RCA_ARATH
ID RCA_ARATH Reviewed; 474 AA.
AC P10896; Q39197; Q39198; Q8H172; Q940T8; Q941B7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic;
DE Short=RA;
DE Short=RuBisCO activase;
DE Flags: Precursor;
GN Name=RCA; OrderedLocusNames=At2g39730; ORFNames=T5I7.3;
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 [MRNA].
RC TISSUE=Leaf;
RX PubMed=2717419; DOI=10.1093/nar/17.7.2871;
RA Werneke J.M., Ogren W.L.;
RT "Structure of an Arabidopsis thaliana cDNA encoding rubisco activase.";
RL Nucleic Acids Res. 17:2871-2871(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8108496; DOI=10.1104/pp.102.1.227;
RA Orozco B.M., McClung C.R., Werneke J.M., Ogren W.L.;
RT "Molecular basis of the ribulose-1,5-bisphosphate carboxylase/oxygenase
RT activase mutation in Arabidopsis thaliana is a guanine-to-adenine
RT transition at the 5'-splice junction of intron 3.";
RL Plant Physiol. 102:227-232(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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 [6]
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 [7]
RP ALTERNATIVE SPLICING.
RX PubMed=2535524; DOI=10.2307/3868990;
RA Werneke J.M., Chatfield J.M., Ogren W.L.;
RT "Alternative mRNA splicing generates the two ribulosebisphosphate
RT carboxylase/oxygenase activase polypeptides in spinach and Arabidopsis.";
RL Plant Cell 1:815-825(1989).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=16461379; DOI=10.1104/pp.105.076083;
RA Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT surprising site for differential accumulation of metabolic enzymes.";
RL Plant Physiol. 140:984-997(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [13]
RP IDENTIFICATION BY MASS 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 [14]
RP PHOSPHORYLATION AT THR-78.
RX PubMed=27064346; DOI=10.3389/fpls.2016.00404;
RA Kim S.Y., Bender K.W., Walker B.J., Zielinski R.E., Spalding M.H.,
RA Ort D.R., Huber S.C.;
RT "The plastid casein kinase 2 phosphorylates Rubisco activase at the Thr-78
RT Site but is not essential for regulation of Rubisco activation state.";
RL Front. Plant Sci. 7:404-404(2016).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 59-437.
RX PubMed=25849391; DOI=10.1107/s1399004715001182;
RA Hasse D., Larsson A.M., Andersson I.;
RT "Structure of Arabidopsis thaliana Rubisco activase.";
RL Acta Crystallogr. D 71:800-808(2015).
CC -!- FUNCTION: Activation of RuBisCO (ribulose-1,5-bisphosphate
CC carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent
CC carboxylation of the epsilon-amino group of lysine leading to a
CC carbamate structure.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid,
CC chloroplast, plastoglobule {ECO:0000269|PubMed:16461379}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P10896-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P10896-2; Sequence=VSP_005539;
CC -!- PTM: Phosphorylated at Thr-78 by CK2. {ECO:0000269|PubMed:27064346}.
CC -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000305}.
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DR EMBL; X14212; CAA32429.1; -; mRNA.
DR EMBL; M86720; AAA20202.1; -; Genomic_DNA.
DR EMBL; M86720; AAA20203.1; -; Genomic_DNA.
DR EMBL; AC003000; AAB87122.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09714.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09715.1; -; Genomic_DNA.
DR EMBL; AY052703; AAK96607.1; -; mRNA.
DR EMBL; AF325049; AAG40401.1; -; mRNA.
DR EMBL; AY052290; AAK96483.1; -; mRNA.
DR EMBL; AY056108; AAL06995.1; -; mRNA.
DR EMBL; BT000613; AAN18180.1; -; mRNA.
DR EMBL; BT000710; AAN31853.1; -; mRNA.
DR EMBL; AY088487; AAM66023.1; -; mRNA.
DR PIR; S04048; S04048.
DR PIR; T01002; T01002.
DR PIR; T01003; T01003.
DR RefSeq; NP_565913.1; NM_129531.3. [P10896-1]
DR RefSeq; NP_850320.1; NM_179989.3. [P10896-2]
DR PDB; 4W5W; X-ray; 2.90 A; A=59-437.
DR PDBsum; 4W5W; -.
DR AlphaFoldDB; P10896; -.
DR SMR; P10896; -.
DR BioGRID; 3896; 3.
DR IntAct; P10896; 2.
DR MINT; P10896; -.
DR STRING; 3702.AT2G39730.1; -.
