PDR1_NICPL
ID PDR1_NICPL Reviewed; 1436 AA.
AC Q949G3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Pleiotropic drug resistance protein 1;
DE AltName: Full=NpPDR1;
GN Name=PDR1; Synonyms=ABC1;
OS Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex 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=4092;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 473-478 AND 1046-1052,
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11340184; DOI=10.2307/3871366;
RA Jasinski M., Stukkens Y., Degand H., Purnelle B., Marchand-Brynaert J.,
RA Boutry M.;
RT "A plant plasma membrane ATP binding cassette-type transporter is involved
RT in antifungal terpenoid secretion.";
RL Plant Cell 13:1095-1107(2001).
RN [2]
RP INDUCTION.
RX PubMed=12848828; DOI=10.1046/j.1365-313x.2003.01792.x;
RA Grec S., Vanham D., de Ribaucourt J.C., Purnelle B., Boutry M.;
RT "Identification of regulatory sequence elements within the transcription
RT promoter region of NpABC1, a gene encoding a plant ABC transporter induced
RT by diterpenes.";
RL Plant J. 35:237-250(2003).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16126865; DOI=10.1104/pp.105.062372;
RA Stukkens Y., Bultreys A., Grec S., Trombik T., Vanham D., Boutry M.;
RT "NpPDR1, a pleiotropic drug resistance-type ATP-binding cassette
RT transporter from Nicotiana plumbaginifolia, plays a major role in plant
RT pathogen defense.";
RL Plant Physiol. 139:341-352(2005).
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).
CC -!- FUNCTION: Excretes secondary metabolites such as terpenes. Involved in
CC both constitutive and jasmonic acid-dependent induced defense. Confers
CC some resistance to sclareol and B.cinerea.
CC {ECO:0000269|PubMed:11340184, ECO:0000269|PubMed:16126865}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11340184};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11340184}.
CC -!- TISSUE SPECIFICITY: Roots, petals and leaf epidermis, where it is
CC confined to glandular trichomes (at protein level).
CC {ECO:0000269|PubMed:11340184, ECO:0000269|PubMed:16126865}.
CC -!- INDUCTION: By terpenes such as sclareolide and sclareol, and by some
CC phytohormones such as jasmonic acid (JA) and ethylene. Strongly induced
CC by compatible pathogens such as the fungus B.cinerea, and the bacteria
CC P.syringae pv tabaci, as well as by non pathogenic bacteria such as
CC P.fluorescens, and P.marginalis pv marginalis. Weak induction by
CC incompatible pathogens such as P.syringae pv syringae (at protein
CC level). {ECO:0000269|PubMed:11340184, ECO:0000269|PubMed:12848828,
CC ECO:0000269|PubMed:16126865}.
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; AJ404328; CAC40990.1; -; mRNA.
DR AlphaFoldDB; Q949G3; -.
DR SMR; Q949G3; -.
DR TCDB; 3.A.1.205.21; the atp-binding cassette (abc) superfamily.
DR PRIDE; Q949G3; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Direct protein sequencing; Membrane;
KW Nucleotide-binding; Plant defense; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1436
FT /note="Pleiotropic drug resistance protein 1"
FT /id="PRO_0000234653"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 764..784
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1184..1204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1214..1234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1270..1290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1301..1321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1327..1347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1358..1378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1408..1428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 165..438
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 516..729
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 838..1090
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1163..1377
FT /note="ABC transmembrane type-2 2"
FT REGION 796..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 883..890
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1436 AA; 161849 MW; 0337AB7941B2EC03 CRC64;
MEPADLSNLR GRSLRASIRG SMRGSIRENS NSIWRNNGAE VFSRSARDED DEEALKWAAL
EKLPTYDRLR KGILFGSQGA AAEVDVDDSG VLERKNLLER LVKVADEDNE KFLLKLKNRI
DRVGIDFPSI EVRFEHLNID ADAYVGSRAL PTFTNFISNF VEGLLDSIHI LPSKKRQVTI
LKDVSGIVKP CRMTLLLGPP GSGKTTLLLA LAGKLDSALK VTGKVTYNGH ELHEFVPQRT
AAYISQHDLH IGEMTVRETL EFSARCQGVG SRYEMLAELS RREKAANIKP DADIDMFMKA
ASTEGQEAKV VTDYILKILG LDICADTMVG DQMIRGISGG QKKRVTTGEM IVGPSKALFM
DEISTGLDSS TTYSIVNSLK QSVRIMKGTA LISLLQPAPE TYNLFDDIIL LSDGYIVYEG
PREEVLEFFE SMGFKCPERK GAADFLQEVT SKKDQQQYWI RRDEPYRFIT SKEFAEAYQS
FHVGRKVSDE LKTTFDKSKS HPAALTTQKY GIGKRQLLKV CTERELLLMQ RNSFVYLFKF
FQLLIIALMT MTIFFRTKMP RDSAEDGGIY SGALFFVVIM IMFNGLSELP MTLYKLPVFY
KQRDFLFYPS WAYAIPSWIL KIPVTFAEVG MWVFLTYYVM GFDPNVGRFF KQFLLLLLVN
QMASALFRFI AAVGRTMGVA STFGAFALLL QFALGGFILA RNDVKDWWIW GYWTSPLMYS
VNAILVNEFD GQKWKHIVAG GTEPLGAAVV RARGFFPDAY WYWIGVGALA GFIVMFNIAY
SVALAYLNPF DKPQATISDE SENNESESSP QITSTQEGDS ASENKKKGMV LPFDPHSITF
DEVVYSVDMP PEMRESGTSD NRLVLLKSVS GAFRPGVLTA LMGVSGAGKT TLMDVLAGRK
TGGYIDGSIK ISGYPKKQDT FARISGYCEQ NDIHSPYVTV FESLVYSAWL RLPQDVNEEK
RMMFVEEVMD LVELTPLRSA LVGLPGVNGL STEQRKRLTI AVELVANPSI IFMDEPTSGL
DARAAAIVMR AVRNTVDTGR TVVCTIHQPS IDIFEAFDEL FLMKRGGQEI YVGPLGRQSC
HLIKYFESIP GVSKIVEGYN PATWMLEVTA SSQEMALGVD FTDLYKKSDL YRRNKALIDE
LSVPRPGTSD LHFDSEFSQP FWTQCMACLW KQHWSYWRNP AYTAVRLIFT TFIALIFGTM
FWDIGTKVSR NQDLVNAMGS MYAAVLFLGV QNSSSVQPVV SVERTVFYRE KAAGMYSAIP
YAFAQVLIEI PYIFVQATVY GLIVYSMIGF EWTVAKFFWD FFFMFFTFLY FTFFGMMTVA
VTPNQNVASI VAGFFYTVWN LFSGFIVPRP RIPIWWRWYY WGCPIAWTLY GLVASQFGDL
QDPLTDQNQT VEQFLRSNFG FKHDFLGVVA AVIVAFAVVF AFTFALGIKA FNFQRR
