BPG2_ARATH
ID BPG2_ARATH Reviewed; 660 AA.
AC Q8W4I6; Q9M2M9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=GTP-binding protein BRASSINAZOLE INSENSITIVE PALE GREEN 2, chloroplastic {ECO:0000303|PubMed:19919572};
DE Short=Protein BRZ-INSENSITIVE-PALE GREEN 2 {ECO:0000303|PubMed:19919572};
DE Flags: Precursor;
GN Name=BPG2 {ECO:0000303|PubMed:19919572};
GN OrderedLocusNames=At3g57180 {ECO:0000312|Araport:AT3G57180};
GN ORFNames=F28O9.30 {ECO:0000312|EMBL:CAB68124.1};
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, DISRUPTION PHENOTYPE, INDUCTION BY LIGHT AND BRASSINAZOLE,
RP MUTAGENESIS OF 98-CYS--GLY-102; 242-CYS--CYS-245; 335-LYS--ASP-337;
RP 404-GLY-LYS-405; 431-THR-THR-432 AND 450-ASP--GLY-453, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19919572; DOI=10.1111/j.1365-313x.2009.04077.x;
RA Komatsu T., Kawaide H., Saito C., Yamagami A., Shimada S., Nakazawa M.,
RA Matsui M., Nakano A., Tsujimoto M., Natsume M., Abe H., Asami T.,
RA Nakano T.;
RT "The chloroplast protein BPG2 functions in brassinosteroid-mediated post-
RT transcriptional accumulation of chloroplast rRNA.";
RL Plant J. 61:409-422(2010).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=19889879; DOI=10.1104/pp.109.145318;
RA Mutwil M., Usadel B., Schuette M., Loraine A., Ebenhoeh O., Persson S.;
RT "Assembly of an interactive correlation network for the Arabidopsis genome
RT using a novel heuristic clustering algorithm.";
RL Plant Physiol. 152:29-43(2010).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY LIGHT, SUBCELLULAR LOCATION,
RP INTERACTION WITH 16S AND 23S RIBOSOMAL RNAS, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=22526496; DOI=10.1007/s00425-012-1638-6;
RA Kim B.H., Malec P., Waloszek A., von Arnim A.G.;
RT "Arabidopsis BPG2: a phytochrome-regulated gene whose protein product binds
RT to plastid ribosomal RNAs.";
RL Planta 236:677-690(2012).
CC -!- FUNCTION: Required for brassinosteroid- (BR) mediated post-
CC transcriptional and translational regulation in the chloroplast,
CC including accumulation of chloroplast rRNA (PubMed:19919572). Involved
CC in chloroplast differentiation (PubMed:19919572, PubMed:22526496).
CC {ECO:0000269|PubMed:19919572, ECO:0000269|PubMed:22526496}.
CC -!- SUBUNIT: Binds to chloroplast 16S and 23S ribosomal RNAs.
CC {ECO:0000269|PubMed:22526496}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19919572, ECO:0000269|PubMed:22526496}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, petioles, leaves and
CC flowers and, at low levels, also in roots.
CC {ECO:0000269|PubMed:19919572, ECO:0000269|PubMed:22526496}.
CC -!- INDUCTION: Induced by light, but repressed by dark (PubMed:19919572,
CC PubMed:22526496). Up-regulated by the specific inhibitor of the
CC biosynthesis of brassinosteroids (BRs) brassinazole (Brz)
CC (PubMed:19919572). {ECO:0000269|PubMed:19919572,
CC ECO:0000269|PubMed:22526496}.
CC -!- DISRUPTION PHENOTYPE: Chlorotic dwarf mutant pale green in bpg2-1 and
CC bpg2-2 (PubMed:19919572, PubMed:19889879, PubMed:22526496). Reduced
CC sensitivity in the light to chlorophyll accumulation promoted by
CC brassinazole (Brz), a specific inhibitor of the biosynthesis of
CC brassinosteroids (BRs), via the suppression of Brz-induced chloroplast
CC protein accumulation. Decreased number of stacked grana thylakoids in
CC chloroplast, but more starch grains, and more and larger
CC plastoglobules. Abnormal accumulation of precursors of chloroplast 16S
CC and 23S rRNA (PubMed:19919572). Reduced level of chlorophyll and
CC carotenoid pigmentation in plastids leading to defective photosystem II
CC and altered photosystem I functions (PubMed:22526496).
CC {ECO:0000269|PubMed:19889879, ECO:0000269|PubMed:19919572,
CC ECO:0000269|PubMed:22526496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB68124.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL137080; CAB68124.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79624.2; -; Genomic_DNA.
DR EMBL; AY062540; AAL32618.1; -; mRNA.
