RBCX1_ARATH
ID RBCX1_ARATH Reviewed; 174 AA.
AC Q94AU9; Q9XEA2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Chaperonin-like RBCX protein 1, chloroplastic {ECO:0000303|PubMed:21922322};
DE Short=AtRBCX1 {ECO:0000303|PubMed:21922322};
DE Flags: Precursor;
GN Name=RBCX1 {ECO:0000303|PubMed:21922322};
GN OrderedLocusNames=At4g04330 {ECO:0000312|Araport:AT4G04330};
GN ORFNames=T19B17.5 {ECO:0000312|EMBL:AAD36948.1};
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 {ECO:0000312|EMBL:AAK76456.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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, PROTEIN SEQUENCE OF 46-50, INTERACTION WITH
RP RBCL; THI1 AND ATPB, AND INDUCTION BY DESICCATION AND SALT.
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 [5] {ECO:0007744|PDB:4GR2}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 47-174, SUBUNIT, AND MUTAGENESIS
RP OF CYS-108 AND CYS-133.
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 THI1 (PubMed:21922322). {ECO:0000269|PubMed:21922322,
CC ECO:0000269|PubMed:23295968}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21922322}. Note=Associated with the thylakoid
CC membranes. {ECO:0000269|PubMed:21922322}.
CC -!- INDUCTION: Up-regulated by salt and desiccation.
CC {ECO:0000269|PubMed:21922322}.
CC -!- SIMILARITY: Belongs to the RbcX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD36948.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77901.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF069441; AAD36948.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161500; CAB77901.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82379.1; -; Genomic_DNA.
DR EMBL; AY045782; AAK76456.1; -; mRNA.
DR EMBL; AY142573; AAN13142.1; -; mRNA.
DR PIR; G85054; G85054.
DR RefSeq; NP_567263.1; NM_116671.3.
DR PDB; 4GR2; X-ray; 2.00 A; A/B=47-174.
DR PDBsum; 4GR2; -.
DR AlphaFoldDB; Q94AU9; -.
DR SMR; Q94AU9; -.
DR IntAct; Q94AU9; 2.
DR STRING; 3702.AT4G04330.1; -.
DR iPTMnet; Q94AU9; -.
DR PaxDb; Q94AU9; -.
DR PRIDE; Q94AU9; -.
DR ProteomicsDB; 236568; -.
DR EnsemblPlants; AT4G04330.1; AT4G04330.1; AT4G04330.
DR GeneID; 825753; -.
DR Gramene; AT4G04330.1; AT4G04330.1; AT4G04330.
DR KEGG; ath:AT4G04330; -.
DR Araport; AT4G04330; -.
DR TAIR; locus:2134877; AT4G04330.
DR eggNOG; ENOG502RZSC; Eukaryota.
DR HOGENOM; CLU_125191_0_0_1; -.
DR InParanoid; Q94AU9; -.
DR OMA; NKMYVPG; -.
DR OrthoDB; 1615024at2759; -.
DR PhylomeDB; Q94AU9; -.
DR PRO; PR:Q94AU9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94AU9; baseline and differential.
DR GO; GO:0009534; C:chloroplast thylakoid; 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:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
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..45
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:21922322"
FT CHAIN 46..174
FT /note="Chaperonin-like RBCX protein 1, chloroplastic"
FT /id="PRO_0000437958"
FT MUTAGEN 108
FT /note="C->L: No effect on rbcL binding; when associated
FT with A-133."
FT /evidence="ECO:0000269|PubMed:23295968"
FT MUTAGEN 133
FT /note="C->A: No effect on rbcL binding; when associated
FT with L-108."
FT /evidence="ECO:0000269|PubMed:23295968"
FT HELIX 57..84
FT /evidence="ECO:0007829|PDB:4GR2"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:4GR2"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4GR2"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:4GR2"
FT HELIX 116..135
FT /evidence="ECO:0007829|PDB:4GR2"
FT HELIX 139..162
FT /evidence="ECO:0007829|PDB:4GR2"
SQ SEQUENCE 174 AA; 20199 MW; EDDB4FE3F88DCB08 CRC64;
MESSSSLLHH SYLSYLNPKF GKRPLVSYPL MQSSRKCKQT RICSNKMYVP GFGEASPEAK
AAKHLHDFFT YVAVRIVSAQ LESYNPEAYM ELREFLDTNS VSDGDKFCAT LMRRSSRHMN
LALRILEVRS AYCKNDFEWD NMKRLAFKNV DDSNTRLMRE YVLETSHVET DSDK
