TGD3_ARATH
ID TGD3_ARATH Reviewed; 345 AA.
AC Q9AT00; O80812; Q84JX9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein TRIGALACTOSYLDIACYLGLYCEROL 3, chloroplastic {ECO:0000303|PubMed:17938172};
DE AltName: Full=ABC transporter I family member 13 {ECO:0000303|PubMed:18299247};
DE Short=ABC transporter ABCI.13 {ECO:0000303|PubMed:18299247};
DE Short=AtABCI13 {ECO:0000303|PubMed:18299247};
DE AltName: Full=Non-intrinsic ABC protein 11 {ECO:0000303|PubMed:11346655};
DE Short=AtNAP11 {ECO:0000303|PubMed:11346655};
DE Flags: Precursor;
GN Name=TGD3 {ECO:0000303|PubMed:17938172};
GN Synonyms=ABCI13 {ECO:0000303|PubMed:18299247},
GN NAP11 {ECO:0000303|PubMed:11346655};
GN OrderedLocusNames=At1g65410 {ECO:0000312|Araport:AT1G65410};
GN ORFNames=T8F5.19 {ECO:0000312|EMBL:AAC27147.1};
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 [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 [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 [GENOMIC DNA] OF 139-264.
RC STRAIN=cv. Bla-1, cv. Bs-1, cv. Chi-1, cv. Co-1, cv. Cvi-0, cv. Gr-3,
RC cv. Ita-0, cv. Kas-1, and cv. Lisse-2;
RX PubMed=12663546; DOI=10.1093/genetics/163.3.1083;
RA Shepard K.A., Purugganan M.D.;
RT "Molecular population genetics of the Arabidopsis CLAVATA2 region: the
RT genomic scale of variation and selection in a selfing species.";
RL Genetics 163:1083-1095(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [6]
RP FUNCTION, MUTAGENESIS OF PHE-94, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17938172; DOI=10.1074/jbc.m704063200;
RA Lu B., Xu C., Awai K., Jones A.D., Benning C.;
RT "A small ATPase protein of Arabidopsis, TGD3, involved in chloroplast lipid
RT import.";
RL J. Biol. Chem. 282:35945-35953(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(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, AND DISRUPTION PHENOTYPE.
RX PubMed=20132520; DOI=10.1111/j.1365-3040.2010.02124.x;
RA Shimoni-Shor E., Hassidim M., Yuval-Naeh N., Keren N.;
RT "Disruption of Nap14, a plastid-localized non-intrinsic ABC protein in
RT Arabidopsis thaliana results in the over-accumulation of transition metals
RT and in aberrant chloroplast structures.";
RL Plant Cell Environ. 33:1029-1038(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 DISRUPTION PHENOTYPE.
RX PubMed=23463370; DOI=10.1007/s11306-011-0318-z;
RA Okazaki Y., Kamide Y., Hirai M.Y., Saito K.;
RT "Plant lipidomics based on hydrophilic interaction chromatography coupled
RT to ion trap time-of-flight mass spectrometry.";
RL Metabolomics 9:121-131(2013).
RN [12]
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: ATPase transporter involved in lipid transfer from the
CC endoplasmic reticulum (ER) to plastids, and necessary for thylakoids
CC formation. Not involved in transition metal transport pathways
CC (PubMed:20132520). {ECO:0000269|PubMed:17938172,
CC ECO:0000269|PubMed:20132520}.
CC -!- SUBUNIT: Catalytic 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 TGD1 and TGD2 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 stroma
CC {ECO:0000269|PubMed:17938172, ECO:0000269|PubMed:18431481}.
CC -!- DISRUPTION PHENOTYPE: Disruption in the biosynthesis of ER-derived
CC thylakoid lipids, and accumulation of oligogalactolipids,
CC triacylglycerols (TAGs), and phosphatidates (PAs). Accumulates Gal(beta
CC 1,6)betaGalDG, an unusual form of digalactosyldiacylglycerol
CC (PubMed:23463370). Growth retardation, early bolting and no viable
CC seeds produced (PubMed:20132520). {ECO:0000269|PubMed:17938172,
CC ECO:0000269|PubMed:20132520, ECO:0000269|PubMed:23463370}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCI family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27147.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004512; AAC27147.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34370.1; -; Genomic_DNA.
DR EMBL; AF361573; AAK32741.1; -; mRNA.
DR EMBL; AY093985; AAM16246.1; -; mRNA.
DR EMBL; AF528639; AAO43374.1; -; Genomic_DNA.
DR EMBL; AF528640; AAO43375.1; -; Genomic_DNA.
DR EMBL; AF528641; AAO43376.1; -; Genomic_DNA.
DR EMBL; AF528642; AAO43377.1; -; Genomic_DNA.
DR EMBL; AF528643; AAO43378.1; -; Genomic_DNA.
DR EMBL; AF528644; AAO43379.1; -; Genomic_DNA.
DR EMBL; AF528645; AAO43380.1; -; Genomic_DNA.
DR EMBL; AF528646; AAO43381.1; -; Genomic_DNA.
DR EMBL; AF528647; AAO43382.1; -; Genomic_DNA.
DR PIR; T02364; T02364.
DR RefSeq; NP_564850.1; NM_105215.3.
DR AlphaFoldDB; Q9AT00; -.
DR SMR; Q9AT00; -.
DR BioGRID; 28073; 2.
DR STRING; 3702.AT1G65410.1; -.
DR TCDB; 3.A.1.27.2; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q9AT00; -.
DR PRIDE; Q9AT00; -.
DR ProteomicsDB; 246400; -.
DR EnsemblPlants; AT1G65410.1; AT1G65410.1; AT1G65410.
DR GeneID; 842852; -.
DR Gramene; AT1G65410.1; AT1G65410.1; AT1G65410.
DR KEGG; ath:AT1G65410; -.
DR Araport; AT1G65410; -.
DR TAIR; locus:2206275; AT1G65410.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_1_22_1; -.
DR InParanoid; Q9AT00; -.
DR OMA; PEVMFFD; -.
DR OrthoDB; 803978at2759; -.
DR PhylomeDB; Q9AT00; -.
DR PRO; PR:Q9AT00; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9AT00; baseline and differential.
DR Genevisible; Q9AT00; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:TAIR.
DR GO; GO:0006869; P:lipid transport; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Lipid transport; Nucleotide-binding; Plastid;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..345
FT /note="Protein TRIGALACTOSYLDIACYLGLYCEROL 3,
FT chloroplastic"
FT /id="PRO_0000250662"
FT DOMAIN 85..336
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 117..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 94
FT /note="F->A: Reduced ATPase activity and transport
FT properties."
FT /evidence="ECO:0000269|PubMed:17938172"
SQ SEQUENCE 345 AA; 37518 MW; BB2918C19AB4585C CRC64;
MLSLSCSSSS SSLLPPSLHY HGSSSVQSIV VPRRSLISFR RKVSCCCIAP PQNLDNDATK
FDSLTKSGGG MCKERGLEND SDVLIECRDV YKSFGEKHIL KGVSFKIRHG EAVGVIGPSG
TGKSTILKIM AGLLAPDKGE VYIRGKKRAG LISDEEISGL RIGLVFQSAA LFDSLSVREN
VGFLLYERSK MSENQISELV TQTLAAVGLK GVENRLPSEL SGGMKKRVAL ARSLIFDTTK
EVIEPEVLLY DEPTAGLDPI ASTVVEDLIR SVHMTDEDAV GKPGKIASYL VVTHQHSTIQ
RAVDRLLFLY EGKIVWQGMT HEFTTSTNPI VQQFATGSLD GPIRY
