TPT_ARATH
ID TPT_ARATH Reviewed; 410 AA.
AC Q9ZSR7; Q56WK8; Q8LB04; Q93ZM3; Q9FNL1;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Triose phosphate/phosphate translocator TPT, chloroplastic;
DE AltName: Full=Protein ACCLIMATION OF PHOTOSYNTHESIS TO ENVIRONMENT 2;
DE Flags: Precursor;
GN Name=TPT; Synonyms=APE2; OrderedLocusNames=At5g46110; ORFNames=MCL19;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-410.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12472685; DOI=10.1046/j.1365-313x.2002.01460.x;
RA Schneider A., Haeusler R.E., Kolukisaoglu U., Kunze R., van der Graaff E.,
RA Schwacke R., Catoni E., Desimone M., Fluegge U.I.;
RT "An Arabidopsis thaliana knock-out mutant of the chloroplast triose
RT phosphate/phosphate translocator is severely compromised only when starch
RT synthesis, but not starch mobilisation is abolished.";
RL Plant J. 32:685-699(2002).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11842155; DOI=10.1104/pp.010576;
RA Eicks M., Maurino V., Knappe S., Fluegge U.I., Fischer K.;
RT "The plastidic pentose phosphate translocator represents a link between the
RT cytosolic and the plastidic pentose phosphate pathways in plants.";
RL Plant Physiol. 128:512-522(2002).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija-2;
RX PubMed=12586872; DOI=10.1104/pp.015479;
RA Walters R.G., Shephard F., Rogers J.J., Rolfe S.A., Horton P.;
RT "Identification of mutants of Arabidopsis defective in acclimation of
RT photosynthesis to the light environment.";
RL Plant Physiol. 131:472-481(2003).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21175634; DOI=10.1111/j.1469-8137.2010.03580.x;
RA Cho M.H., Lim H., Shin D.H., Jeon J.S., Bhoo S.H., Park Y.I., Hahn T.R.;
RT "Role of the plastidic glucose translocator in the export of starch
RT degradation products from the chloroplasts in Arabidopsis thaliana.";
RL New Phytol. 190:101-112(2011).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-83, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER LYS-82, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
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).
CC -!- FUNCTION: Triose phosphate/phosphate translocator that transports
CC inorganic phosphate, 3-phosphoglycerate (3-PGA) and triose phosphate.
CC Functions in the export of photoassimilates from chloroplasts during
CC the day. In the light, triose phosphates are exported from the
CC chloroplast stroma in counter exchange with inorganic phosphate (Pi),
CC generated during sucrose biosynthesis in the cytosol. Involved in
CC photosynthetic acclimation, a light response resulting in increased
CC tolerance to high-intensity light. {ECO:0000269|PubMed:12472685,
CC ECO:0000269|PubMed:12586872, ECO:0000269|PubMed:20712627}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZSR7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in shoots, leaves and flowers.
CC {ECO:0000269|PubMed:11842155, ECO:0000269|PubMed:21175634}.
CC -!- INDUCTION: Expressed with a circadian rhythm showing an increase during
CC the day and a decrease at night under long day conditions.
CC {ECO:0000269|PubMed:21175634}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but strong reduction of triose phosphate export from the
CC chloroplast and reduced photosynthetic acclimation.
CC {ECO:0000269|PubMed:12472685, ECO:0000269|PubMed:12586872}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9)
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL10481.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB08256.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB006698; BAB08256.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95338.1; -; Genomic_DNA.
DR EMBL; AF097648; AAC83815.1; -; mRNA.
DR EMBL; AY037211; AAK59796.1; -; mRNA.
DR EMBL; AY050811; AAK92746.1; -; mRNA.
DR EMBL; AY056790; AAL10481.1; ALT_FRAME; mRNA.
DR EMBL; AY091414; AAM14353.1; -; mRNA.
DR EMBL; BT002683; AAO11599.1; -; mRNA.
DR EMBL; AY087499; AAM65042.1; -; mRNA.
DR EMBL; AK222032; BAD94739.1; -; mRNA.
DR PIR; T51692; T51692.
DR RefSeq; NP_851138.1; NM_180807.2. [Q9ZSR7-1]
DR AlphaFoldDB; Q9ZSR7; -.
DR SMR; Q9ZSR7; -.
DR BioGRID; 19901; 3.
DR IntAct; Q9ZSR7; 2.
DR STRING; 3702.AT5G46110.4; -.
DR TCDB; 2.A.7.9.23; the drug/metabolite transporter (dmt) superfamily.
DR iPTMnet; Q9ZSR7; -.
DR PaxDb; Q9ZSR7; -.
DR EnsemblPlants; AT5G46110.1; AT5G46110.1; AT5G46110. [Q9ZSR7-1]
DR GeneID; 834652; -.
DR Gramene; AT5G46110.1; AT5G46110.1; AT5G46110. [Q9ZSR7-1]
DR KEGG; ath:AT5G46110; -.
DR Araport; AT5G46110; -.
DR eggNOG; KOG1441; Eukaryota.
DR HOGENOM; CLU_019048_0_2_1; -.
DR InParanoid; Q9ZSR7; -.
DR PhylomeDB; Q9ZSR7; -.
DR PRO; PR:Q9ZSR7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZSR7; baseline and differential.
DR Genevisible; Q9ZSR7; AT.
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:0015297; F:antiporter activity; IBA:GO_Central.
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:0015713; P:phosphoglycerate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0009643; P:photosynthetic acclimation; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chloroplast; Membrane; Plastid;
KW Reference proteome; Sugar transport; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..82
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 83..410
FT /note="Triose phosphate/phosphate translocator TPT,
FT chloroplastic"
FT /id="PRO_0000406095"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 83
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 94
FT /note="D -> E (in Ref. 4; AAM65042)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="V -> A (in Ref. 5; BAD94739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 44633 MW; 5B44019F6F95600A CRC64;
MESRVLLRAT ANVVGIPKLR RPIGAIHRQF STASSSSFSV KPIGGIGEGA NLISGRQLRP
ILLLDSSAIN GGEKREILKP VKAAAAEGGD TAGDAKVGFL AKYPWLVTGF FFFMWYFLNV
IFNILNKKIY NYFPYPYFVS VIHLFVGVVY CLISWSVGLP KRAPIDSNLL KVLIPVAVCH
ALGHVTSNVS FAAVAVSFTH TIKALEPFFN AAASQFIMGQ SIPITLWLSL APVVLGVAMA
SLTELSFNWL GFISAMISNI SFTYRSIFSK KAMTDMDSTN VYAYISIIAL FVCIPPAIIV
EGPKLLNHGF ADAIAKVGMT KFISDLFWVG MFYHLYNQLA TNTLERVAPL THAVGNVLKR
VFVIGFSIVI FGNKISTQTG IGTGIAIAGV AMYSIIKAKI EEEKRQGKKA
