XPT_ARATH
ID XPT_ARATH Reviewed; 417 AA.
AC Q9LF61; Q94JT2; Q9FR26;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Xylulose 5-phosphate/phosphate translocator, chloroplastic;
DE Short=Xul-5-P/phosphate translocator;
DE Flags: Precursor;
GN Name=XPT; Synonyms=RPT; OrderedLocusNames=At5g17630; ORFNames=K10A8.110;
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], FUNCTION, AND 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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-83, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-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 [6]
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: Sugar phosphate/phosphate translocator that transports
CC inorganic phosphate, triose phosphate, 3-phosphoglycerate, xylulose 5-
CC phosphate (Xul-5-P) and to a lesser extent ribulose 5-phosphate. Does
CC not transport ribose 5-phosphate or hexose phosphates. Provides
CC cytosolic Xul-5-P to the chloroplast, where it is used as an
CC intermediate in the plastidic pentose phosphate pathways.
CC {ECO:0000269|PubMed:11842155}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11842155}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9)
CC subfamily. {ECO:0000305}.
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DR EMBL; AF209211; AAG48163.1; -; Genomic_DNA.
DR EMBL; AL391151; CAC01907.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92450.1; -; Genomic_DNA.
DR EMBL; AF372964; AAK50101.1; -; mRNA.
DR EMBL; BT000586; AAN18155.1; -; mRNA.
DR PIR; T51467; T51467.
DR RefSeq; NP_197265.1; NM_121769.4.
DR AlphaFoldDB; Q9LF61; -.
DR SMR; Q9LF61; -.
DR BioGRID; 16905; 9.
DR IntAct; Q9LF61; 9.
DR STRING; 3702.AT5G17630.1; -.
DR TCDB; 2.A.7.9.22; the drug/metabolite transporter (dmt) superfamily.
DR iPTMnet; Q9LF61; -.
DR PaxDb; Q9LF61; -.
DR PRIDE; Q9LF61; -.
DR ProteomicsDB; 242459; -.
DR EnsemblPlants; AT5G17630.1; AT5G17630.1; AT5G17630.
DR GeneID; 831629; -.
DR Gramene; AT5G17630.1; AT5G17630.1; AT5G17630.
DR KEGG; ath:AT5G17630; -.
DR Araport; AT5G17630; -.
DR TAIR; locus:2151381; AT5G17630.
DR eggNOG; KOG1441; Eukaryota.
DR HOGENOM; CLU_019048_0_1_1; -.
DR InParanoid; Q9LF61; -.
DR OMA; SIWMLIL; -.
DR OrthoDB; 1453018at2759; -.
DR PhylomeDB; Q9LF61; -.
DR PRO; PR:Q9LF61; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LF61; baseline and differential.
DR Genevisible; Q9LF61; AT.
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: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: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; Chloroplast; Membrane; Plastid; Reference proteome;
KW Sugar transport; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..82
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 83..417
FT /note="Xylulose 5-phosphate/phosphate translocator,
FT chloroplastic"
FT /id="PRO_0000406098"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 127..243
FT /note="EamA"
FT REGION 66..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 101
FT /note="E -> G (in Ref. 4; AAK50101/AAN18155)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="L -> W (in Ref. 1; AAG48163)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="F -> C (in Ref. 1; AAG48163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 45770 MW; 1ADC0FE38987F291 CRC64;
MISLNLSPSL NPGLLHKTRT CQQPTRLSAL LVTNPKPFNH RHPLGLSPIP NLQIRDVSAK
PLLSLTNPES SSGFSRKPRS IAAVGSSDSN PDEKSDLGEA EKKEKKAKTL QLGIVFGLWY
FQNIVFNIFN KKALNVFPYP WLLASFQLFA GSIWMLVLWS FKLYPCPKIS KPFIIALLGP
ALFHTIGHIS ACVSFSKVAV SFTHVIKSAE PVFSVIFSSL LGDSYPLAVW LSILPIVMGC
SLAAVTEVSF NLGGLSGAMI SNVGFVLRNI YSKRSLQSFK EIDGLNLYGC ISILSLLYLF
PVAIFVEGSH WVPGYHKAIA SVGTPSTFYF WVLLSGVFYH LYNQSSYQAL DEISPLTFSV
GNTMKRVVVI ISTVLVFRNP VRPLNALGSA IAIFGTFLYS QATAKKKKIE VGGDKKN
