RCA_SPIOL
ID RCA_SPIOL Reviewed; 472 AA.
AC P10871; Q43327;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic;
DE Short=RA;
DE Short=RuBisCO activase;
DE Flags: Precursor;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Leaf;
RX PubMed=3277181; DOI=10.1073/pnas.85.3.787;
RA Werneke J.M., Zielinski R.E., Ogren W.L.;
RT "Structure and expression of spinach leaf cDNA encoding
RT ribulosebisphosphate carboxylase/oxygenase activase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:787-791(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND 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).
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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=45 kDa;
CC IsoId=P10871-1; Sequence=Displayed;
CC Name=2; Synonyms=41 kDa;
CC IsoId=P10871-2; Sequence=VSP_005541;
CC -!- SIMILARITY: Belongs to the RuBisCO activase family. {ECO:0000305}.
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DR EMBL; J03610; AAA34038.1; -; mRNA.
DR EMBL; S45033; AAD13840.1; -; Genomic_DNA.
DR EMBL; S45033; AAD13841.1; -; Genomic_DNA.
DR PIR; A31082; A31082.
DR AlphaFoldDB; P10871; -.
DR SMR; P10871; -.
DR IntAct; P10871; 1.
DR PRIDE; P10871; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 Alternative splicing; ATP-binding; Chloroplast; Direct protein sequencing;
KW Nucleotide-binding; Plastid; Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT CHAIN 59..472
FT /note="Ribulose bisphosphate carboxylase/oxygenase
FT activase, chloroplastic"
FT /id="PRO_0000030241"
FT REGION 448..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 436..472
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005541"
FT CONFLICT 129
FT /note="F -> L (in Ref. 1; AAA34038)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="M -> L (in Ref. 1; AAA34038)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="H -> D (in Ref. 1; AAA34038)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 51559 MW; D6D04A3EF6E3489E CRC64;
MATAVSTVGA ATRAPLNLNG SSAGASVPTS GFLGSSLKKH TNVRFPSSSR TTSMTVKAAE
NEEKNTDKWA HLAKDFSDDQ LDIRRGKGMV DSLFQAPADA GTHVPIQSSF EYESQGLRKY
DIDNMLGDFY IAPAFMDKLV VHITKNFLNL PNIKIPLILG VWGGKGQGKS FQCELVFAKL
GINPIMMSAG ELESGNAGEP AKLIRQRYRE AADLIAKGKM CALFINDLEP GAGRMGGTTQ
YTVNNQMVNA TLMNIADNPT NVQLPGMYNK QDNARVPIIV TGNDFSTLYA PLIRDGRMEK
FYWAPTREDR IGVCTGIFKT DKVPAEHVVK LVDAFPGQSI DFFGALRARV YHDEVRKWVN
SVGVDNVGKK LVNSKDGPPV FEQPEMTLQK LMEYGNMLVQ EQENVKRVQL ADQYMSSAAL
GDANKDAIDR GTFFGKAAQQ VSLPVAQGCT DPEAKNYDPT ARSDDGSCTY NL