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DTX34_ARATH
ID   DTX34_ARATH             Reviewed;         542 AA.
AC   F4JH46; O23067; Q84W63;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Protein DETOXIFICATION 34 {ECO:0000303|PubMed:11739388};
DE            Short=AtDTX34 {ECO:0000303|PubMed:11739388};
DE   AltName: Full=Multidrug and toxic compound extrusion protein 34 {ECO:0000305};
DE            Short=MATE protein 34 {ECO:0000305};
GN   Name=DTX34 {ECO:0000303|PubMed:11739388};
GN   OrderedLocusNames=At4g00350 {ECO:0000312|Araport:AT4G00350};
GN   ORFNames=A_IG005I10.20 {ECO:0000312|EMBL:AAB62839.1},
GN   F5I10.20 {ECO:0000312|EMBL:AAF02797.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [5]
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   [6]
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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4JH46-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4JH46-2; Sequence=VSP_057896;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC       2.A.66.1) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB62839.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g00350 has been split into 2 genes: At4g00350 and At4g00355.; Evidence={ECO:0000305};
CC       Sequence=AAF02797.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g00350 has been split into 2 genes: At4g00350 and At4g00355.; Evidence={ECO:0000305};
CC       Sequence=CAB80793.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g00350 has been split into 2 genes: At4g00350 and At4g00355.; Evidence={ECO:0000305};
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DR   EMBL; AF013293; AAB62839.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF195115; AAF02797.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161471; CAB80793.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE81864.1; -; Genomic_DNA.
DR   EMBL; BT004194; AAO42212.1; -; mRNA.
DR   EMBL; BX826625; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T01536; T01536.
DR   RefSeq; NP_567173.3; NM_116258.4. [F4JH46-1]
DR   AlphaFoldDB; F4JH46; -.
DR   SMR; F4JH46; -.
DR   IntAct; F4JH46; 24.
DR   STRING; 3702.AT4G00350.1; -.
DR   PaxDb; F4JH46; -.
DR   PRIDE; F4JH46; -.
DR   ProteomicsDB; 220714; -. [F4JH46-1]
DR   EnsemblPlants; AT4G00350.1; AT4G00350.1; AT4G00350. [F4JH46-1]
DR   GeneID; 827306; -.
DR   Gramene; AT4G00350.1; AT4G00350.1; AT4G00350. [F4JH46-1]
DR   KEGG; ath:AT4G00350; -.
DR   Araport; AT4G00350; -.
DR   TAIR; locus:2126036; AT4G00350.
DR   eggNOG; KOG1347; Eukaryota.
DR   HOGENOM; CLU_012893_1_4_1; -.
DR   InParanoid; F4JH46; -.
DR   OMA; AILMYMV; -.
DR   OrthoDB; 743037at2759; -.
DR   PRO; PR:F4JH46; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JH46; baseline and differential.
DR   Genevisible; F4JH46; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR   CDD; cd13132; MATE_eukaryotic; 1.
DR   InterPro; IPR045069; MATE_euk.
DR   InterPro; IPR002528; MATE_fam.
DR   Pfam; PF01554; MatE; 2.
DR   TIGRFAMs; TIGR00797; matE; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..542
FT                   /note="Protein DETOXIFICATION 34"
FT                   /id="PRO_0000434075"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        435..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         111..138
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057896"
FT   CONFLICT        385
FT                   /note="A -> V (in Ref. 3; AAO42212)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   542 AA;  59045 MW;  9FBD1E5855C6427A CRC64;
     MEIPVREERR SSSSSAGPLQ QTISLAADDA IDSGPSSPLV VKVSVFETEH ETTKLIHAPS
     TLLGETTGDA DFPPIQSFRD AKLVCVVETS KLWEIAAPIA FNILCNYGVN SFTSIFVGHI
     GDLELSAVAI ALSVVSNFSF GFLLGMASAL ETLCGQAFGA GQMDMLGVYM QRSWLILLGT
     SVCLLPLYIY ATPLLILLGQ EPEIAEISGK FTTQIIPQMF ALAINFPTQK FLQSQSKVGI
     MAWIGFFALT LHIFILYLFI NVFKWGLNGA AAAFDVSAWG IAIAQVVYVV GWCKDGWKGL
     SWLAFQDVWP FLKLSFASAV MLCLEIWYFM TIIVLTGHLE DPVIAVGSLS ICMNINGWEG
     MLFIGINAAI SVRVSNELGS GHPRAAKYSV IVTVIESLVI GVVCAIVILI TRDDFAVIFT
     ESEEMRKAVA DLAYLLGITM ILNSLQPVIS GVAVGGGWQA PVAYINLFCY YAFGLPLGFL
     LGYKTSLGVQ GIWIGMICGT SLQTLILLYM IYITNWNKEV EQASERMKQW GAGYEKLEKI
     AT
 
 
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