DR EMBL; BT003368; AAO29986.1; -; mRNA.
DR PIR; T45796; T45796.
DR RefSeq; NP_191277.5; NM_115578.5.
DR AlphaFoldDB; Q8W4I6; -.
DR SMR; Q8W4I6; -.
DR STRING; 3702.AT3G57180.1; -.
DR PaxDb; Q8W4I6; -.
DR PeptideAtlas; Q8W4I6; -.
DR PRIDE; Q8W4I6; -.
DR ProteomicsDB; 240736; -.
DR DNASU; 824885; -.
DR GeneID; 824885; -.
DR KEGG; ath:AT3G57180; -.
DR Araport; AT3G57180; -.
DR TAIR; locus:2082558; AT3G57180.
DR eggNOG; KOG1249; Eukaryota.
DR HOGENOM; CLU_415977_0_0_1; -.
DR InParanoid; Q8W4I6; -.
DR OrthoDB; 612803at2759; -.
DR PRO; PR:Q8W4I6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8W4I6; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:1901259; P:chloroplast rRNA processing; IMP:UniProtKB.
DR GO; GO:0032502; P:developmental process; IMP:TAIR.
DR GO; GO:1904143; P:positive regulation of carotenoid biosynthetic process; IMP:UniProtKB.
DR GO; GO:1902326; P:positive regulation of chlorophyll biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0009741; P:response to brassinosteroid; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Brassinosteroid signaling pathway; Chloroplast; GTP-binding; Hydrolase;
KW Nucleotide-binding; Plastid; Reference proteome; RNA-binding;
KW rRNA processing; rRNA-binding; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..660
FT /note="GTP-binding protein BRASSINAZOLE INSENSITIVE PALE
FT GREEN 2, chloroplastic"
FT /id="PRO_0000435523"
FT DOMAIN 273..457
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 127..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..158
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 98..102
FT /note="CPGCG->APAAA: Pale green and unable to complement
FT the bpg2-1 mutant."
FT /evidence="ECO:0000269|PubMed:19919572"
FT MUTAGEN 242..245
FT /note="CARC->AAAA: Pale green and unable to complement the
FT bpg2-1 mutant."
FT /evidence="ECO:0000269|PubMed:19919572"
FT MUTAGEN 335..337
FT /note="KVD->AVA: Pale green and unable to complement the
FT bpg2-1 mutant."
FT /evidence="ECO:0000269|PubMed:19919572"
FT MUTAGEN 404..405
FT /note="GK->AA: Pale green and unable to complement the
FT bpg2-1 mutant."
FT /evidence="ECO:0000269|PubMed:19919572"
FT MUTAGEN 431..432
FT /note="TT->AA: Pale green and unable to complement the
FT bpg2-1 mutant."
FT /evidence="ECO:0000269|PubMed:19919572"
FT MUTAGEN 450..453
FT /note="DTPG->ATPA: Pale green and unable to complement the
FT bpg2-1 mutant."
FT /evidence="ECO:0000269|PubMed:19919572"
SQ SEQUENCE 660 AA; 73087 MW; E4242B0CD807BD5A CRC64;
MVVLISSTVT ICNVKPKLED GNFRVSRLIH RPEVPFFSGL SNEKKKKCAV SVMCLAVKKE
QVVQSVESVN GTIFPKKSKN LIMSEGRDED EDYGKIICPG CGIFMQDNDP DLPGYYQKRK
VIANNLEGDE HVENDELAGF EMVDDDADEE EEGEDDEMDD EIKNAIEGSN SESESGFEWE
SDEWEEKKEV NDVELDGFAP AGVGYGNVTE EKEKKKRVSK TERKKIAREE AKKDNYDDVT
VCARCHSLRN YGQVKNQAAE NLLPDFDFDR LISTRLIKPM SNSSTTVVVM VVDCVDFDGS
FPKRAAKSLF QVLQKAENDP KGSKNLPKLV LVATKVDLLP TQISPARLDR WVRHRAKAGG
APKLSGVYMV SARKDIGVKN LLAYIKELAG PRGNVWVIGA QNAGKSTLIN ALSKKDGAKV
TRLTEAPVPG TTLGILKIGG ILSAKAKMYD TPGLLHPYLM SLRLNSEERK MVEIRKEVQP
RSYRVKAGQS VHIGGLVRLD LVSASVETIY ITIWASHSVS LHLGKTENAE EIFKGHSGLR
LQPPIGENRA SELGTWEEKE IQVSGNSWDV KSIDISVAGL GWLSLGLKGA ATLALWTYQG
IDVTLREPLV IDRAPYLERP GFWLPKAITE VLGTHSSKLV DARRRKKQQD STDFLSDSVA
