RBCX2_ARATH
ID RBCX2_ARATH Reviewed; 203 AA.
AC Q8L9X2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Chaperonin-like RbcX protein 2, chloroplastic {ECO:0000303|PubMed:21922322};
DE Short=AtRBCX2 {ECO:0000303|PubMed:21922322};
DE Flags: Precursor;
GN Name=RBCX2 {ECO:0000303|PubMed:21922322};
GN OrderedLocusNames=At5g19855 {ECO:0000312|Araport:AT5G19855};
GN ORFNames=F28I16 {ECO:0000312|EMBL:AF296836},
GN T29J13 {ECO:0000312|EMBL:AF296838};
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 {ECO:0000312|EMBL:AAM65713.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, SUBCELLULAR LOCATION, PROTEIN SEQUENCE OF 79-83, INTERACTION WITH
RP RBCL; THI1 AND RBCS-1B, AND LACK OF INDUCTION BY STRESS.
RX PubMed=21922322; DOI=10.1007/s11103-011-9823-8;
RA Kolesinski P., Piechota J., Szczepaniak A.;
RT "Initial characteristics of RbcX proteins from Arabidopsis thaliana.";
RL Plant Mol. Biol. 77:447-459(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 79-203, SUBUNIT, AND MUTAGENESIS
RP OF CYS-168.
RX PubMed=23295968; DOI=10.1016/j.bbagen.2012.12.025;
RA Kolesinski P., Golik P., Grudnik P., Piechota J., Markiewicz M.,
RA Tarnawski M., Dubin G., Szczepaniak A.;
RT "Insights into eukaryotic Rubisco assembly - crystal structures of RbcX
RT chaperones from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1830:2899-2906(2013).
CC -!- FUNCTION: Chaperone involved in RuBisCO assembly process.
CC {ECO:0000269|PubMed:21922322}.
CC -!- SUBUNIT: Homodimer (PubMed:23295968). Interacts with rbcL, atpB and
CC RBCS-1B (PubMed:21922322). {ECO:0000269|PubMed:21922322,
CC ECO:0000269|PubMed:23295968}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:21922322}.
CC -!- INDUCTION: Not regulated by cold, salt or desiccation.
CC {ECO:0000269|PubMed:21922322}.
CC -!- SIMILARITY: Belongs to the RbcX family. {ECO:0000305}.
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DR EMBL; AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF296838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92757.1; -; Genomic_DNA.
DR EMBL; BT004014; AAO42050.1; -; mRNA.
DR EMBL; BT005149; AAO50682.1; -; mRNA.
DR EMBL; AY088169; AAM65713.1; -; mRNA.
DR RefSeq; NP_568382.1; NM_121991.4.
DR PDB; 4GR6; X-ray; 2.00 A; A/B=79-203.
DR PDBsum; 4GR6; -.
DR AlphaFoldDB; Q8L9X2; -.
DR SMR; Q8L9X2; -.
DR STRING; 3702.AT5G19855.1; -.
DR PaxDb; Q8L9X2; -.
DR PRIDE; Q8L9X2; -.
DR ProteomicsDB; 225958; -.
DR EnsemblPlants; AT5G19855.1; AT5G19855.1; AT5G19855.
DR GeneID; 832106; -.
DR Gramene; AT5G19855.1; AT5G19855.1; AT5G19855.
DR KEGG; ath:AT5G19855; -.
DR Araport; AT5G19855; -.
DR TAIR; locus:505006621; AT5G19855.
DR eggNOG; ENOG502QRY0; Eukaryota.
DR HOGENOM; CLU_092281_1_0_1; -.
DR InParanoid; Q8L9X2; -.
DR OMA; YEDTFHD; -.
DR OrthoDB; 1107038at2759; -.
DR PhylomeDB; Q8L9X2; -.
DR PRO; PR:Q8L9X2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L9X2; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0044183; F:protein folding chaperone; IDA:TAIR.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:TAIR.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IEA:InterPro.
DR Gene3D; 1.10.1200.210; -; 1.
DR InterPro; IPR038052; Chaperonin_RbcX_sf.
DR InterPro; IPR003435; Chaperonin_RcbX.
DR PANTHER; PTHR33791; PTHR33791; 1.
DR Pfam; PF02341; RbcX; 1.
DR SUPFAM; SSF158615; SSF158615; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbon dioxide fixation; Chaperone; Chloroplast;
KW Direct protein sequencing; Photosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..78
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:21922322"
FT CHAIN 79..203
FT /note="Chaperonin-like RbcX protein 2, chloroplastic"
FT /id="PRO_0000437959"
FT MUTAGEN 168
FT /note="C->A: No effect on rbcL binding."
FT /evidence="ECO:0000269|PubMed:23295968"
FT HELIX 90..115
FT /evidence="ECO:0007829|PDB:4GR6"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:4GR6"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4GR6"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:4GR6"
FT HELIX 147..167
FT /evidence="ECO:0007829|PDB:4GR6"
FT HELIX 170..189
FT /evidence="ECO:0007829|PDB:4GR6"
SQ SEQUENCE 203 AA; 23476 MW; C84E24AF978FCBA2 CRC64;
MVSAWFVVGS PVMDSSSSPC LCLDAHTTGT IRRKKILGKA RNLELGSSFT GSRIVFRLSP
KRVSRIANRK SKKLLIVNED VAGNYDDTFG DVQKQIVNYF TYKAVRTVLH QLYEMNPPQY
TWFYNHIITN RPTDGKRFLR ALGKESQELA ERVMITRLHL YGKWIKKCDH GKIYQEISDE
NLALMRERLM ETVIWPSDDT NSR
