GPT1_ARATH
ID GPT1_ARATH Reviewed; 388 AA.
AC Q9M5A9; Q0WW77; Q8LCH1; Q9FFU8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glucose-6-phosphate/phosphate translocator 1, chloroplastic {ECO:0000303|PubMed:15722468};
DE Short=AtGPT1 {ECO:0000303|PubMed:15722468};
DE Flags: Precursor;
GN Name=GPT1 {ECO:0000303|PubMed:15722468};
GN OrderedLocusNames=At5g54800 {ECO:0000312|Araport:AT5G54800};
GN ORFNames=MBG8.6 {ECO:0000312|EMBL:BAB08759.1};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15722468; DOI=10.1105/tpc.104.029124;
RA Niewiadomski P., Knappe S., Geimer S., Fischer K., Schulz B., Unte U.S.,
RA Rosso M.G., Ache P., Fluegge U.-I., Schneider A.;
RT "The Arabidopsis plastidic glucose 6-phosphate/phosphate translocator GPT1
RT is essential for pollen maturation and embryo sac development.";
RL Plant Cell 17:760-775(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=12084821; DOI=10.1105/tpc.000877;
RA Ruuska S.A., Girke T., Benning C., Ohlrogge J.B.;
RT "Contrapuntal networks of gene expression during Arabidopsis seed
RT filling.";
RL Plant Cell 14:1191-1206(2002).
RN [8]
RP FUNCTION.
RX PubMed=20659277; DOI=10.1111/j.1365-313x.2010.04313.x;
RA Andriotis V.M., Pike M.J., Bunnewell S., Hills M.J., Smith A.M.;
RT "The plastidial glucose-6-phosphate/phosphate antiporter GPT1 is essential
RT for morphogenesis in Arabidopsis embryos.";
RL Plant J. 64:128-139(2010).
RN [9]
RP GENE FAMILY.
RX PubMed=25053812; DOI=10.1073/pnas.1406073111;
RA Rautengarten C., Ebert B., Moreno I., Temple H., Herter T., Link B.,
RA Donas-Cofre D., Moreno A., Saez-Aguayo S., Blanco F., Mortimer J.C.,
RA Schultink A., Reiter W.D., Dupree P., Pauly M., Heazlewood J.L.,
RA Scheller H.V., Orellana A.;
RT "The Golgi localized bifunctional UDP-rhamnose/UDP-galactose transporter
RT family of Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11563-11568(2014).
RN [10]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-27 AND
RP CYS-65.
RX PubMed=32111666; DOI=10.1105/tpc.19.00959;
RA Baune M.C., Lansing H., Fischer K., Meyer T., Charton L., Linka N.,
RA von Schaewen A.;
RT "The Arabidopsis plastidial glucose-6-phosphate transporter GPT1 is dually
RT targeted to peroxisomes via the endoplasmic reticulum.";
RL Plant Cell 32:1703-1726(2020).
CC -!- FUNCTION: Glucose 6-phosphate (Glc6P) transporter (PubMed:15722468).
CC Transports also inorganic phosphate, 3-phosphoglycerate, triose
CC phosphates and, to a leser extent, phosphoenolpyruvate
CC (PubMed:15722468). Responsible for the transport of Glc6P into plastids
CC of heterotrophic tissues where it can be used as a carbon source for
CC starch biosynthesis, as substrate for fatty acid biosynthesis or as
CC substrate for NADPH generation via the oxidative pentose phosphate
CC pathway (OPPP) (PubMed:15722468). Required for pollen maturation and
CC embryo sac development (PubMed:15722468, PubMed:20659277).
CC Preferentially exchanges Glc6P for ribulose-5-phosphate (Ru5P) in
CC reconstituted yeast proteoliposomes (PubMed:32111666). May supply the
CC substrate (Glc6P) for OPPP reactions inside peroxisomes and exchange it
CC with the product Ru5P which leaves the organelle (PubMed:32111666).
CC {ECO:0000269|PubMed:15722468, ECO:0000269|PubMed:20659277,
CC ECO:0000269|PubMed:32111666}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:32111666}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:32111666}; Multi-pass membrane protein
CC {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:32111666};
CC Multi-pass membrane protein {ECO:0000255}. Note=Targeted to peroxisomes
CC via the endoplasmic reticulum. {ECO:0000269|PubMed:32111666}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds, flowers, rosette leaves, and
CC roots, with highest levels found in stamens. Found in the root cap, in
CC guard cells and in mesophyll cells. {ECO:0000269|PubMed:15722468}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the transient accumulation of
CC starch in the developing seeds. Decline rapidly 8 days after flowering.