DR iPTMnet; P10896; -.
DR MetOSite; P10896; -.
DR SWISS-2DPAGE; P10896; -.
DR World-2DPAGE; 0003:P10896; -.
DR PaxDb; P10896; -.
DR PRIDE; P10896; -.
DR ProteomicsDB; 236535; -. [P10896-1]
DR EnsemblPlants; AT2G39730.1; AT2G39730.1; AT2G39730. [P10896-1]
DR EnsemblPlants; AT2G39730.2; AT2G39730.2; AT2G39730. [P10896-2]
DR GeneID; 818558; -.
DR Gramene; AT2G39730.1; AT2G39730.1; AT2G39730. [P10896-1]
DR Gramene; AT2G39730.2; AT2G39730.2; AT2G39730. [P10896-2]
DR KEGG; ath:AT2G39730; -.
DR Araport; AT2G39730; -.
DR TAIR; locus:2063922; AT2G39730.
DR eggNOG; KOG0651; Eukaryota.
DR HOGENOM; CLU_038420_0_0_1; -.
DR InParanoid; P10896; -.
DR OrthoDB; 655049at2759; -.
DR PhylomeDB; P10896; -.
DR PRO; PR:P10896; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P10896; baseline and differential.
DR Genevisible; P10896; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; IEA:UniProtKB-SubCell.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0043531; F:ADP binding; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IDA:TAIR.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0046863; F:ribulose-1,5-bisphosphate carboxylase/oxygenase activator activity; IDA:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044960; RCA-like.
DR PANTHER; PTHR32429; PTHR32429; 1.
DR Pfam; PF00004; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chloroplast;
KW Nucleotide-binding; Phosphoprotein; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT CHAIN 59..474
FT /note="Ribulose bisphosphate carboxylase/oxygenase
FT activase, chloroplastic"
FT /id="PRO_0000030228"
FT BINDING 165..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 78
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:27064346"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT VAR_SEQ 439..474
FT /note="GAQQVNLPVPEGCTDPVAENFDPTARSDDGTCVYNF -> TEEKEPSK (in
FT isoform Short)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_005539"
FT CONFLICT 163..164
FT /note="IW -> SR (in Ref. 1; CAA32429)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..203
FT /note="PA -> VR (in Ref. 1; CAA32429)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="F -> L (in Ref. 5; AAN18180)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="A -> G (in Ref. 1; CAA32429)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="R -> L (in Ref. 1; CAA32429)"
FT /evidence="ECO:0000305"
FT CONFLICT 304..306
FT /note="YWA -> LTG (in Ref. 1; CAA32429)"
FT /evidence="ECO:0000305"
FT CONFLICT 316..317
FT /note="CK -> W (in Ref. 1; CAA32429)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="G -> D (in Ref. 5; AAN18180/AAK96483)"
FT /evidence="ECO:0000305"
FT CONFLICT 441..442
FT /note="QQ -> HE (in Ref. 1; CAA32429)"
FT /evidence="ECO:0000305"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:4W5W"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:4W5W"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:4W5W"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:4W5W"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:4W5W"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:4W5W"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:4W5W"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 342..364
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:4W5W"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:4W5W"
FT HELIX 390..414
FT /evidence="ECO:0007829|PDB:4W5W"
SQ SEQUENCE 474 AA; 51981 MW; 4AD07691E1892A4F CRC64;
MAAAVSTVGA INRAPLSLNG SGSGAVSAPA STFLGKKVVT VSRFAQSNKK SNGSFKVLAV
KEDKQTDGDR WRGLAYDTSD DQQDITRGKG MVDSVFQAPM GTGTHHAVLS SYEYVSQGLR
QYNLDNMMDG FYIAPAFMDK LVVHITKNFL TLPNIKVPLI LGIWGGKGQG KSFQCELVMA
KMGINPIMMS AGELESGNAG EPAKLIRQRY REAADLIKKG KMCCLFINDL DAGAGRMGGT
TQYTVNNQMV NATLMNIADN PTNVQLPGMY NKEENARVPI ICTGNDFSTL YAPLIRDGRM
EKFYWAPTRE DRIGVCKGIF RTDKIKDEDI VTLVDQFPGQ SIDFFGALRA RVYDDEVRKF
VESLGVEKIG KRLVNSREGP PVFEQPEMTY EKLMEYGNML VMEQENVKRV QLAETYLSQA
ALGDANADAI GRGTFYGKGA QQVNLPVPEG CTDPVAENFD PTARSDDGTC VYNF
