GPT2_ARATH
ID GPT2_ARATH Reviewed; 388 AA.
AC Q94B38; O80688;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Glucose-6-phosphate/phosphate translocator 2, chloroplastic {ECO:0000303|PubMed:15722468};
DE Short=AtGPT2 {ECO:0000303|PubMed:15722468};
DE Flags: Precursor;
GN Name=GPT2 {ECO:0000303|PubMed:15722468};
GN OrderedLocusNames=At1g61800 {ECO:0000312|Araport:AT1G61800};
GN ORFNames=F8K4.1 {ECO:0000312|EMBL:AAC28500.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [4]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, 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 [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=19939944; DOI=10.1104/pp.109.149351;
RA Athanasiou K., Dyson B.C., Webster R.E., Johnson G.N.;
RT "Dynamic acclimation of photosynthesis increases plant fitness in changing
RT environments.";
RL Plant Physiol. 152:366-373(2010).
RN [6]
RP FUNCTION.
RX PubMed=20712627; DOI=10.1111/j.1438-8677.2010.00349.x;
RA Kunz H.H., Haeusler R.E., Fettke J., Herbst K., Niewiadomski P., Gierth M.,
RA Bell K., Steup M., Fluegge U.I., Schneider A.;
RT "The role of plastidial glucose-6-phosphate/phosphate translocators in
RT vegetative tissues of Arabidopsis thaliana mutants impaired in starch
RT biosynthesis.";
RL Plant Biol. 12:115-128(2010).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24489010; DOI=10.1093/aob/mct298;
RA Dyson B.C., Webster R.E., Johnson G.N.;
RT "GPT2: a glucose 6-phosphate/phosphate translocator with a novel role in
RT the regulation of sugar signalling during seedling development.";
RL Ann. Bot. 113:643-652(2014).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=25474495; DOI=10.1111/pce.12495;
RA Dyson B.C., Allwood J.W., Feil R., Xu Y., Miller M., Bowsher C.G.,
RA Goodacre R., Lunn J.E., Johnson G.N.;
RT "Acclimation of metabolism to light in Arabidopsis thaliana: the glucose 6-
RT phosphate/phosphate translocator GPT2 directs metabolic acclimation.";
RL Plant Cell Environ. 38:1404-1417(2015).
RN [10]
RP INDUCTION.
RX PubMed=31316533; DOI=10.3389/fpls.2019.00827;
RA Weise S.E., Liu T., Childs K.L., Preiser A.L., Katulski H.M.,
RA Perrin-Porzondek C., Sharkey T.D.;
RT "Transcriptional regulation of the glucose-6-phosphate/phosphate
RT translocator 2 is related to carbon exchange across the chloroplast
RT envelope.";
RL Front. Plant Sci. 10:827-827(2019).
RN [11]
RP SUBCELLULAR LOCATION.
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, PubMed:20712627). Required for dynamic
CC acclimation of photosynthesis and partitioning of Glc6P between the
CC chloroplast and the cytosol (PubMed:19939944, PubMed:25474495). May
CC modulate the sensing of sugar status during early seedling development
CC (PubMed:24489010). {ECO:0000269|PubMed:15722468,
CC ECO:0000269|PubMed:19939944, ECO:0000269|PubMed:20712627,
CC ECO:0000269|PubMed:24489010, ECO:0000269|PubMed:25474495}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:32111666}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds, flowers, stamens, and rosette
CC leaves, with highest levels found in sepals and senescing leaves.
CC {ECO:0000269|PubMed:15722468}.
CC -!- INDUCTION: Induced when grown in high light conditions
CC (PubMed:19939944, PubMed:31316533). Highly expressed in response to
CC Pseudomonas syringae treatment (PubMed:15722468).
CC {ECO:0000269|PubMed:15722468, ECO:0000269|PubMed:19939944,
CC ECO:0000269|PubMed:31316533}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:15722468). Slight delay in seedling establishement,
CC specifically in the process of cotyledon greening (PubMed:24489010).
