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 28-FEB-2018, entry version 157. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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 RT 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 RT carboxylase/oxygenase activase mutation in Arabidopsis thaliana is a RT guanine-to-adenine 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., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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=10.1105/tpc.1.8.815; 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 RT Arabidopsis."; RL Plant Cell 1:815-825(1989). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE RP SCALE 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 RP SCALE 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. RT A surprising site for differential accumulation of metabolic RT 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., RA Andreasson E., Rathjen J.P., Peck S.C.; RT "Phosphoproteomic analysis of nuclei-enriched fractions from RT Arabidopsis 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 RP BY 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 RT using polyethylene glycol fractionation, immobilized metal-ion RT affinity 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., RA Meinnel T., 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 RT Thr-78 Site but is not essential for regulation of Rubisco activation RT 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. CC {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 UniGene; At.25263; -. DR UniGene; At.25299; -. DR UniGene; At.25319; -. DR UniGene; At.47493; -. DR PDB; 4W5W; X-ray; 2.90 A; A=59-437. DR PDBsum; 4W5W; -. DR ProteinModelPortal; P10896; -. DR SMR; P10896; -. DR BioGrid; 3896; 3. DR IntAct; P10896; 2. DR MINT; P10896; -. DR STRING; 3702.AT2G39730.1; -. DR iPTMnet; P10896; -. DR SWISS-2DPAGE; P10896; -. DR World-2DPAGE; 0003:P10896; -. DR PaxDb; P10896; -. DR PRIDE; P10896; -. 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; HOG000243931; -. DR InParanoid; P10896; -. DR OMA; HGRKGEG; -. DR OrthoDB; EOG09360DH8; -. 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:0016020; C:membrane; IDA: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 Complete proteome; Nucleotide-binding; Phosphoprotein; Plastid; KW Reference proteome; Transit peptide. FT TRANSIT 1 58 Chloroplast. FT CHAIN 59 474 Ribulose bisphosphate FT carboxylase/oxygenase activase, FT chloroplastic. FT /FTId=PRO_0000030228. FT NP_BIND 165 172 ATP. {ECO:0000255}. FT MOD_RES 78 78 Phosphothreonine; by CK2. FT {ECO:0000269|PubMed:27064346}. FT MOD_RES 283 283 Phosphothreonine. FT {ECO:0000244|PubMed:22092075}. FT VAR_SEQ 439 474 GAQQVNLPVPEGCTDPVAENFDPTARSDDGTCVYNF -> T FT EEKEPSK (in isoform Short). FT {ECO:0000303|PubMed:14593172}. FT /FTId=VSP_005539. FT CONFLICT 163 164 IW -> SR (in Ref. 1; CAA32429). FT {ECO:0000305}. FT CONFLICT 202 203 PA -> VR (in Ref. 1; CAA32429). FT {ECO:0000305}. FT CONFLICT 226 226 F -> L (in Ref. 5; AAN18180). FT {ECO:0000305}. FT CONFLICT 292 292 A -> G (in Ref. 1; CAA32429). FT {ECO:0000305}. FT CONFLICT 296 296 R -> L (in Ref. 1; CAA32429). FT {ECO:0000305}. FT CONFLICT 304 306 YWA -> LTG (in Ref. 1; CAA32429). FT {ECO:0000305}. FT CONFLICT 316 317 CK -> W (in Ref. 1; CAA32429). FT {ECO:0000305}. FT CONFLICT 339 339 G -> D (in Ref. 5; AAN18180/AAK96483). FT {ECO:0000305}. FT CONFLICT 441 442 QQ -> HE (in Ref. 1; CAA32429). FT {ECO:0000305}. FT HELIX 135 147 {ECO:0000244|PDB:4W5W}. FT STRAND 159 164 {ECO:0000244|PDB:4W5W}. FT HELIX 171 181 {ECO:0000244|PDB:4W5W}. FT STRAND 187 190 {ECO:0000244|PDB:4W5W}. FT HELIX 204 218 {ECO:0000244|PDB:4W5W}. FT STRAND 225 227 {ECO:0000244|PDB:4W5W}. FT HELIX 241 253 {ECO:0000244|PDB:4W5W}. FT STRAND 255 257 {ECO:0000244|PDB:4W5W}. FT STRAND 280 286 {ECO:0000244|PDB:4W5W}. FT HELIX 292 297 {ECO:0000244|PDB:4W5W}. FT STRAND 299 304 {ECO:0000244|PDB:4W5W}. FT HELIX 309 319 {ECO:0000244|PDB:4W5W}. FT STRAND 321 324 {ECO:0000244|PDB:4W5W}. FT HELIX 327 336 {ECO:0000244|PDB:4W5W}. FT HELIX 342 364 {ECO:0000244|PDB:4W5W}. FT HELIX 366 368 {ECO:0000244|PDB:4W5W}. FT HELIX 369 373 {ECO:0000244|PDB:4W5W}. FT STRAND 376 378 {ECO:0000244|PDB:4W5W}. FT HELIX 390 414 {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 //