ID   RAF1_MAIZE              Reviewed;         463 AA.
AC   B4FR29;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Rubisco accumulation factor 1, chloroplastic {ECO:0000303|PubMed:22942379};
DE   Flags: Precursor;
GN   Name=RAF1 {ECO:0000303|PubMed:22942379};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. B73;
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2]
RP   FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=22942379; DOI=10.1105/tpc.112.102012;
RA   Feiz L., Williams-Carrier R., Wostrikoff K., Belcher S., Barkan A.,
RA   Stern D.B.;
RT   "Ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulation factor1 is
RT   required for holoenzyme assembly in maize.";
RL   Plant Cell 24:3435-3446(2012).
CC   -!- FUNCTION: Required for assembly or stability of RuBisCO. Acts at a
CC       postchaperonin step to fold and/or assemble the large subunit (LS) into
CC       RuBisCO. {ECO:0000269|PubMed:22942379}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:22942379}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in bundle sheath.
CC       {ECO:0000269|PubMed:22942379}.
CC   -!- DOMAIN: Has 3 domains, the N-terminal alpha-helical domain, an extended
CC       flexible linker and the C-terminal beta-sheet domain. The N-terminal
CC       alpha-helical domain stabilizes RbcL dimers and RbcL dimer-dimer
CC       interactions, facilitating RbcL(8) formation. The C-terminal beta-sheet
CC       domain probably dimerizes Raf1 (By similarity). The 2 C-terminal beta-
CC       sheet domains are swapped and pack against each other to form the dimer
CC       interface (By similarity). {ECO:0000250|UniProtKB:Q8YLP6,
CC       ECO:0000250|UniProtKB:Q9SR19}.
CC   -!- DISRUPTION PHENOTYPE: Seedling lethal due to a lack of RuBisCO.
CC       {ECO:0000269|PubMed:22942379}.
CC   -!- SIMILARITY: Belongs to the RAF family. {ECO:0000305}.
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DR   EMBL; BT039567; ACF84572.1; -; mRNA.
DR   RefSeq; NP_001140763.1; NM_001147291.1.
DR   AlphaFoldDB; B4FR29; -.
DR   SMR; B4FR29; -.
DR   STRING; 4577.GRMZM2G457621_P01; -.
DR   PaxDb; B4FR29; -.
DR   EnsemblPlants; Zm00001eb066000_T001; Zm00001eb066000_P001; Zm00001eb066000.
DR   GeneID; 100272838; -.
DR   Gramene; Zm00001eb066000_T001; Zm00001eb066000_P001; Zm00001eb066000.
DR   KEGG; zma:100272838; -.
DR   eggNOG; ENOG502QRYH; Eukaryota.
DR   HOGENOM; CLU_041979_0_0_1; -.
DR   OMA; IVASQVY; -.
DR   OrthoDB; 1337198at2759; -.
DR   Proteomes; UP000007305; Chromosome 2.
DR   ExpressionAtlas; B4FR29; differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IEA:UniProt.
DR   InterPro; IPR037494; RAF1.
DR   InterPro; IPR040858; Raf1_C.
DR   InterPro; IPR040781; Raf1_HTH.
DR   InterPro; IPR041358; Raf1_N.
DR   PANTHER; PTHR35299; PTHR35299; 1.
DR   Pfam; PF18579; Raf1_HTH; 1.
DR   Pfam; PF18578; Raf1_N; 1.
DR   Pfam; PF18087; RuBisCo_chap_C; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Chloroplast; Coiled coil; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..463
FT                   /note="Rubisco accumulation factor 1, chloroplastic"
FT                   /id="PRO_0000424240"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..275
FT                   /note="N-terminal alpha-helix"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SR19"
FT   REGION          305..450
FT                   /note="C-terminal beta sheet"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SR19"
FT   COILED          240..294
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        58..84
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  50918 MW;  78FA291A397534AF CRC64;
     MLSLSHPHPH PAASTTAPRH QRTAPVWHRR RASHIAASAI LLPGGGSTGG RGGPGDRRLP
     FTPPPMAPPG QLYQPFHPPP SPLPPSLRNL DLSERLQILR DRMGLWHEYA PLISSLSRDG
     FNPSSIQEAT GISGVEQNCL VVASQVRDSL LDDRAAAFPP DLLPYFDSLG GPEVLYELRF
     LNARQRADAA RHAIGYRLEP KGVRELARAM KGFPRWRGEE GWEAFSKDSP ADCLAFARFR
     QSREAIDVQD RVAELERALQ VVETESGRAR VELELERARR KAAGEEEVDE EGEEDDAAAS
     LRPGVTVVRL RYGEVAEATT VILLPVVRET DGVAAMESAP RRAKTDVGLG VVEVDRAWAR
     WAVVPGWGPV AEAADDAVVV ELADGRRLPW RMSDEEPVLV IANRSKKEVV EEGVYVLERE
     GRLVVERGKK LAEQGIAAAA AEVVIVVRPP KDEDDMVSDE EWD