PPT1_ARATH
ID PPT1_ARATH Reviewed; 408 AA.
AC Q8RXN3; P92991; Q8LDB3; Q9M669;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Phosphoenolpyruvate/phosphate translocator 1, chloroplastic;
DE Short=AtPPT1;
DE AltName: Full=Protein CAB UNDEREXPRESSED 1;
DE Flags: Precursor;
GN Name=PPT1; Synonyms=CUE1; OrderedLocusNames=At5g33320; ORFNames=F19N2.40;
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 [GENOMIC DNA / MRNA].
RA Deterding S., Fluegge U.-I., Fischer K.;
RT "The phosphate/phosphoenolpyruvate translocator gene from Arabidopsis.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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].
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 [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-251; ARG-265 AND ALA-388.
RX PubMed=10488230; DOI=10.2307/3871041;
RA Streatfield S.J., Weber A., Kinsman E.A., Haeusler R.E., Li J.,
RA Post-Beittenmiller D., Kaiser W.M., Pyke K.A., Fluegge U.I., Chory J.;
RT "The phosphoenolpyruvate/phosphate translocator is required for phenolic
RT metabolism, palisade cell development, and plastid-dependent nuclear gene
RT expression.";
RL Plant Cell 11:1609-1622(1999).
RN [7]
RP ACETYLATION AT ALA-86, CLEAVAGE OF TRANSIT PEPTIDE AFTER ALA-85,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14617088; DOI=10.1046/j.1365-313x.2003.01889.x;
RA Voll L., Haeusler R.E., Hecker R., Weber A., Weissenboeck G., Fiene G.,
RA Waffenschmidt S., Fluegge U.I.;
RT "The phenotype of the Arabidopsis cue1 mutant is not simply caused by a
RT general restriction of the shikimate pathway.";
RL Plant J. 36:301-317(2003).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14617097; DOI=10.1046/j.1365-313x.2003.01888.x;
RA Knappe S., Loettgert T., Schneider A., Voll L., Fluegge U.I., Fischer K.;
RT "Characterization of two functional phosphoenolpyruvate/phosphate
RT translocator (PPT) genes in Arabidopsis--AtPPT1 may be involved in the
RT provision of signals for correct mesophyll development.";
RL Plant J. 36:411-420(2003).
RN [10]
RP FUNCTION.
RX PubMed=17981875; DOI=10.1093/pcp/pcm150;
RA Nozawa A., Nanamiya H., Miyata T., Linka N., Endo Y., Weber A.P.,
RA Tozawa Y.;
RT "A cell-free translation and proteoliposome reconstitution system for
RT functional analysis of plant solute transporters.";
RL Plant Cell Physiol. 48:1815-1820(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-86, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-85, 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: Phosphoenolpyruvate/phosphate translocator that transports
CC phosphoenolpyruvate (PEP), 2-phosphoglycerate, 3-phosphoglycerate and
CC dihydroxyacetone phosphate. Imports PEP to the chloroplast stroma as
CC one substrate of the shikimate pathway, from which aromatic amino acids
CC and a variety of secondary products derive. Required for correct leaf
CC mesophyll cell development and expression of chlorophyll a/b binding
CC protein 3 (CAB3). {ECO:0000269|PubMed:10488230,
CC ECO:0000269|PubMed:14617088, ECO:0000269|PubMed:14617097,
CC ECO:0000269|PubMed:17981875}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in root columella, lateral root cap and
CC root vasculature tissue. In leaves, highly expressed in xylem
CC parenchyma cells. In flowers, expressed in sepals, petals, filaments of
CC the stamens, anthers and stigma. {ECO:0000269|PubMed:14617097}.
CC -!- DISRUPTION PHENOTYPE: Reticulate leaf phenotype. Reduced number of leaf
CC palisade mesophyll cells and increased bundle sheath cells. Small
CC chloroplasts in mesophyll cells. Reduced photosynthetic electron
CC transport rate. Under-expression of CAB3 protein. Reduced levels of
CC aromatic amino acids and phenolic compounds derived from shikimate
CC pathway. {ECO:0000269|PubMed:14617088, ECO:0000269|PubMed:14617097}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. PPT (TC 2.A.7.9)
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U66321; AAB40646.1; -; mRNA.
