GDU4_ARATH
ID GDU4_ARATH Reviewed; 156 AA.
AC Q8S8A0;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Protein GLUTAMINE DUMPER 4;
GN Name=GDU4; OrderedLocusNames=At2g24762; ORFNames=F27A10.11;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) 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 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.
CC {ECO:0000269|PubMed:20018597, ECO:0000269|Ref.7}.
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, even in the
CC minor veins of the leaves. {ECO:0000269|PubMed:20018597,
CC ECO:0000269|Ref.7}.
CC -!- DOMAIN: The VIMAG motif is necessary for the function of the protein.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Overexpression of GLUTAMINE DUMPER 4 leads to free amino
CC acid levels accumulation (Ref.7, PubMed:20018597).
CC -!- SIMILARITY: Belongs to the GLUTAMINE DUMPER 1 (TC 9.B.60) family.
CC {ECO:0000305}.
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DR EMBL; AC007266; AAM15477.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07624.1; -; Genomic_DNA.
DR EMBL; BT024696; ABD57521.1; -; mRNA.
DR RefSeq; NP_565577.1; NM_128035.5.
DR AlphaFoldDB; Q8S8A0; -.
DR SMR; Q8S8A0; -.
DR BioGRID; 2365; 21.
DR IntAct; Q8S8A0; 22.
DR MINT; Q8S8A0; -.
DR STRING; 3702.AT2G24762.1; -.
DR PaxDb; Q8S8A0; -.
DR PRIDE; Q8S8A0; -.
DR ProteomicsDB; 247126; -.
DR EnsemblPlants; AT2G24762.1; AT2G24762.1; AT2G24762.
DR GeneID; 817013; -.
DR Gramene; AT2G24762.1; AT2G24762.1; AT2G24762.
DR KEGG; ath:AT2G24762; -.
DR Araport; AT2G24762; -.
DR TAIR; locus:505006270; AT2G24762.
DR eggNOG; ENOG502S4AK; Eukaryota.
DR HOGENOM; CLU_112624_2_1_1; -.
DR InParanoid; Q8S8A0; -.
DR OMA; PPISPWH; -.
DR OrthoDB; 1520115at2759; -.
DR PhylomeDB; Q8S8A0; -.
DR PRO; PR:Q8S8A0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8A0; baseline and differential.
DR Genevisible; Q8S8A0; AT.
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:0080143; P:regulation of amino acid export; IMP:TAIR.
DR InterPro; IPR040359; GDU.
DR PANTHER; PTHR33228; PTHR33228; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..156
FT /note="Protein GLUTAMINE DUMPER 4"
FT /id="PRO_0000419942"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 67..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 99..103
FT /note="VIMAG"
FT COMPBIAS 70..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 156 AA; 16851 MW; 413DFCC110E4885F CRC64;
MRPLSIKPTS LDVARHATSV ESFGNHRPPI SPWHSPVPYL FGGLAAMLGL IAFALLILAC
SYWRLSTSGD DSGERVDEEK ESRSGVKAAS AACEEKVLVI MAGDDLPRFL ATPAANKCMC
GHEGRMVIFK EDGIGAGEEK MGDREKAKEN EETTSQ
