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GDU7_ARATH
ID   GDU7_ARATH              Reviewed;          97 AA.
AC   Q3E8L0; A0MFK2;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Protein GLUTAMINE DUMPER 7;
GN   Name=GDU7; OrderedLocusNames=At5g38770; ORFNames=MKD10.70;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
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 GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
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, even in the
CC       minor veins of the leaves. {ECO:0000269|PubMed:20018597,
CC       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 7 leads to free amino
CC       acid levels accumulation (Ref.6, PubMed:20018597).
CC   -!- SIMILARITY: Belongs to the GLUTAMINE DUMPER 1 (TC 9.B.60) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK28285.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB011478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED94358.1; -; Genomic_DNA.
DR   EMBL; DQ447014; ABE65568.1; -; Genomic_DNA.
DR   EMBL; DQ653328; ABK28285.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_198693.1; NM_123238.2.
DR   AlphaFoldDB; Q3E8L0; -.
DR   BioGRID; 19119; 2.
DR   IntAct; Q3E8L0; 3.
DR   MINT; Q3E8L0; -.
DR   PaxDb; Q3E8L0; -.
DR   PRIDE; Q3E8L0; -.
DR   EnsemblPlants; AT5G38770.1; AT5G38770.1; AT5G38770.
DR   GeneID; 833868; -.
DR   Gramene; AT5G38770.1; AT5G38770.1; AT5G38770.
DR   KEGG; ath:AT5G38770; -.
DR   Araport; AT5G38770; -.
DR   TAIR; locus:2166635; AT5G38770.
DR   HOGENOM; CLU_112624_3_0_1; -.
DR   OMA; MAYACYH; -.
DR   OrthoDB; 1624437at2759; -.
DR   PhylomeDB; Q3E8L0; -.
DR   PRO; PR:Q3E8L0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q3E8L0; baseline and differential.
DR   Genevisible; Q3E8L0; 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..97
FT                   /note="Protein GLUTAMINE DUMPER 7"
FT                   /id="PRO_0000419945"
FT   TOPO_DOM        1..25
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           78..82
FT                   /note="VIMAG"
SQ   SEQUENCE   97 AA;  10819 MW;  F9BC331DF150103B CRC64;
     MSLHRDSMVP VNSRLENMDS PILSKICAWG VMLGLFALSL FAMAYACYHK QTSNSCIEEK
     QGKKQVLKPL DMEPKIVVIM AGNENPTFFA KPTQINA
 
 
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