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GDU6_ARATH
ID   GDU6_ARATH              Reviewed;         111 AA.
AC   Q3EAV6;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Protein GLUTAMINE DUMPER 6;
GN   Name=GDU6; OrderedLocusNames=At3g30725; ORFNames=T4A2.7;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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.
CC       {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 6 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; AP002066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002686; AEE77654.1; -; Genomic_DNA.
DR   RefSeq; NP_850650.1; NM_180319.2.
DR   AlphaFoldDB; Q3EAV6; -.
DR   SMR; Q3EAV6; -.
DR   BioGRID; 8135; 2.
DR   IntAct; Q3EAV6; 4.
DR   MINT; Q3EAV6; -.
DR   STRING; 3702.AT3G30725.1; -.
DR   PaxDb; Q3EAV6; -.
DR   EnsemblPlants; AT3G30725.1; AT3G30725.1; AT3G30725.
DR   GeneID; 822809; -.
DR   Gramene; AT3G30725.1; AT3G30725.1; AT3G30725.
DR   KEGG; ath:AT3G30725; -.
DR   Araport; AT3G30725; -.
DR   TAIR; locus:1005716497; AT3G30725.
DR   eggNOG; ENOG502S94S; Eukaryota.
DR   HOGENOM; CLU_112624_3_0_1; -.
DR   InParanoid; Q3EAV6; -.
DR   OMA; PTYMAKP; -.
DR   OrthoDB; 1624437at2759; -.
DR   PhylomeDB; Q3EAV6; -.
DR   PRO; PR:Q3EAV6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q3EAV6; 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: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..111
FT                   /note="Protein GLUTAMINE DUMPER 6"
FT                   /id="PRO_0000419944"
FT   TOPO_DOM        1..16
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..111
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          40..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           75..79
FT                   /note="VIMAG; degenerate"
FT   COMPBIAS        48..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   111 AA;  12127 MW;  26C94317CC0A0ABA CRC64;
     MRPTPKVEIW KSPVPYLFGG LFLLVLLIAL ALLSLVCTHQ KPSSSSNNNH MDEEDDVGDK
     DAKPITREYL PKIVVILAGD NKPTCLAVPV VVPPPTSIFR CNCDNVTVIS T
 
 
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