TGD1_ARATH
ID TGD1_ARATH Reviewed; 350 AA.
AC Q8L4R0; Q9FXH8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein TRIGALACTOSYLDIACYLGLYCEROL 1, chloroplastic {ECO:0000303|PubMed:12743031};
DE AltName: Full=ABC transporter I family member 14 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCI.14 {ECO:0000303|PubMed:18299247};
DE Short=AtABCI14 {ECO:0000303|PubMed:18299247};
DE Flags: Precursor;
GN Name=TGD1 {ECO:0000303|PubMed:12743031};
GN Synonyms=ABCI14 {ECO:0000303|PubMed:18299247};
GN OrderedLocusNames=At1g19800 {ECO:0000312|Araport:AT1G19800};
GN ORFNames=F14P1.27 {ECO:0000312|EMBL:AAG12551.1};
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], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=12743031; DOI=10.1093/emboj/cdg234;
RA Xu C., Fan J., Riekhof W., Froehlich J.E., Benning C.;
RT "A permease-like protein involved in ER to thylakoid lipid transfer in
RT Arabidopsis.";
RL EMBO J. 22:2370-2379(2003).
RN [2]
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 [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] OF 108-350.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DISRUPTION PHENOTYPE.
RX PubMed=16199613; DOI=10.1105/tpc.105.035592;
RA Xu C., Fan J., Froehlich J.E., Awai K., Benning C.;
RT "Mutation of the TGD1 chloroplast envelope protein affects phosphatidate
RT metabolism in Arabidopsis.";
RL Plant Cell 17:3094-3110(2005).
RN [7]
RP FUNCTION.
RX PubMed=18689504; DOI=10.1105/tpc.108.061176;
RA Xu C., Fan J., Cornish A.J., Benning C.;
RT "Lipid trafficking between the endoplasmic reticulum and the plastid in
RT Arabidopsis requires the extraplastidic TGD4 protein.";
RL Plant Cell 20:2190-2204(2008).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=20410050; DOI=10.1093/pcp/pcq053;
RA Xu C., Moellering E.R., Muthan B., Fan J., Benning C.;
RT "Lipid transport mediated by Arabidopsis TGD proteins is unidirectional
RT from the endoplasmic reticulum to the plastid.";
RL Plant Cell Physiol. 51:1019-1028(2010).
RN [10]
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 [11]
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: Required during embryogenesis. Permease involved in lipid
CC transfer from the endoplasmic reticulum (ER) to plastids, and necessary
CC for thylakoids formation. {ECO:0000269|PubMed:12743031,
CC ECO:0000269|PubMed:16199613, ECO:0000269|PubMed:18689504,
CC ECO:0000269|PubMed:20410050}.
CC -!- SUBUNIT: Permease subunit of the TGD complex, a lipid translocator at
CC the inner chloroplast envelope membrane made of TGD1, TGD2 and TGD3
CC (PubMed:22544736). Interacts with TGD2 and TGD3 with an overall subunit
CC stoichiometry of 2 TGD1, 2 TGD3 and 8 to 12 TGD2 (PubMed:22544736).
CC Interacts with TGD5 (PubMed:26410300). {ECO:0000269|PubMed:22544736,
CC ECO:0000269|PubMed:26410300}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:12743031, ECO:0000269|PubMed:16199613}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: High levels in green tissues, but low levels in
CC nongreen tissues such as roots. {ECO:0000269|PubMed:12743031}.
CC -!- DISRUPTION PHENOTYPE: Disruption in the biosynthesis of ER-derived
CC thylakoid lipids, and accumulation of oligogalactolipids,
CC triacylglycerols (TAGs), and phosphatidates (PAs). Reduced growth with
CC stout leaves and siliques. Impaired embryogenesis.
CC {ECO:0000269|PubMed:12743031, ECO:0000269|PubMed:16199613}.
CC -!- SIMILARITY: Belongs to the MlaE permease family. {ECO:0000305}.
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=AAG12551.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY568410; AAS75319.1; -; mRNA.
DR EMBL; AC007797; AAG12551.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29899.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29900.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29901.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60434.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60435.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60436.1; -; Genomic_DNA.
DR EMBL; AY096644; AAM20141.1; -; mRNA.
DR EMBL; AY114021; AAM45069.1; -; mRNA.
DR EMBL; AK317390; BAH20061.1; -; mRNA.
