GDU1_ARATH
ID GDU1_ARATH Reviewed; 158 AA.
AC O81775; Q0WT07;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein GLUTAMINE DUMPER 1;
GN Name=GDU1; OrderedLocusNames=At4g31730; ORFNames=F28M20.80;
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].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15208395; DOI=10.1105/tpc.021642;
RA Pilot G., Stransky H., Bushey D.F., Pratelli R., Ludewig U., Wingate V.P.,
RA Frommer W.B.;
RT "Overexpression of GLUTAMINE DUMPER1 leads to hypersecretion of glutamine
RT from hydathodes of Arabidopsis leaves.";
RL Plant Cell 16:1827-1840(2004).
RN [6]
RP GENE FAMILY, DOMAIN, FUNCTION, AND MUTAGENESIS OF GLY-100.
RX PubMed=17157837; DOI=10.1016/j.febslet.2006.11.064;
RA Pratelli R., Pilot G.;
RT "The plant-specific VIMAG domain of Glutamine Dumper1 is necessary for the
RT function of the protein in Arabidopsis.";
RL FEBS Lett. 580:6961-6966(2006).
RN [7]
RP ERRATUM OF PUBMED:17157837.
RX DOI=10.1016/j.febslet.2007.02.027;
RA Pratelli R., Pilot G.;
RL FEBS Lett. 581:1248-1249(2007).
RN [8]
RP FUNCTION.
RX PubMed=19704691; DOI=10.4161/psb.2.3.3972;
RA Pratelli R., Pilot G.;
RT "Altered amino acid metabolism in glutamine dumper1 plants.";
RL Plant Signal. Behav. 2:182-184(2007).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RA Pratelli R., Frommer W.B., Pilot G.;
RT "The over-expression of GDU-like genes leads to modification in amino acid
RT content and transport.";
RL (In) Proceedings of the 19th international conference on Arabidopsis
RL research, pp.abstract#10018, Montreal (2008).
RN [10]
RP FUNCTION.
RX PubMed=20042021; DOI=10.1111/j.1365-313x.2009.04120.x;
RA Chen H., Zhang Z., Teng K., Lai J., Zhang Y., Huang Y., Li Y., Liang L.,
RA Wang Y., Chu C., Guo H., Xie Q.;
RT "Up-regulation of LSB1/GDU3 affects geminivirus infection by activating the
RT salicylic acid pathway.";
RL Plant J. 62:12-23(2010).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20018597; DOI=10.1104/pp.109.151746;
RA Pratelli R., Voll L.M., Horst R.J., Frommer W.B., Pilot G.;
RT "Stimulation of nonselective amino acid export by glutamine dumper
RT proteins.";
RL Plant Physiol. 152:762-773(2010).
RN [12]
RP INTERACTION WITH LOG2, FUNCTION, UBIQUITINATION, MUTAGENESIS OF GLY-100,
RP AND SUBCELLULAR LOCATION.
RX PubMed=22291198; DOI=10.1104/pp.111.191965;
RA Pratelli R., Guerra D.D., Yu S., Wogulis M., Kraft E., Frommer W.B.,
RA Callis J., Pilot G.;
RT "The ubiquitin E3 ligase LOSS OF GDU2 is required for GLUTAMINE DUMPER1-
RT induced amino acid secretion in Arabidopsis.";
RL Plant Physiol. 158:1628-1642(2012).
CC -!- FUNCTION: Probable subunit of an amino acid transporter involved in the
CC regulation of the amino acid metabolism. Stimulates amino acid export
CC by activating nonselective amino acid facilitators. Required the
CC interaction with the RING-type E3 ubiquitin-protein ligase LOG2 to
CC fulfill its function. Plays a role in the Gln export at hydathodes, at
CC xylem parenchyma into xylem sap and from mesophyll into leaf apoplasm.
CC Acts upstream genes involved in the salicylic acid (SA) pathway and in
CC the geminivirus-host interaction. {ECO:0000269|PubMed:15208395,
CC ECO:0000269|PubMed:17157837, ECO:0000269|PubMed:19704691,
CC ECO:0000269|PubMed:20018597, ECO:0000269|PubMed:20042021,
CC ECO:0000269|PubMed:22291198, ECO:0000269|Ref.9}.
CC -!- SUBUNIT: Interacts with LOG2. {ECO:0000269|PubMed:22291198}.