CC {ECO:0000269|PubMed:15722468, ECO:0000269|PubMed:24489010}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. GPT (TC 2.A.7.9)
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28500.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004392; AAC28500.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33888.1; -; Genomic_DNA.
DR EMBL; AY042874; AAK68814.1; -; mRNA.
DR EMBL; AY081479; AAM10041.1; -; mRNA.
DR PIR; T02126; T02126.
DR RefSeq; NP_001320539.1; NM_001334001.1.
DR RefSeq; NP_564785.1; NM_104862.4.
DR AlphaFoldDB; Q94B38; -.
DR SMR; Q94B38; -.
DR BioGRID; 27700; 4.
DR IntAct; Q94B38; 4.
DR STRING; 3702.AT1G61800.1; -.
DR TCDB; 2.A.7.9.6; the drug/metabolite transporter (dmt) superfamily.
DR MetOSite; Q94B38; -.
DR PaxDb; Q94B38; -.
DR ProteomicsDB; 220642; -.
DR EnsemblPlants; AT1G61800.1; AT1G61800.1; AT1G61800.
DR GeneID; 842477; -.
DR Gramene; AT1G61800.1; AT1G61800.1; AT1G61800.
DR KEGG; ath:AT1G61800; -.
DR Araport; AT1G61800; -.
DR TAIR; locus:2036778; AT1G61800.
DR eggNOG; KOG1441; Eukaryota.
DR HOGENOM; CLU_019048_0_1_1; -.
DR InParanoid; Q94B38; -.
DR OMA; WENAVSQ; -.
DR OrthoDB; 1453018at2759; -.
DR PhylomeDB; Q94B38; -.
DR PRO; PR:Q94B38; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94B38; baseline and differential.
DR Genevisible; Q94B38; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast 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:0000325; C:plant-type vacuole; 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:0071917; F:triose-phosphate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IDA:UniProtKB.
DR GO; GO:0015714; P:phosphoenolpyruvate transport; IDA:UniProtKB.
DR GO; GO:0015713; P:phosphoglycerate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0009643; P:photosynthetic acclimation; IMP:UniProtKB.
DR GO; GO:0010109; P:regulation of photosynthesis; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:TAIR.
DR GO; GO:0009624; P:response to nematode; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR GO; GO:0035436; P:triose phosphate transmembrane transport; IDA:UniProtKB.
DR InterPro; IPR004853; Sugar_P_trans_dom.
DR InterPro; IPR004696; Tpt_PEP_transl.
DR Pfam; PF03151; TPT; 1.
DR TIGRFAMs; TIGR00817; tpt; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; Plastid; Reference proteome; Sugar transport;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..388
FT /note="Glucose-6-phosphate/phosphate translocator 2,
FT chloroplastic"
FT /id="PRO_0000035712"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
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 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 113..231
FT /note="EamA"
FT CONFLICT 293
FT /note="G -> V (in Ref. 3; AAK68814/AAM10041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 42754 MW; 12709304B706FAB8 CRC64;
MLSSIKPSSS SFSTAISGSV RRSIPTKLKF SPLLIIKNCH NQSFNANVVS HQKPLHISSA
SNFKREVKVE AYEADRSRPL DINIELPDEQ SAQKLKIGIY FATWWALNVV FNIYNKKVLN
AFPYPWLTST LSLACGSLMM LVSWATRIAD APKTDLEFWK TLFPVAVAHT IGHVAATVSM
SKVAVSFTHI IKSGEPAFSV LVSRFFMGET FPLPVYLSLL PIIGGCALAA ITELNFNITG
FMGAMISNLA FVFRNIFSKK GMKGKSVSGM NYYACLSMMS LVILTPFSIA VEGPQMWAAG
WQNAVSQVGP NFVWWVVAQS VFYHLYNQVS YMSLDQISPL TFSIGNTMKR ISVIVASIII
FHTPIQPVNA LGAAIAIFGT FLYSQAKQ
