TUR2_SPIPO
ID TUR2_SPIPO Reviewed; 1441 AA.
AC O24367;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pleiotropic drug resistance protein TUR2;
DE Short=Protein Turion 2;
GN Name=TUR2;
OS Spirodela polyrhiza (Giant duckweed) (Lemna polyrhiza).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Lemnoideae; Spirodela.
OX NCBI_TaxID=29656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=8702621; DOI=10.1074/jbc.271.32.19351;
RA Smart C.C., Fleming A.J.;
RT "Hormonal and environmental regulation of a plant PDR5-like ABC
RT transporter.";
RL J. Biol. Chem. 271:19351-19357(1996).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=12061897; DOI=10.1046/j.1365-313x.2002.01321.x;
RA van den Brule S., Mueller A., Fleming A.J., Smart C.C.;
RT "The ABC transporter SpTUR2 confers resistance to the antifungal diterpene
RT sclareol.";
RL Plant J. 30:649-662(2002).
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 (By similarity). Seems
CC involved in turion (dormant buds) formation. Confers resistance to the
CC diterpenoid antifungal agent sclareol. {ECO:0000250,
CC ECO:0000269|PubMed:12061897, ECO:0000269|PubMed:8702621}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12061897};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12061897}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8702621}.
CC -!- INDUCTION: Induced by abiotic stresses such as cold-stress,
CC cycloheximide and sodium chloride (NaCl). Induction by abscisic acid
CC (ABA) is repressed by cytokinin such as kinetin (at protein level).
CC {ECO:0000269|PubMed:12061897, ECO:0000269|PubMed:8702621}.
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; Z70524; CAA94437.1; -; mRNA.
DR AlphaFoldDB; O24367; -.
DR SMR; O24367; -.
DR TCDB; 3.A.1.205.20; 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; 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; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Plant defense;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1441
FT /note="Pleiotropic drug resistance protein TUR2"
FT /id="PRO_0000234657"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1187..1207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1215..1235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1275..1295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1302..1322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1332..1352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1363..1383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1413..1433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 158..430
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 508..721
FT /note="ABC transmembrane type-2 1"
FT DOMAIN 843..1095
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1168..1382
FT /note="ABC transmembrane type-2 2"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 888..895
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1441 AA; 162698 MW; 62D6A8DE0923EB76 CRC64;
MEIAGYRGGS LRGSLQGSLR RSVSAWRSPS TSDVFGRSSR EEDDEEALKW AALEKLPTYD
RLRKGIMTGD GGEIQEVDIQ GLGFQERKNL LEKLVRNAEE DNERFLLKLR NRMERVGIDN
PTIEVRFEHL NINAEAFVGN RGVPTLVNFF VNKAIWILSA LHLMPSGKRP ISILHDVSGI
IKPCRMTLLL GPPGAGKTTL LLALAGKLDN TLKVTGNVTY NGHGMHEFVP QRTSAYISQH
DVHIGEMTVR ETLAFSSRCQ GVGTRYEMLT ELSRREKEAN IKPDPDVDVY MKAVAVEGQE
SVVTDYILKI LGLDICADTM VGDGMIRGIS GGQKKRVTTG EMLVGPSKAL FMDEISTGLD
SSTTFQIVNS LRQSVHILGG TALIALLQPA PETYDLFDDI LLLSDGQIVY QGPRENVLEF
FESMGFKCPE RKGVADFLQE VTSRKDQQQY WVRENEPYRF VPVNEFSEAF KSFHVGAKLH
EELSTPFDRS RNHPAALTTS KYGISKMELL KACIDREWLL MKRNSFVYIF KVVQLIVLAL
IAMTVFFRTK LPRNGLEDAT IFFGAMFLGL VTHLFNGFAE LAMSIAKLPV FYKQRDLLFY
PPWAYALPTW ILKIPISFVE CGVWIAMTYY VIGFDPNVVR MFRHYLLLVL ISQVASGLFR
LLAAVGRDMV VADTFGAFAQ LVLLVLGGFI IAREKIKKFW IWGYWSSPLM YAQNAIAVNE
FLGHSWNKLV DATGQTLGER FLRNRGIFVD KNWYWIGVGA LIGYMVLFNF LFILFLEWLD
PLGKGQTTVS EEALQEKEAN RTGANVELAT RGSAATSDGG SVEIRKDGNR KKGMVLPFTP
LSITFDNVKY SVDMPQEMKD RGVTEDKLLL LKGVSGAFRP GVLTALMGVS GRGKTTLMDV
LAGRKTGGYI EGDIRISGYP KNQETFARIS GYCEQNDIHS PHVTVYESLL YSAWLRLPAE
VDEKQRKMFV DEVMDLVELN SLRGSLVGLP GVTGLSTEQR KRLTIAVELV ANPSIIFMDE
PTSGLDARAA AIVMRAVRNT VDTGRTVVCT IHQPSIDIFE AFDELFLMKR GGEEIYVGPL
GRQSSHLIKY FESIDGVKKI KERYNPATWM LEVTTISQEE ILGLNFAEVY RNSDLYKRNK
DLIKELSTPP PGSKDLFFAT QFSQSFVMQC LACLWKQHKS YWRNPSYTAT RLFFTVVIAL
IFGTIFWDLG KKRSTSLDLI NAMGSMYAAV LFIGIQNAQT VQPIVDVERT VFYREKAAGM
YSALPYAYAQ VLIEVPHILV QTLLYGLLVY SMIGFDWTAA KFLWYMFFMF FTFLYFTYYG
MMAVAMTPNS DIAAIVAAAF YAIWNIFAGF IIPRPRIPIW WRWYYWACPV AWTLYGLVVS
QFGEYTDTMS DVDETVKDFL RRFLGFRHDF LPVVGVMVVV FTVLFASIFA FSIKTLNFQR
R