CC -!- INTERACTION:
CC O81775; Q9S752: LOG2; NbExp=15; IntAct=EBI-6290661, EBI-6290644;
CC O81775; Q5XIQ4: Mgrn1; Xeno; NbExp=3; IntAct=EBI-6290661, EBI-920669;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15208395,
CC ECO:0000269|PubMed:22291198, ECO:0000269|Ref.9}; Single-pass membrane
CC protein {ECO:0000269|PubMed:15208395, ECO:0000269|PubMed:22291198,
CC ECO:0000269|Ref.9}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues and in
CC hydathodes. Expressed in the phloem and xylem (at the protein level).
CC {ECO:0000269|PubMed:15208395, ECO:0000269|PubMed:20018597,
CC ECO:0000269|Ref.9}.
CC -!- DOMAIN: The VIMAG motif is necessary for the function of the protein.
CC {ECO:0000269|PubMed:17157837}.
CC -!- PTM: Ubiquitinated by LOG2 (in vitro). {ECO:0000269|PubMed:22291198}.
CC -!- MISCELLANEOUS: Overexpression of GLUTAMINE DUMPER 1 leads to free amino
CC acid levels accumulation, plant size decrease, hypersecretion of
CC glutamine from hydathodes and to a full resistance to geminivirus
CC infection (Ref.9, PubMed:15208395, PubMed:20042021, PubMed:20018597).
CC -!- SIMILARITY: Belongs to the GLUTAMINE DUMPER 1 (TC 9.B.60) family.
CC {ECO:0000305}.
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DR EMBL; AL031004; CAA19750.1; -; Genomic_DNA.
DR EMBL; AL161579; CAB79891.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85951.1; -; Genomic_DNA.
DR EMBL; BT011573; AAS46626.1; -; mRNA.
DR EMBL; BT012238; AAS76725.1; -; mRNA.
DR EMBL; AK227758; BAE99741.1; -; mRNA.
DR PIR; T05097; T05097.
DR RefSeq; NP_194901.1; NM_119322.4.
DR AlphaFoldDB; O81775; -.
DR SMR; O81775; -.
DR BioGRID; 14587; 5.
DR IntAct; O81775; 4.
DR MINT; O81775; -.
DR STRING; 3702.AT4G31730.1; -.
DR TCDB; 1.A.41.2.2; the avian reovirus p10 viroporin/glutamine dumper 1 (p10 viroporin/gdu1) family.
DR PaxDb; O81775; -.
DR PRIDE; O81775; -.
DR ProteomicsDB; 247123; -.
DR EnsemblPlants; AT4G31730.1; AT4G31730.1; AT4G31730.
DR GeneID; 829301; -.
DR Gramene; AT4G31730.1; AT4G31730.1; AT4G31730.
DR KEGG; ath:AT4G31730; -.
DR Araport; AT4G31730; -.
DR TAIR; locus:2124894; AT4G31730.
DR eggNOG; ENOG502S4AK; Eukaryota.
DR HOGENOM; CLU_112624_2_1_1; -.
DR InParanoid; O81775; -.
DR OMA; CTCGGHE; -.
DR OrthoDB; 1520115at2759; -.
DR PhylomeDB; O81775; -.
DR PRO; PR:O81775; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81775; baseline and differential.
DR Genevisible; O81775; AT.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010585; P:glutamine secretion; IMP:TAIR.
DR GO; GO:0080143; P:regulation of amino acid export; IMP:UniProtKB.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IMP:UniProtKB.
DR InterPro; IPR040359; GDU.
DR PANTHER; PTHR33228; PTHR33228; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..158
FT /note="Protein GLUTAMINE DUMPER 1"
FT /id="PRO_0000419939"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 65..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..100
FT /note="VIMAG"
FT COMPBIAS 68..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 100
FT /note="G->R: In log1-1; Disrupts the binding with LOG2;
FT Abolishes its function."
FT /evidence="ECO:0000269|PubMed:17157837,
FT ECO:0000269|PubMed:22291198"
FT CONFLICT 49
FT /note="A -> V (in Ref. 4; BAE99741)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="M -> V (in Ref. 4; BAE99741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 17254 MW; 6211B8ABBBA3A695 CRC64;
MRPLSVQSKF EDVATSTSVN HHGVTPQSPW HSPVPYLFGG LAAMLGLIAF ALLILACSYW
RLSSSGEEDG QNVDEEKESR SGDKAANGAY EEKFLVIMAG EDLPRYLATP AMKKCTCGGH
EGKMVISQEE SVAKEEEKMR EGEEEKVKDT GETTTTSH
