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Database: UniProt
Entry: O24367
LinkDB: O24367
Original site: O24367 
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-OCT-2014, entry version 79.
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; 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. {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
CC       acid (ABA) is repressed by cytokinin such as kinetin (at protein
CC       level). {ECO:0000269|PubMed:12061897, ECO:0000269|PubMed:8702621}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
CC       family. PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 ABC transmembrane type-2 domains.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00434}.
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DR   EMBL; Z70524; CAA94437.1; -; mRNA.
DR   ProteinModelPortal; O24367; -.
DR   TCDB; 3.A.1.205.20; the atp-binding cassette (abc) superfamily.
DR   PRIDE; O24367; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
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.
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; 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;
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. {ECO:0000255}.
FT   TRANSMEM    559    579       Helical. {ECO:0000255}.
FT   TRANSMEM    614    634       Helical. {ECO:0000255}.
FT   TRANSMEM    646    666       Helical. {ECO:0000255}.
FT   TRANSMEM    671    691       Helical. {ECO:0000255}.
FT   TRANSMEM    756    776       Helical. {ECO:0000255}.
FT   TRANSMEM   1187   1207       Helical. {ECO:0000255}.
FT   TRANSMEM   1215   1235       Helical. {ECO:0000255}.
FT   TRANSMEM   1275   1295       Helical. {ECO:0000255}.
FT   TRANSMEM   1302   1322       Helical. {ECO:0000255}.
FT   TRANSMEM   1332   1352       Helical. {ECO:0000255}.
FT   TRANSMEM   1363   1383       Helical. {ECO:0000255}.
FT   TRANSMEM   1413   1433       Helical. {ECO:0000255}.
FT   DOMAIN      158    430       ABC transporter 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   DOMAIN      508    721       ABC transmembrane type-2 1.
FT   DOMAIN      843   1095       ABC transporter 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   DOMAIN     1168   1382       ABC transmembrane type-2 2.
FT   NP_BIND     191    198       ATP 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   NP_BIND     888    895       ATP 2. {ECO:0000255|PROSITE-
FT                                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
//
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