GDU5_ARATH
ID GDU5_ARATH Reviewed; 131 AA.
AC Q3E965;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Protein GLUTAMINE DUMPER 5;
GN Name=GDU5; OrderedLocusNames=At5g24920; ORFNames=F6A4.130;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 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 [4]
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 [5]
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 [6]
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 [7]
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.6}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|Ref.6}; Single-pass
CC membrane protein {ECO:0000269|Ref.6}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues. Also detected in
CC guard cells. {ECO:0000269|PubMed:20018597, ECO:0000269|Ref.6}.
CC -!- DOMAIN: The VIMAG motif is necessary for the function of the protein.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Overexpression of GLUTAMINE DUMPER 5 leads to free amino
CC acid levels accumulation and plant size decrease (Ref.6,
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; AF069716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93378.1; -; Genomic_DNA.
DR RefSeq; NP_197874.2; NM_122401.3.
DR AlphaFoldDB; Q3E965; -.
DR SMR; Q3E965; -.
DR BioGRID; 17837; 11.
DR IntAct; Q3E965; 11.
DR MINT; Q3E965; -.
DR STRING; 3702.AT5G24920.1; -.
DR PaxDb; Q3E965; -.
DR PRIDE; Q3E965; -.
DR ProteomicsDB; 247127; -.
DR EnsemblPlants; AT5G24920.1; AT5G24920.1; AT5G24920.
DR GeneID; 832562; -.
DR Gramene; AT5G24920.1; AT5G24920.1; AT5G24920.
DR KEGG; ath:AT5G24920; -.
DR Araport; AT5G24920; -.
DR TAIR; locus:2149448; AT5G24920.
DR eggNOG; ENOG502S4AK; Eukaryota.
DR HOGENOM; CLU_112624_2_3_1; -.
DR InParanoid; Q3E965; -.
DR OMA; KICLDCV; -.
DR OrthoDB; 1520115at2759; -.
DR PhylomeDB; Q3E965; -.
DR PRO; PR:Q3E965; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E965; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; ISS:TAIR.
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..131
FT /note="Protein GLUTAMINE DUMPER 5"
FT /id="PRO_0000419943"
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..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 88..92
FT /note="VIMAG"
SQ SEQUENCE 131 AA; 14684 MW; F492ED829E802DE1 CRC64;
MRQFPSIRGN INEKMMTTMV ESQTRSPWRT PVPYLFGGLA AMLGLIAFAL LLLACSYWRL
SRQTEDEEKQ TESGEKVVAK AFEEKILVIM AGQNNPTFLA TPVAAKICLD CVNMEKKEGQ
NGESKVTEEN H