQN DIHSPYVTVY ESLVYSAWLR LPQDVDEKTR
KMFVDEVMEL VELGPLRSAL VGLPGVNGLS TEQRKRLTIA VELVANPSII FMDEPTSGLD
ARAAAIVMRT VRNTVDTGRT VVCTIHQPSI DIFEAFDELF LMKRGGQEIY VGPLGRHSCH
LIKYFESNPG VAKIKEGYNP ATWMLEVTAS AQEMMLGIDF TEVYKNSDLY RRNKALISEL
GVPRPGSKDL HFETQYSQSF WTQCVACLWK QHWSYWRNPA YTAVRFIFTT FIALIFGTMF
WDLGTKVSKS QDLLNAMGSM YAAVLFLGVQ NASSVQPVVA IERTVFYRER AAGMYSAIPY
AFGQVSIEIP YIFVQSVFYG IIVYAMIGFE WDVGKFFWYL FIMFFTLLYF TFYGMMGVAV
TPNQNVASIV AAFFYGVWNL FSGFIIPRPR MPVWWRWYYW ANPVAWTLYG LVASQFGDIQ
TKLSDNETVE QFLRRYFGFK HDFLGVVAAV LTAYVFMFAF TFAFAIKAFN FQRR
