TGD2_ARATH
ID TGD2_ARATH Reviewed; 381 AA.
AC Q9LTR2; Q3EB35; Q8LDY9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein TRIGALACTOSYLDIACYLGLYCEROL 2, chloroplastic {ECO:0000303|PubMed:16818883};
DE AltName: Full=ABC transporter I family member 15 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCI.15 {ECO:0000303|PubMed:18299247};
DE Short=AtABCI15 {ECO:0000303|PubMed:18299247};
DE Flags: Precursor;
GN Name=TGD2 {ECO:0000303|PubMed:16818883};
GN Synonyms=ABCI15 {ECO:0000303|PubMed:18299247};
GN OrderedLocusNames=At3g20320 {ECO:0000312|Araport:AT3G20320};
GN ORFNames=MQC12.6 {ECO:0000312|EMBL:BAB02812.1};
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] (ISOFORM 1), FUNCTION, MUTAGENESIS OF GLY-234,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=16818883; DOI=10.1073/pnas.0602754103;
RA Awai K., Xu C., Tamot B., Benning C.;
RT "A phosphatidic acid-binding protein of the chloroplast inner envelope
RT membrane involved in lipid trafficking.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10817-10822(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] (IOSOFORM 1).
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] (IOSOFORM 1).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
RN [7]
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF LYS-221.
RX PubMed=19416982; DOI=10.1074/jbc.m109.016014;
RA Lu B., Benning C.;
RT "A 25-amino acid sequence of the Arabidopsis TGD2 protein is sufficient for
RT specific binding of phosphatidic acid.";
RL J. Biol. Chem. 284:17420-17427(2009).
RN [8]
RP SUBUNIT, AND MUTAGENESIS OF GLY-98; GLY-192; PRO-203; GLY-234; GLY-237 AND
RP GLY-251.
RX PubMed=21309871; DOI=10.1111/j.1365-313x.2011.04536.x;
RA Roston R., Gao J., Xu C., Benning C.;
RT "Arabidopsis chloroplast lipid transport protein TGD2 disrupts membranes
RT and is part of a large complex.";
RL Plant J. 66:759-769(2011).
RN [9]
RP IDENTIFICATION IN THE TGD COMPLEX, AND INTERACTION WITH TGD1 AND TGD3.
RX PubMed=22544736; DOI=10.1074/jbc.m112.370213;
RA Roston R.L., Gao J., Murcha M.W., Whelan J., Benning C.;
RT "TGD1, -2, and -3 proteins involved in lipid trafficking form ATP-binding
RT cassette (ABC) transporter with multiple substrate-binding proteins.";
RL J. Biol. Chem. 287:21406-21415(2012).
RN [10]
RP INTERACTION WITH TGD5.
RX PubMed=26410300; DOI=10.1105/tpc.15.00394;
RA Fan J., Zhai Z., Yan C., Xu C.;
RT "Arabidopsis TRIGALACTOSYLDIACYLGLYCEROL5 interacts with TGD1, TGD2, and
RT TGD4 to facilitate lipid transfer from the endoplasmic reticulum to
RT plastids.";
RL Plant Cell 27:2941-2955(2015).
CC -!- FUNCTION: Component of a phosphatidic acid/lipid transport complex in
CC the chloroplast envelope. Specifically binds phosphatidic acid (PA).
CC Involved in lipid transfer from the endoplasmic reticulum (ER) to
CC plastids, and necessary for thylakoids formation.
CC {ECO:0000269|PubMed:16818883}.
CC -!- SUBUNIT: Homomultimer (PubMed:19416982, PubMed:21309871). Substrate-
CC binding subunit of the TGD complex, a lipid translocator at the inner
CC chloroplast envelope membrane made of TGD1, TGD2 and TGD3
CC (PubMed:21309871, PubMed:22544736). Interacts with TGD1 and TGD3 with
CC an overall subunit stoichiometry of 2 TGD1, 2 TGD3 and 8 to 12 TGD2
CC (PubMed:22544736). Interacts with TGD5 (PubMed:26410300).
CC {ECO:0000269|PubMed:19416982, ECO:0000269|PubMed:21309871,
CC ECO:0000269|PubMed:22544736, ECO:0000269|PubMed:26410300}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:16818883}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LTR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LTR2-2; Sequence=VSP_037648;
CC -!- DOMAIN: Amino acids 201-225 are sufficient for specific binding of
CC phosphatidic acid. {ECO:0000269|PubMed:19416982}.
CC -!- CAUTION: Was originally (PubMed:18299247) thought to belong to the ABC
CC transporter family. Lacks the conserved ABC domain, which is one of the
CC features of the ABC transporter family. {ECO:0000305|PubMed:18299247}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM62940.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB024036; BAB02812.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76363.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76364.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63486.1; -; Genomic_DNA.
DR EMBL; AY048230; AAK82493.1; -; mRNA.
DR EMBL; AY094020; AAM16176.1; -; mRNA.
DR EMBL; AY085722; AAM62940.1; ALT_INIT; mRNA.
DR RefSeq; NP_001319601.1; NM_001338475.1. [Q9LTR2-2]
DR RefSeq; NP_566659.1; NM_112923.4. [Q9LTR2-1]
DR RefSeq; NP_974345.1; NM_202616.1. [Q9LTR2-2]
DR AlphaFoldDB; Q9LTR2; -.
