GDU3_ARATH
ID GDU3_ARATH Reviewed; 148 AA.
AC Q9FHH5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein GLUTAMINE DUMPER 3;
DE AltName: Full=Protein LESS SUSCEPTIBLE TO BSCTV 1;
DE Short=Protein LBS1;
GN Name=GDU3; Synonyms=LBS1; OrderedLocusNames=At5g57685; ORFNames=MRI1.4;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
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 [5]
RP GENE FAMILY.
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 [6]
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 [7]
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 [8]
RP FUNCTION, AND INDUCTION BY GEMINIVIRUS.
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 [9]
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).
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. Acts upstream genes
CC involved in the salicylic acid (SA) pathway and in the geminivirus-host
CC interaction. {ECO:0000269|PubMed:20018597, ECO:0000269|PubMed:20042021,
CC ECO:0000269|Ref.7}.
CC -!- INTERACTION:
CC Q9FHH5; Q9LSZ5: MQM1.2; NbExp=3; IntAct=EBI-6290786, EBI-25521735;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|Ref.7}; Single-pass
CC membrane protein {ECO:0000269|Ref.7}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues. Also detected in
CC anthers. {ECO:0000269|PubMed:20018597, ECO:0000269|Ref.7}.
CC -!- INDUCTION: By geminivirus (BSCTV) infection.
CC {ECO:0000269|PubMed:20042021}.
CC -!- DOMAIN: The VIMAG motif is necessary for the function of the protein.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Overexpression of GLUTAMINE DUMPER 3 leads to free amino
CC acid levels accumulation, plant size decrease and to an enhanced
CC resistance to geminivirus infection (Ref.7, PubMed:20042021,
CC PubMed:20018597).
CC -!- SIMILARITY: Belongs to the GLUTAMINE DUMPER 1 (TC 9.B.60) family.
CC {ECO:0000305}.
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DR EMBL; AB018118; BAB09586.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96935.1; -; Genomic_DNA.
DR EMBL; BT012591; AAT06410.1; -; mRNA.
DR EMBL; BT014818; AAT41801.1; -; mRNA.
DR RefSeq; NP_680451.2; NM_148146.5.
DR AlphaFoldDB; Q9FHH5; -.
DR SMR; Q9FHH5; -.
DR BioGRID; 21119; 14.
DR IntAct; Q9FHH5; 14.
DR MINT; Q9FHH5; -.
DR STRING; 3702.AT5G57685.1; -.
DR PaxDb; Q9FHH5; -.
DR PRIDE; Q9FHH5; -.
DR ProteomicsDB; 247125; -.
DR EnsemblPlants; AT5G57685.1; AT5G57685.1; AT5G57685.
DR GeneID; 835875; -.
DR Gramene; AT5G57685.1; AT5G57685.1; AT5G57685.
DR KEGG; ath:AT5G57685; -.
DR Araport; AT5G57685; -.
DR TAIR; locus:504954872; AT5G57685.
DR eggNOG; ENOG502S1CH; Eukaryota.
DR HOGENOM; CLU_112624_2_2_1; -.
DR InParanoid; Q9FHH5; -.
DR OMA; GCSYWRL; -.
DR OrthoDB; 1520115at2759; -.
DR PhylomeDB; Q9FHH5; -.
DR PRO; PR:Q9FHH5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHH5; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host process; IMP:TAIR.
DR GO; GO:0080143; P:regulation of amino acid export; IMP:TAIR.
DR GO; GO:0009615; P:response to virus; IMP:TAIR.
DR GO; GO:0032940; P:secretion by cell; ISS:TAIR.
DR InterPro; IPR040359; GDU.
DR PANTHER; PTHR33228; PTHR33228; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..148
FT /note="Protein GLUTAMINE DUMPER 3"
FT /id="PRO_0000419941"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 99..103
FT /note="VIMAG"
SQ SEQUENCE 148 AA; 16203 MW; E0FF8FD1A16A399F CRC64;
MEGRQYYPPR ENVEGNRTTM GGGPHSPWHS PVPYLFGGLA AMLGLIAFAL LILACSYWRL
SGYLDGEENQ SRERDLEVGD VKPDKTAVKP VALPEKFLVI MAGNVKPTYL ATPSVKTCTC
DDDDDEDDDV EGSDQVVPRS SESNGETH
