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DTX45_ARATH
ID   DTX45_ARATH             Reviewed;         560 AA.
AC   Q9SVE7;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protein DETOXIFICATION 45, chloroplastic {ECO:0000303|PubMed:11739388};
DE            Short=AtDTX45 {ECO:0000303|PubMed:11739388};
DE   AltName: Full=Multidrug and toxic compound extrusion protein 45 {ECO:0000305};
DE            Short=MATE protein 45 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=DTX45 {ECO:0000303|PubMed:11739388};
GN   OrderedLocusNames=At4g38380 {ECO:0000312|Araport:AT4G38380};
GN   ORFNames=F22I13.150 {ECO:0000312|EMBL:CAB37494.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11739388; DOI=10.1074/jbc.m108777200;
RA   Li L., He Z., Pandey G.K., Tsuchiya T., Luan S.;
RT   "Functional cloning and characterization of a plant efflux carrier for
RT   multidrug and heavy metal detoxification.";
RL   J. Biol. Chem. 277:5360-5368(2002).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=12603313; DOI=10.1046/j.1432-1033.2003.03418.x;
RA   Hvorup R.N., Winnen B., Chang A.B., Jiang Y., Zhou X.F., Saier M.H. Jr.;
RT   "The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) exporter
RT   superfamily.";
RL   Eur. J. Biochem. 270:799-813(2003).
RN   [5]
RP   INDUCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=18826429; DOI=10.1111/j.1365-313x.2008.03696.x;
RA   Liu J., Magalhaes J.V., Shaff J., Kochian L.V.;
RT   "Aluminum-activated citrate and malate transporters from the MATE and ALMT
RT   families function independently to confer Arabidopsis aluminum tolerance.";
RL   Plant J. 57:389-399(2009).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18826429}.
CC   -!- INDUCTION: Not induced by aluminum. {ECO:0000269|PubMed:18826429}.
CC   -!- DISRUPTION PHENOTYPE: No reduction in aluminum tolerance.
CC       {ECO:0000269|PubMed:18826429}.
CC   -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC       2.A.66.1) family. {ECO:0000305}.
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DR   EMBL; AL035539; CAB37494.1; -; Genomic_DNA.
DR   EMBL; AL161593; CAB80503.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86921.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM68079.1; -; Genomic_DNA.
DR   PIR; T05666; T05666.
DR   RefSeq; NP_001329858.1; NM_001342492.1.
DR   RefSeq; NP_195551.5; NM_120000.7.
DR   AlphaFoldDB; Q9SVE7; -.
DR   SMR; Q9SVE7; -.
DR   STRING; 3702.AT4G38380.1; -.
DR   iPTMnet; Q9SVE7; -.
DR   PaxDb; Q9SVE7; -.
DR   PRIDE; Q9SVE7; -.
DR   EnsemblPlants; AT4G38380.1; AT4G38380.1; AT4G38380.
DR   EnsemblPlants; AT4G38380.2; AT4G38380.2; AT4G38380.
DR   GeneID; 829995; -.
DR   Gramene; AT4G38380.1; AT4G38380.1; AT4G38380.
DR   Gramene; AT4G38380.2; AT4G38380.2; AT4G38380.
DR   KEGG; ath:AT4G38380; -.
DR   Araport; AT4G38380; -.
DR   TAIR; locus:2121783; AT4G38380.
DR   eggNOG; KOG1347; Eukaryota.
DR   HOGENOM; CLU_012893_16_2_1; -.
DR   InParanoid; Q9SVE7; -.
DR   OrthoDB; 1474417at2759; -.
DR   PRO; PR:Q9SVE7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SVE7; baseline and differential.
DR   Genevisible; Q9SVE7; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd13136; MATE_DinF_like; 1.
DR   InterPro; IPR044644; DinF-like.
DR   InterPro; IPR002528; MATE_fam.
DR   PANTHER; PTHR42893; PTHR42893; 1.
DR   Pfam; PF01554; MatE; 2.
DR   TIGRFAMs; TIGR00797; matE; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Membrane; Plastid; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..75
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           76..560
FT                   /note="Protein DETOXIFICATION 45, chloroplastic"
FT                   /id="PRO_0000405274"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   560 AA;  59817 MW;  3D2BC468320F3BBE CRC64;
     MESSRVVVGG GLPLANRRNS SFAKPKIQQG TFLPLSRINN VSAPQKCSLH TNPNPMFPFV
     TRRKSQTNPD CGVVKLGEED DSCSSLDKLP EVNGVHTGVA RPVDIKRELV MLSLPAIAGQ
     AIDPLTLLME TAYIGRLGSV ELGSAGVSMA IFNTISKLFN IPLLSVATSF VAEDIAKIAA
     QDLASEDSQS DIPSQGLPER KQLSSVSTAL VLAIGIGIFE ALALSLASGP FLRLMGIQSM
     SEMFIPARQF LVLRALGAPA YVVSLALQGI FRGFKDTKTP VYCLGIGNFL AVFLFPLFIY
     KFRMGVAGAA ISSVISQYTV AILMLILLNK RVILLPPKIG SLKFGDYLKS GGFVLGRTLS
     VLVTMTVATS MAARQGVFAM AAHQICMQVW LAVSLLTDAL ASSGQALIAS SASKRDFEGV
     KEVTTFVLKI GVVTGIALAI VLGMSFSSIA GLFSKDPEVL RIVRKGVLFV AATQPITALA
     FIFDGLHYGM SDFPYAACSM MVVGGISSAF MLYAPAGLGL SGVWVGLSMF MGLRMVAGFS
     RLMWRKGPWW FMHTSDKRLA
 
 
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