GDU2_ARATH
ID GDU2_ARATH Reviewed; 129 AA.
AC Q9SW07; Q8LCT0;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protein GLUTAMINE DUMPER 2;
GN Name=GDU2; OrderedLocusNames=At4g25760; ORFNames=F14M19.40;
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [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, 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 [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.
CC {ECO:0000269|PubMed:20018597, ECO:0000269|Ref.8}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|Ref.8}; Single-pass
CC membrane protein {ECO:0000269|Ref.8}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues.
CC {ECO:0000269|PubMed:20018597, ECO:0000269|Ref.8}.
CC -!- DOMAIN: The VIMAG motif is necessary for the function of the protein.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Overexpression of GLUTAMINE DUMPER 2 leads to free amino
CC acid levels accumulation and plant size decrease (Ref.8,
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; AL049480; CAB39597.1; -; Genomic_DNA.
DR EMBL; AL161563; CAB81386.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85110.1; -; Genomic_DNA.
DR EMBL; BX828970; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY086421; AAM63423.1; -; mRNA.
DR PIR; T04230; T04230.
DR RefSeq; NP_567728.1; NM_118708.2.
DR AlphaFoldDB; Q9SW07; -.
DR SMR; Q9SW07; -.
DR BioGRID; 13968; 43.
DR IntAct; Q9SW07; 6.
DR MINT; Q9SW07; -.
DR STRING; 3702.AT4G25760.1; -.
DR PaxDb; Q9SW07; -.
DR PRIDE; Q9SW07; -.
DR EnsemblPlants; AT4G25760.1; AT4G25760.1; AT4G25760.
DR GeneID; 828681; -.
DR Gramene; AT4G25760.1; AT4G25760.1; AT4G25760.
DR KEGG; ath:AT4G25760; -.
DR Araport; AT4G25760; -.
DR TAIR; locus:2117517; AT4G25760.
DR eggNOG; ENOG502S1CH; Eukaryota.
DR HOGENOM; CLU_112624_2_2_1; -.
DR InParanoid; Q9SW07; -.
DR OMA; EGRQYNY; -.
DR OrthoDB; 1520115at2759; -.
DR PRO; PR:Q9SW07; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SW07; baseline and differential.
DR Genevisible; Q9SW07; 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..129
FT /note="Protein GLUTAMINE DUMPER 2"
FT /id="PRO_0000419940"
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..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 66..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 94..98
FT /note="VIMAG"
FT CONFLICT 100
FT /note="V -> I (in Ref. 4; AAM63423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 129 AA; 14223 MW; A7355B3280DDFF38 CRC64;
MQTMEGRQYN YQDSINASSS MVVPHSPWHS PVPYLFGGLA AMLALICVAL LILACSYWRL
SGSAERDLEA GDDAKPDNDT NKTKHTEMPE KFLVIMAGDV RPTYLATPAT RSEQSCTCGD
HNEEEGRRG
