ID PLGG1_ARATH Reviewed; 512 AA.
AC Q9FVQ4; Q8LAS5;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Plastidal glycolate/glycerate translocator 1, chloroplastic;
DE AltName: Full=Bacterial membrane protein LrgB-like protein;
DE Short=AtLrgB;
DE Flags: Precursor;
GN Name=PLGG1; OrderedLocusNames=At1g32080; ORFNames=F3C3.12, T12O21.2;
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 [LARGE SCALE MRNA].
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 [5]
RP ACETYLATION AT ALA-77, CLEAVAGE OF TRANSIT PEPTIDE AFTER GLN-76,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-77, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER GLN-76, 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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21916894; DOI=10.1111/j.1469-8137.2011.03867.x;
RA Yang Y., Jin H., Chen Y., Lin W., Wang C., Chen Z., Han N., Bian H.,
RA Zhu M., Wang J.;
RT "A chloroplast envelope membrane protein containing a putative LrgB domain
RT related to the control of bacterial death and lysis is required for
RT chloroplast development in Arabidopsis thaliana.";
RL New Phytol. 193:81-95(2012).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22180599; DOI=10.1093/pcp/pcr180;
RA Yamaguchi M., Takechi K., Myouga F., Imura S., Sato H., Takio S.,
RA Shinozaki K., Takano H.;
RT "Loss of the plastid envelope protein AtLrgB causes spontaneous chlorotic
RT cell death in Arabidopsis thaliana.";
RL Plant Cell Physiol. 53:125-134(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23382251; DOI=10.1073/pnas.1215142110;
RA Pick T.R., Braeutigam A., Schulz M.A., Obata T., Fernie A.R., Weber A.P.;
RT "PLGG1, a plastidic glycolate glycerate transporter, is required for
RT photorespiration and defines a unique class of metabolite transporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3185-3190(2013).
CC -!- FUNCTION: Glycolate/glycerate transporter required for
CC photorespiration. {ECO:0000269|PubMed:21916894,
CC ECO:0000269|PubMed:22180599, ECO:0000269|PubMed:23382251}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000305|PubMed:12766230, ECO:0000305|PubMed:23382251}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:12766230,
CC ECO:0000305|PubMed:23382251}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers, but not in
CC roots. {ECO:0000269|PubMed:21916894, ECO:0000269|PubMed:22180599}.
CC -!- DISRUPTION PHENOTYPE: Interveinal chlorotic and premature necrotic
CC leaves. Bleached leaf phenotype when grown under ambient air, but
CC normal growth under CO(2)-enriched air. {ECO:0000269|PubMed:21916894,
CC ECO:0000269|PubMed:23382251}.
CC -!- SIMILARITY: Belongs to the CidB/LrgB family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to be involved in chloroplast
CC development or function against cell death (PubMed:21916894,
CC PubMed:22180599). {ECO:0000305}.
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DR EMBL; AC074309; AAG50795.1; -; Genomic_DNA.
DR EMBL; AC084165; AAG23435.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31434.1; -; Genomic_DNA.
DR EMBL; AY039880; AAK63984.1; -; mRNA.
DR EMBL; AY101515; AAM26636.1; -; mRNA.
DR EMBL; AY087643; AAM65181.1; -; mRNA.
DR PIR; B86445; B86445.
DR RefSeq; NP_564388.1; NM_102942.4.
DR AlphaFoldDB; Q9FVQ4; -.
DR BioGRID; 25334; 1.
DR STRING; 3702.Q9FVQ4; -.
DR TCDB; 2.A.122.2.1; the lrgb/cidb holin-like glycolate/glycerate transporter (lrgb/cidb/ggt) family.
DR iPTMnet; Q9FVQ4; -.
DR PaxDb; 3702-AT1G32080-1; -.
DR ProteomicsDB; 234917; -.
DR EnsemblPlants; AT1G32080.1; AT1G32080.1; AT1G32080.
DR GeneID; 840100; -.
DR Gramene; AT1G32080.1; AT1G32080.1; AT1G32080.
DR KEGG; ath:AT1G32080; -.
DR Araport; AT1G32080; -.
DR TAIR; AT1G32080; LRGB.
DR eggNOG; ENOG502QQ63; Eukaryota.
DR HOGENOM; CLU_036862_1_0_1; -.
DR InParanoid; Q9FVQ4; -.
DR OMA; ASGIKIC; -.
DR OrthoDB; 938810at2759; -.
DR PhylomeDB; Q9FVQ4; -.
DR PRO; PR:Q9FVQ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FVQ4; baseline and differential.
DR Genevisible; Q9FVQ4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:UniProtKB.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:1901974; F:glycerate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0043879; F:glycolate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0042631; P:cellular response to water deprivation; IMP:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:1901975; P:glycerate transmembrane transport; IMP:UniProtKB.
DR GO; GO:0097339; P:glycolate transmembrane transport; IMP:UniProtKB.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0009853; P:photorespiration; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR InterPro; IPR007300; CidB/LrgB.
DR PANTHER; PTHR30249:SF0; PLASTIDAL GLYCOLATE_GLYCERATE TRANSLOCATOR 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR30249; PUTATIVE SEROTONIN TRANSPORTER; 1.
DR Pfam; PF04172; LrgB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; Membrane; Photorespiration; Plastid;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..76
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:12766230,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 77..512
FT /note="Plastidal glycolate/glycerate translocator 1,
FT chloroplastic"
FT /id="PRO_0000422096"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 77
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12766230,
FT ECO:0007744|PubMed:22223895"
FT CONFLICT 26
FT /note="K -> N (in Ref. 4; AAM65181)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 54017 MW; 12C1482190E69FED CRC64;
MATLLATPIF SPLASSPARN RLSCSKIRFG SKNGKILNSD GAQKLNLSKF RKPDGQRFLQ
MGSSKEMNFE RKLSVQAMDG AGTGNTSTIS RNVIAISHLL VSLGIILAAD YFLKQAFVAA
SIKFPSALFG MFCIFSVLMI FDSVVPAAAN GLMNFFEPAF LFIQRWLPLF YVPSLVVLPL
SVRDIPAASG VKICYIVAGG WLASLCVAGY TAIAVRKMVK TEMTEAEPMA KPSPFSTLEL
WSWSGIFVVS FVGALFYPNS LGTSARTSLP FLLSSTVLGY IVGSGLPSSI KKVFHPIICC
ALSAVLAALA FGYASGSGLD PVLGNYLTKV ASDPGAGDIL MGFLGSVILS FAFSMFKQRK
LVKRHAAEIF TSVIVSTVFS LYSTALVGRL VGLEPSLTVS ILPRCITVAL ALSIVSLFEG
TNSSLTAAVV VVTGLIGANF VQVVLDKLRL RDPIARGIAT ASSAHGLGTA ALSAKEPEAL
PFCAIAYALT GIFGSLLCSV PAVRQSLLAV VG
//