CC Not detected in mature seeds. {ECO:0000269|PubMed:12084821,
CC ECO:0000269|PubMed:15722468}.
CC -!- DISRUPTION PHENOTYPE: Gametophytic lethal phenotype in homozygous
CC plants. {ECO:0000269|PubMed:15722468}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. GPT (TC 2.A.7.9)
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08759.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF233658; AAF42936.1; -; mRNA.
DR EMBL; AB005232; BAB08759.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96542.1; -; Genomic_DNA.
DR EMBL; AY057679; AAL15310.1; -; mRNA.
DR EMBL; BT002212; AAN72224.1; -; mRNA.
DR EMBL; AK226479; BAE98621.1; -; mRNA.
DR EMBL; AY086600; AAM63660.1; -; mRNA.
DR RefSeq; NP_568812.1; NM_124861.5.
DR AlphaFoldDB; Q9M5A9; -.
DR SMR; Q9M5A9; -.
DR BioGRID; 20814; 18.
DR IntAct; Q9M5A9; 17.
DR STRING; 3702.AT5G54800.1; -.
DR SwissPalm; Q9M5A9; -.
DR PaxDb; Q9M5A9; -.
DR PRIDE; Q9M5A9; -.
DR ProteomicsDB; 220700; -.
DR EnsemblPlants; AT5G54800.1; AT5G54800.1; AT5G54800.
DR GeneID; 835570; -.
DR Gramene; AT5G54800.1; AT5G54800.1; AT5G54800.
DR KEGG; ath:AT5G54800; -.
DR Araport; AT5G54800; -.
DR TAIR; locus:2160175; AT5G54800.
DR eggNOG; KOG1441; Eukaryota.
DR HOGENOM; CLU_019048_0_1_1; -.
DR InParanoid; Q9M5A9; -.
DR OMA; VIQCNAY; -.
DR OrthoDB; 1453018at2759; -.
DR PhylomeDB; Q9M5A9; -.
DR PRO; PR:Q9M5A9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M5A9; baseline and differential.
DR Genevisible; Q9M5A9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0015152; F:glucose-6-phosphate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015120; F:phosphoglycerate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0071917; F:triose-phosphate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IDA:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IMP:TAIR.
DR GO; GO:0015714; P:phosphoenolpyruvate transport; IDA:UniProtKB.
DR GO; GO:0015713; P:phosphoglycerate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0010152; P:pollen maturation; IMP:TAIR.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR GO; GO:0035436; P:triose phosphate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0007033; P:vacuole organization; IMP:TAIR.
DR InterPro; IPR004853; Sugar_P_trans_dom.
DR InterPro; IPR004696; Tpt_PEP_transl.
DR Pfam; PF03151; TPT; 1.
DR TIGRFAMs; TIGR00817; tpt; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Endoplasmic reticulum; Membrane; Peroxisome; Plastid;
KW Reference proteome; Sugar transport; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 66..388
FT /note="Glucose-6-phosphate/phosphate translocator 1,
FT chloroplastic"
FT /id="PRO_0000035711"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 112..229
FT /note="EamA"
FT MUTAGEN 27
FT /note="S->A,D: No effect on targeting to endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:32111666"
FT MUTAGEN 65
FT /note="C->S: No effect on targeting to endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:32111666"
FT CONFLICT 57
FT /note="R -> K (in Ref. 6; AAM63660)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="I -> N (in Ref. 6; AAM63660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 42329 MW; 996C07330D9DCB43 CRC64;
MVLSVKQTLS PKIGLFRRNP SSSLGRSPVS LSFPSTELPK RTVLAVSKPL HLSSSLRAKS
PVVRCEAYEA DRSEPHPIGD DAAAAETKSE AAKKLKIGIY FATWWALNVV FNIYNKKVLN
AYPYPWLTST LSLAAGSLMM LISWAVGIVE TPKTDFDFWK TLFPVAVAHT IGHVAATVSM
SKVAVSFTHI IKSGEPAFSV LVSRFILGET FPTSVYLSLI PIIGGCALSA LTELNFNMIG
FMGAMISNLA FVFRNIFSKK GMKGKSVSGM NYYACLSMLS LLILTPFAIA VEGPQMWVDG
WQTALATVGP QFVWWVVAQS VFYHLYNQVS YMSLDQISPL TFSVGNTMKR ISVIVSSIII
FRTPVQPVNA LGAAIAILGT FLYSQAKL