DR PIR; B86331; B86331.
DR RefSeq; NP_001322720.1; NM_001332408.1.
DR RefSeq; NP_001322721.1; NM_001332409.1.
DR RefSeq; NP_001322722.1; NM_001332407.1.
DR RefSeq; NP_173410.1; NM_101836.4.
DR RefSeq; NP_973868.1; NM_202139.3.
DR RefSeq; NP_973869.1; NM_202140.2.
DR AlphaFoldDB; Q8L4R0; -.
DR SMR; Q8L4R0; -.
DR BioGRID; 23807; 24.
DR IntAct; Q8L4R0; 22.
DR STRING; 3702.AT1G19800.2; -.
DR TCDB; 3.A.1.27.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q8L4R0; -.
DR PRIDE; Q8L4R0; -.
DR ProteomicsDB; 246471; -.
DR EnsemblPlants; AT1G19800.1; AT1G19800.1; AT1G19800.
DR EnsemblPlants; AT1G19800.2; AT1G19800.2; AT1G19800.
DR EnsemblPlants; AT1G19800.3; AT1G19800.3; AT1G19800.
DR EnsemblPlants; AT1G19800.4; AT1G19800.4; AT1G19800.
DR EnsemblPlants; AT1G19800.5; AT1G19800.5; AT1G19800.
DR EnsemblPlants; AT1G19800.6; AT1G19800.6; AT1G19800.
DR GeneID; 838568; -.
DR Gramene; AT1G19800.1; AT1G19800.1; AT1G19800.
DR Gramene; AT1G19800.2; AT1G19800.2; AT1G19800.
DR Gramene; AT1G19800.3; AT1G19800.3; AT1G19800.
DR Gramene; AT1G19800.4; AT1G19800.4; AT1G19800.
DR Gramene; AT1G19800.5; AT1G19800.5; AT1G19800.
DR Gramene; AT1G19800.6; AT1G19800.6; AT1G19800.
DR KEGG; ath:AT1G19800; -.
DR Araport; AT1G19800; -.
DR TAIR; locus:2013099; AT1G19800.
DR eggNOG; ENOG502QPRJ; Eukaryota.
DR HOGENOM; CLU_045686_1_0_1; -.
DR InParanoid; Q8L4R0; -.
DR OMA; YFQNGAP; -.
DR OrthoDB; 899719at2759; -.
DR PhylomeDB; Q8L4R0; -.
DR PRO; PR:Q8L4R0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L4R0; baseline and differential.
DR Genevisible; Q8L4R0; AT.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; TAS:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005319; F:lipid transporter activity; IMP:TAIR.
DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IMP:TAIR.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
DR InterPro; IPR003453; ABC_MlaE_Proteobac.
DR InterPro; IPR030802; Permease_MalE.
DR PANTHER; PTHR30188; PTHR30188; 1.
DR Pfam; PF02405; MlaE; 1.
DR TIGRFAMs; TIGR00056; TIGR00056; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lipid transport; Membrane; Plastid; Plastid inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT CHAIN ?..350
FT /note="Protein TRIGALACTOSYLDIACYLGLYCEROL 1,
FT chloroplastic"
FT /id="PRO_0000379144"
FT TOPO_DOM ?..97
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305|PubMed:16199613"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..136
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:16199613"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..168
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305|PubMed:16199613"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..229
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:16199613"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..288
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305|PubMed:16199613"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..318
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:16199613"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..350
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305|PubMed:16199613"
FT REGION 67..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 37907 MW; 5356B6CABE7B103E CRC64;
MMQTCCIHQS FCFPHRVFPR FDASIGIKPP KLCQVGFIGK TQSYGISSPI RQRRLYVNLN
ANDGHPSMSM LEEETSTENN APSQEAELPF SKWSPSKYIW RGLSVPIIAG QVVLRILKGK
IHWRNTLQQL ERTGPKSLGV CLLTSTFVGM AFTIQFVREF TRLGLNRSIG GVLALAFSRE
LSPVITSIVV AGRMGSAFAA ELGTMQVSEQ TDTLRVLGAD PIDYLITPRV IASCLALPFL
TLMCFTVGMA SSALLSDAVY GISINIIMDS AHRALRPWDI VSAMIKSQVF GAIISVISCS
WGVTTTGGAK GVGESTTSAV VMSLVGIFIA DFVLSSFFFQ GAGDSLKNCV
