ID RCA_ARATH Reviewed; 474 AA. AC P10896; Q39197; Q39198; Q940T8; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-JAN-2011, entry version 109. 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; core eudicotyledons; OC rosids; malvids; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RX MEDLINE=89240055; 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 MEDLINE=94151424; 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 MEDLINE=20083487; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; 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 [5] 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 [6] RP ALTERNATIVE SPLICING. RX MEDLINE=92393414; 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 [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RC STRAIN=cv. Wassilewskija; RX MEDLINE=22745486; 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 [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-78, AND MASS RP SPECTROMETRY. 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-78, AND MASS RP SPECTROMETRY. RC STRAIN=cv. Columbia; TISSUE=Seedling; 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). 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 -!- INTERACTION: CC Q42403:TRX3; NbExp=1; IntAct=EBI-449165, EBI-449157; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, CC chloroplast, plastoglobule. 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 -!- SIMILARITY: Belongs to the RuBisCO activase family. 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; AY052703; AAK96607.1; -; mRNA. DR EMBL; AF325049; AAG40401.1; -; mRNA. DR EMBL; AY056108; AAL06995.1; -; mRNA. DR EMBL; BT000710; AAN31853.1; -; mRNA. DR EMBL; AY088487; AAM66023.1; -; mRNA. DR IPI; IPI00518163; -. DR IPI; IPI00526733; -. DR PIR; S04048; S04048. DR PIR; T01002; T01002. DR PIR; T01003; T01003. DR RefSeq; NP_565913.1; NM_129531.2. DR RefSeq; NP_850320.1; NM_179989.2. DR UniGene; At.25299; -. DR UniGene; At.25319; -. DR UniGene; At.47493; -. DR ProteinModelPortal; P10896; -. DR SMR; P10896; 148-323. DR IntAct; P10896; 1. DR STRING; P10896; -. DR SWISS-2DPAGE; P10896; -. DR World-2DPAGE; 0003:P10896; -. DR PRIDE; P10896; -. DR ProMEX; P10896; -. DR EnsemblPlants; AT2G39730.1-TAIR; AT2G39730.1-P; AT2G39730-TAIR-G. DR GeneID; 818558; -. DR GenomeReviews; CT485783_GR; AT2G39730. DR KEGG; ath:AT2G39730; -. DR NMPDR; fig|3702.1.peg.11091; -. DR TAIR; At2g39730; -. DR eggNOG; KOG0651; -. DR HOGENOM; HBG320501; -. DR InParanoid; P10896; -. DR OMA; RDDRIGV; -. DR ArrayExpress; P10896; -. DR Genevestigator; P10896; -. DR GO; GO:0048046; C:apoplast; IDA:TAIR. DR GO; GO:0005618; C:cell wall; IDA:TAIR. DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR. DR GO; GO:0009535; C:chloroplast thylakoid 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:0043531; F:ADP binding; IDA:TAIR. DR GO; GO:0005524; F:ATP binding; IDA:TAIR. DR GO; GO:0005515; F:protein binding; IPI:IntAct. 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:0009409; P:response to cold; IEP:TAIR. DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR. DR InterPro; IPR003959; ATPase_AAA_core. DR Pfam; PF00004; AAA; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Chloroplast; Complete proteome; KW Nucleotide-binding; Phosphoprotein; Plastid; 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 (Potential). FT MOD_RES 78 78 Phosphothreonine. FT VAR_SEQ 439 474 GAQQVNLPVPEGCTDPVAENFDPTARSDDGTCVYNF -> T FT EEKEPSK (in isoform Short). FT /FTId=VSP_005539. FT CONFLICT 163 164 IW -> SR (in Ref. 1; CAA32429). FT CONFLICT 202 203 PA -> VR (in Ref. 1; CAA32429). FT CONFLICT 292 292 A -> G (in Ref. 1; CAA32429). FT CONFLICT 296 296 R -> L (in Ref. 1; CAA32429). FT CONFLICT 304 306 YWA -> LTG (in Ref. 1; CAA32429). FT CONFLICT 316 317 CK -> W (in Ref. 1; CAA32429). FT CONFLICT 441 442 QQ -> HE (in Ref. 1; CAA32429). 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 //