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 29-MAY-2013, entry version 71.
DE RecName: Full=Pleiotropic drug resistance protein TUR2;
DE Short=Protein Turion 2;
GN Name=TUR2;
OS Spirodela polyrrhiza (Giant duckweed).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; Liliopsida; Araceae; Lemnoideae;
OC Spirodela.
OX NCBI_TaxID=29656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP 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
RT diterpene 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
RT ABC 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
CC the diterpenoid antifungal agent sclareol.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: Induced by abiotic stresses such as cold-stress,
CC cycloheximide and sodium chloride (NaCl). Induction by abscisic
CC acid (ABA) is repressed by cytokinin such as kinetin (at protein
CC level).
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
CC family. PDR (TC 3.A.1.205) subfamily.
CC -!- SIMILARITY: Contains 2 ABC transmembrane type-2 domains.
CC -!- SIMILARITY: Contains 2 ABC transporter domains.
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DR EMBL; Z70524; CAA94437.1; -; mRNA.
DR ProteinModelPortal; O24367; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013581; PDR_assoc.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF08370; PDR_assoc; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51012; ABC_TM2; FALSE_NEG.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; FALSE_NEG.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Plant defense; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 1441 Pleiotropic drug resistance protein TUR2.
FT /FTId=PRO_0000234657.
FT TRANSMEM 526 546 Helical; (Potential).
FT TRANSMEM 559 579 Helical; (Potential).
FT TRANSMEM 614 634 Helical; (Potential).
FT TRANSMEM 646 666 Helical; (Potential).
FT TRANSMEM 671 691 Helical; (Potential).
FT TRANSMEM 756 776 Helical; (Potential).
FT TRANSMEM 1187 1207 Helical; (Potential).
FT TRANSMEM 1215 1235 Helical; (Potential).
FT TRANSMEM 1275 1295 Helical; (Potential).
FT TRANSMEM 1302 1322 Helical; (Potential).
FT TRANSMEM 1332 1352 Helical; (Potential).
FT TRANSMEM 1363 1383 Helical; (Potential).
FT TRANSMEM 1413 1433 Helical; (Potential).
FT DOMAIN 158 430 ABC transporter 1.
FT DOMAIN 508 721 ABC transmembrane type-2 1.
FT DOMAIN 843 1095 ABC transporter 2.
FT DOMAIN 1168 1382 ABC transmembrane type-2 2.
FT NP_BIND 191 198 ATP 1 (Potential).
FT NP_BIND 888 895 ATP 2 (Potential).
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
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