DR EMBL; AF209210; AAF63704.1; -; Genomic_DNA.
DR EMBL; AC051625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93894.1; -; Genomic_DNA.
DR EMBL; AY080788; AAL87271.1; -; mRNA.
DR EMBL; AY133809; AAM91743.1; -; mRNA.
DR EMBL; AY086100; AAM63308.1; -; mRNA.
DR RefSeq; NP_198317.1; NM_122856.3.
DR AlphaFoldDB; Q8RXN3; -.
DR SMR; Q8RXN3; -.
DR BioGRID; 18566; 3.
DR STRING; 3702.AT5G33320.1; -.
DR iPTMnet; Q8RXN3; -.
DR PaxDb; Q8RXN3; -.
DR PRIDE; Q8RXN3; -.
DR ProteomicsDB; 226493; -.
DR EnsemblPlants; AT5G33320.1; AT5G33320.1; AT5G33320.
DR GeneID; 833308; -.
DR Gramene; AT5G33320.1; AT5G33320.1; AT5G33320.
DR KEGG; ath:AT5G33320; -.
DR Araport; AT5G33320; -.
DR TAIR; locus:2145944; AT5G33320.
DR eggNOG; KOG1441; Eukaryota.
DR HOGENOM; CLU_019048_0_0_1; -.
DR InParanoid; Q8RXN3; -.
DR OMA; FWYTVSS; -.
DR OrthoDB; 1453018at2759; -.
DR PhylomeDB; Q8RXN3; -.
DR PRO; PR:Q8RXN3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RXN3; baseline and differential.
DR Genevisible; Q8RXN3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA: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:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009528; C:plastid inner membrane; TAS:TAIR.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0015121; F:phosphoenolpyruvate:phosphate antiporter activity; IDA:UniProtKB.
DR GO; GO:0015120; F:phosphoglycerate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0009670; F:triose-phosphate:phosphate antiporter activity; IEA:EnsemblPlants.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015714; P:phosphoenolpyruvate transport; IDA:UniProtKB.
DR GO; GO:0015713; P:phosphoglycerate 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; Chloroplast; Membrane; Plastid; Pyruvate; Reference proteome;
KW Sugar transport; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..85
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:12766230,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 86..408
FT /note="Phosphoenolpyruvate/phosphate translocator 1,
FT chloroplastic"
FT /id="PRO_0000406099"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 124..241
FT /note="EamA"
FT MOD_RES 86
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12766230,
FT ECO:0007744|PubMed:22223895"
FT MUTAGEN 251
FT /note="G->E: In cue1-7; strong reticulate leaf phenotype."
FT /evidence="ECO:0000269|PubMed:10488230"
FT MUTAGEN 265
FT /note="R->C: In cue1-5; weak reticulate leaf phenotype."
FT /evidence="ECO:0000269|PubMed:10488230"
FT MUTAGEN 388
FT /note="A->V: In cue1-3; weak reticulate leaf phenotype."
FT /evidence="ECO:0000269|PubMed:10488230"
FT CONFLICT 153
FT /note="I -> T (in Ref. 1; AAF63704)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="L -> I (in Ref. 1; AAB40646)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="K -> Q (in Ref. 5; AAM63308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 44224 MW; 4C912B12D77CE5F6 CRC64;
MQSSAVFSLS PSLPLLKPRR LSLRHHPITT AASSSDLNVS PNVVSIPSLS RRSWRLASSD
SPLRAWSGVP SPISHSLDTN RFRTAATAVP ESAEEGDNSG KLTKVLELGL LFAMWYLFNI
YFNIYNKQVL KALHAPMTVT LVQFAVGSVL ITIMWVLNLY KRPKISGAQL AAILPLAVVH
TLGNLFTNMS LGKVSVSFTH TIKAMEPFFS VLLSAMFLGE KPTPWVLGAI VPIVGGVALA
SISEVSFNWA GFSSAMASNL TNQSRNVLSK KVMVKKDDSL DNITLFSIIT LMSLVLMAPV
TFFTEGIKFT PSYIQSAGVN VKQIYTKSLI AALCFHAYQQ VSYMILARVS PVTHSVGNCV
KRVVVIVSSV IFFKTPVSPV NAFGTGIALA GVFLYSRVKG IKPKPKTA
