TGD4_ARATH
ID TGD4_ARATH Reviewed; 479 AA.
AC Q9M903;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein TRIGALACTOSYLDIACYLGLYCEROL 4, chloroplastic {ECO:0000303|PubMed:18689504};
DE AltName: Full=Protein PIGMENT DEFECTIVE 320;
GN Name=TGD4 {ECO:0000303|PubMed:18689504}; Synonyms=PDE320;
GN OrderedLocusNames=At3g06960 {ECO:0000312|Araport:AT3G06960};
GN ORFNames=F17A9.11 {ECO:0000312|EMBL:AAF27000.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PRO-20.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22269056; DOI=10.1111/j.1365-313x.2012.04900.x;
RA Wang Z., Xu C., Benning C.;
RT "TGD4 involved in endoplasmic reticulum-to-chloroplast lipid trafficking is
RT a phosphatidic acid binding protein.";
RL Plant J. 70:614-623(2012).
RN [7]
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LYS-114; LYS-116; ARG-120;
RP SER-128; ARG-129; LYS-135; LYS-138; ASP-139 AND LYS-140.
RX PubMed=23297418; DOI=10.1074/jbc.m112.438986;
RA Wang Z., Anderson N.S., Benning C.;
RT "The phosphatidic acid binding site of the Arabidopsis
RT trigalactosyldiacylglycerol 4 (TGD4) protein required for lipid import into
RT chloroplasts.";
RL J. Biol. Chem. 288:4763-4771(2013).
RN [8]
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: Involved in lipid transfer from the endoplasmic reticulum
CC (ER) to plastids. Specifically binds phosphatidic acid (PtdOH).
CC {ECO:0000269|PubMed:18689504, ECO:0000269|PubMed:20410050,
CC ECO:0000269|PubMed:22269056, ECO:0000269|PubMed:23297418}.
CC -!- SUBUNIT: Homodimer. Forms dimeric beta-barrel (PubMed:23297418).
CC Interacts with TGD5 (PubMed:26410300). {ECO:0000269|PubMed:23297418,
CC ECO:0000269|PubMed:26410300}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:22269056}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:18689504}.
CC Note=According to PubMed:18689504 TGD4 localizes to the ER (GFP
CC experiment), but PubMed:22269056 found that TDG4 was located in the
CC chloroplast outer envelope using cell fractionation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M903-1; Sequence=Displayed;
CC -!- DOMAIN: Amino acids 110-145 are necessary and sufficient for
CC phosphatidic acid binding, while amino acids 1-80 are only necessary.
CC {ECO:0000269|PubMed:23297418}.
CC -!- DISRUPTION PHENOTYPE: Stunted, pale yellow and infertile plants, which
CC accumulate oligogalactoglycerolipids and phosphatidates.
CC {ECO:0000269|PubMed:18689504, ECO:0000269|PubMed:20410050,
CC ECO:0000269|PubMed:22269056}.
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DR EMBL; AC016827; AAF27000.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74480.1; -; Genomic_DNA.
DR EMBL; AF367275; AAK56264.1; -; mRNA.
DR EMBL; AY059159; AAL15384.1; -; mRNA.
DR RefSeq; NP_566296.1; NM_111576.5. [Q9M903-1]
DR AlphaFoldDB; Q9M903; -.
DR BioGRID; 5216; 1.
DR STRING; 3702.AT3G06960.1; -.
DR TCDB; 1.B.82.1.1; the chloroplast trigalactosyldiacylglycerol-4 porin (tgd4) family.
DR PaxDb; Q9M903; -.
DR PRIDE; Q9M903; -.
DR ProteomicsDB; 234229; -. [Q9M903-1]
DR DNASU; 819881; -.
DR EnsemblPlants; AT3G06960.1; AT3G06960.1; AT3G06960. [Q9M903-1]
DR GeneID; 819881; -.
DR Gramene; AT3G06960.1; AT3G06960.1; AT3G06960. [Q9M903-1]
DR KEGG; ath:AT3G06960; -.
DR Araport; AT3G06960; -.
DR TAIR; locus:2077562; AT3G06960.
DR eggNOG; ENOG502R4W6; Eukaryota.
DR HOGENOM; CLU_046616_0_0_1; -.
DR InParanoid; Q9M903; -.
DR OMA; IAWYSPK; -.
DR OrthoDB; 666397at2759; -.
DR PhylomeDB; Q9M903; -.
DR PRO; PR:Q9M903; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M903; baseline and differential.
DR Genevisible; Q9M903; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0034196; P:acylglycerol transport; IMP:TAIR.
DR GO; GO:1990052; P:ER to chloroplast lipid transport; IMP:TAIR.
DR InterPro; IPR044160; TGD4-like.
DR PANTHER; PTHR34954; PTHR34954; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Endoplasmic reticulum; Lipid transport;
KW Membrane; Plastid; Plastid outer membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..479
FT /note="Protein TRIGALACTOSYLDIACYLGLYCEROL 4,
FT chloroplastic"
FT /id="PRO_0000424527"
FT TRANSMEM 288..310
FT /evidence="ECO:0000255"
FT MUTAGEN 20
FT /note="P->L: In tgd4-1; accumulation of
FT trigalactosyldiacylglycerol (TGDG) in leaves and slightly
FT pale green phenotype."
FT /evidence="ECO:0000269|PubMed:18689504"
FT MUTAGEN 114
FT /note="K->A: No effect on phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:23297418"
FT MUTAGEN 116
FT /note="K->A: No effect on phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:23297418"
FT MUTAGEN 120
FT /note="R->A: No effect on phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:23297418"
FT MUTAGEN 128
FT /note="S->A: 40% decreased phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:23297418"
FT MUTAGEN 129
FT /note="R->A: 40% decreased phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:23297418"
FT MUTAGEN 135
FT /note="K->A: 40% decreased phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:23297418"
FT MUTAGEN 138
FT /note="K->A: 40% decreased phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:23297418"
FT MUTAGEN 139
FT /note="D->A: No effect on phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:23297418"
FT MUTAGEN 140
FT /note="K->A: No effect on phosphatidic acid binding."
FT /evidence="ECO:0000269|PubMed:23297418"
SQ SEQUENCE 479 AA; 52822 MW; 3546063EA2C5821A CRC64;
MNRMRWVGEG DIWDLDMSTP VTLEGTARAV PDDPLPLGLS RGTRLSRPKQ VEFFHRFMAS
PLIPSFSPIR PNTGDGGGGG FSLQRVLTLP FSNNWLVSLL GQFDVQRFVT EIDKTKAFGR
GSSSTVASRL NTIGKHLKDK SLYALGFCSE FLLSPDDTLL LSYDAYKGDL DKNPRAKAIF
NHEFPLHNLT AEAVWPGLFV DKHGEYWDVP LSMAIDLASL PAESGPSYHL CLHHNSGSPK
KLHSDTMEVP PPSLLPGLSL KSAVSYRTNM DLWRGTTPKL ETCKPYDVFL SSPHVAVSGI
IGSVMTAAFG ENSIRSKFEN DSEGVGGFSL HFPSVNSGFM ADALGRASLT AQYGNFQKFF
FDLTRFHARL DFPHGLRFLT GATSVAQDLL NSRQPSLEAF QKICPEVLVS LQQQIVGPFS
FKVESGIEID LRNGANPVTV DKTVFAIEYA LQVLLSAKAV VSYSPKQNEF MVELRFFET
