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 17-JUN-2020, entry version 167. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 eggNOG; COG1222; LUCA. 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; IDA:TAIR. DR GO; GO:0005618; C:cell wall; IDA:TAIR. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR. DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0010287; C:plastoglobule; IDA:TAIR. DR GO; GO:0010319; C:stromule; IDA:TAIR. DR GO; GO:0009579; C:thylakoid; IDA:TAIR. DR GO; GO:0043531; F:ADP binding; IDA:TAIR. DR GO; GO:0005524; F:ATP binding; IDA:TAIR. DR GO; GO:0030234; F:enzyme regulator activity; IDA:TAIR. DR GO; GO:0046863; F:ribulose-1,5-bisphosphate carboxylase/oxygenase activator activity; IDA:TAIR. DR GO; GO:0042742; P:defense response to bacterium; IEP: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 InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR027417; P-loop_NTPase. 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 NP_BIND 165..172 FT /note="ATP" 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:0000244|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:0000244|PDB:4W5W" FT STRAND 159..164 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 171..181 FT /evidence="ECO:0000244|PDB:4W5W" FT STRAND 187..190 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 204..218 FT /evidence="ECO:0000244|PDB:4W5W" FT STRAND 225..227 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 241..253 FT /evidence="ECO:0000244|PDB:4W5W" FT STRAND 255..257 FT /evidence="ECO:0000244|PDB:4W5W" FT STRAND 280..286 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 292..297 FT /evidence="ECO:0000244|PDB:4W5W" FT STRAND 299..304 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 309..319 FT /evidence="ECO:0000244|PDB:4W5W" FT STRAND 321..324 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 327..336 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 342..364 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 366..368 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 369..373 FT /evidence="ECO:0000244|PDB:4W5W" FT STRAND 376..378 FT /evidence="ECO:0000244|PDB:4W5W" FT HELIX 390..414 FT /evidence="ECO:0000244|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 //