DR BioGRID; 6908; 7.
DR IntAct; Q9LTR2; 4.
DR STRING; 3702.AT3G20320.1; -.
DR TCDB; 3.A.1.27.2; the atp-binding cassette (abc) superfamily.
DR SwissPalm; Q9LTR2; -.
DR PaxDb; Q9LTR2; -.
DR PRIDE; Q9LTR2; -.
DR ProteomicsDB; 234407; -. [Q9LTR2-1]
DR EnsemblPlants; AT3G20320.1; AT3G20320.1; AT3G20320. [Q9LTR2-1]
DR EnsemblPlants; AT3G20320.2; AT3G20320.2; AT3G20320. [Q9LTR2-2]
DR EnsemblPlants; AT3G20320.3; AT3G20320.3; AT3G20320. [Q9LTR2-2]
DR GeneID; 821576; -.
DR Gramene; AT3G20320.1; AT3G20320.1; AT3G20320. [Q9LTR2-1]
DR Gramene; AT3G20320.2; AT3G20320.2; AT3G20320. [Q9LTR2-2]
DR Gramene; AT3G20320.3; AT3G20320.3; AT3G20320. [Q9LTR2-2]
DR KEGG; ath:AT3G20320; -.
DR Araport; AT3G20320; -.
DR TAIR; locus:2092354; AT3G20320.
DR eggNOG; ENOG502QY75; Eukaryota.
DR HOGENOM; CLU_050607_0_0_1; -.
DR InParanoid; Q9LTR2; -.
DR OMA; WYLFAEF; -.
DR PhylomeDB; Q9LTR2; -.
DR PRO; PR:Q9LTR2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LTR2; baseline and differential.
DR Genevisible; Q9LTR2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005319; F:lipid transporter activity; IMP:TAIR.
DR GO; GO:0005543; F:phospholipid binding; IDA:TAIR.
DR GO; GO:0032365; P:intracellular lipid transport; IMP:TAIR.
DR GO; GO:0006869; P:lipid transport; IMP:TAIR.
DR InterPro; IPR003399; Mce/MlaD.
DR InterPro; IPR039342; TGD2-like.
DR PANTHER; PTHR34675; PTHR34675; 1.
DR Pfam; PF02470; MlaD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Lipid transport; Membrane; Plastid;
KW Plastid inner membrane; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..381
FT /note="Protein TRIGALACTOSYLDIACYLGLYCEROL 2,
FT chloroplastic"
FT /id="PRO_0000379145"
FT TOPO_DOM 46..96
FT /note="Stromal"
FT /evidence="ECO:0000269|PubMed:16818883"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..381
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000269|PubMed:16818883"
FT VAR_SEQ 283..381
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037648"
FT MUTAGEN 98
FT /note="G->D: In tgd2-3; accumulation of
FT trigalactosyldiacylglycerol."
FT /evidence="ECO:0000269|PubMed:21309871"
FT MUTAGEN 192
FT /note="G->S: In tgd2-5; accumulation of
FT trigalactosyldiacylglycerol."
FT /evidence="ECO:0000269|PubMed:21309871"
FT MUTAGEN 203
FT /note="P->S: In tgd2-6; accumulation of
FT trigalactosyldiacylglycerol."
FT /evidence="ECO:0000269|PubMed:21309871"
FT MUTAGEN 221
FT /note="K->A: Reduced phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:19416982"
FT MUTAGEN 234
FT /note="G->R: In tgd2-1; loss of function resulting in
FT accumulation of trigalactosyldiacylglycerol and smaller and
FT slightly pale plants."
FT /evidence="ECO:0000269|PubMed:16818883,
FT ECO:0000269|PubMed:21309871"
FT MUTAGEN 237
FT /note="G->R: In tgd2-2; accumulation of
FT trigalactosyldiacylglycerol."
FT /evidence="ECO:0000269|PubMed:21309871"
FT MUTAGEN 251
FT /note="G->E: In tgd2-4; accumulation of
FT trigalactosyldiacylglycerol."
FT /evidence="ECO:0000269|PubMed:21309871"
SQ SEQUENCE 381 AA; 41630 MW; 80E1C6C9B6C67762 CRC64;
MIGNPVIQVP SSLMPSSSMI ACPRVSPNGV PYLPPKPRTR HLVVRAASNS DAAHGQPSSD
GGKNPLTVVL DVPRNIWRQT LKPLSDFGFG KRSIWEGGVG LFIVSGATLL ALSWAWLRGF
QMRSKFRKYQ TVFELSHASG ICTGTPVRIR GVTVGTIIRV NPSLKNIEAV AEIEDDKIII
PRNSLVEVNQ SGLLMETMID IMPRNPIPEP SVGPLHPECG KEGLIVCDRQ TIKGVQGVSL
DELVGIFTRI GREVEAIGVA NTYSLAERAA SVIEEARPLL KKIQAMAEDA QPLLSEFRDS
GLLKEVECLT RSLTQASDDL RKVNSSIMTP ENTELIQKSI YTLVYTLKNV ESISSDILGF
TGDEATRKNL KLLIKSLSRL L
