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   27-MAR-2024, entry version 119.
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}, T29J13
GN   {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.Q8L9X2; -.
DR   PaxDb; 3702-AT5G19855-1; -.
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; AT5G19855; RBCX2.
DR   eggNOG; ENOG502QRY0; Eukaryota.
DR   HOGENOM; CLU_092281_1_0_1; -.
DR   InParanoid; Q8L9X2; -.
DR   OMA; YEDTFHD; -.
DR   OrthoDB; 295972at2759; -.
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; Chaperonin-like RbcX; 1.
DR   InterPro; IPR038052; Chaperonin_RbcX_sf.
DR   InterPro; IPR003435; Chaperonin_RcbX.
DR   PANTHER; PTHR33791; CHAPERONIN-LIKE RBCX PROTEIN 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR33791:SF1; CHAPERONIN-LIKE RBCX PROTEIN 2, CHLOROPLASTIC; 1.
DR   Pfam; PF02341; RbcX; 1.
DR   SUPFAM; SSF158615; RbcX-like; 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
//