CP12_CHLRE
ID CP12_CHLRE Reviewed; 107 AA.
AC A6Q0K5; A8IZ71;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Calvin cycle protein CP12, chloroplastic;
DE AltName: Full=CP12 domain-containing protein;
DE AltName: Full=Chloroplast protein 12;
DE Flags: Precursor;
GN Name=CP12; ORFNames=CHLREDRAFT_148487;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAO03469.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-32, FUNCTION,
RP SUBUNIT, AND STRUCTURE BY NMR.
RC STRAIN=cw15 {ECO:0000312|EMBL:CAO03469.1};
RX PubMed=12846565; DOI=10.1021/bi034474x;
RA Graciet E., Gans P., Wedel N., Lebreton S., Camadro J.-M., Gontero B.;
RT "The small protein CP12: a protein linker for supramolecular complex
RT assembly.";
RL Biochemistry 42:8163-8170(2003).
RN [3]
RP INTERACTION WITH GAPDH.
RX PubMed=12492483; DOI=10.1046/j.1432-1033.2003.03372.x;
RA Graciet E., Lebreton S., Camadro J.-M., Gontero B.;
RT "Characterization of native and recombinant A4 glyceraldehyde 3-phosphate
RT dehydrogenase. Kinetic evidence for conformation changes upon association
RT with the small protein CP12.";
RL Eur. J. Biochem. 270:129-136(2003).
RN [4]
RP MASS SPECTROMETRY, DISULFIDE BOND, AND MUTAGENESIS OF HIS-74.
RX PubMed=16259044; DOI=10.1002/rcm.2192;
RA Delobel A., Graciet E., Andreescu S., Gontero B., Halgand F., Laprevote O.;
RT "Mass spectrometric analysis of the interactions between CP12, a
RT chloroplast protein, and metal ions: a possible regulatory role within a
RT PRK/GAPDH/CP12 complex.";
RL Rapid Commun. Mass Spectrom. 19:3379-3388(2005).
CC -!- FUNCTION: Acts as a linker essential in the assembly of a core complex
CC of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast
CC enzymes GAPDH and PRK during darkness in photosynthetic tissues.
CC {ECO:0000269|PubMed:12846565}.
CC -!- SUBUNIT: Monomer (By similarity). Component of a complex that contains
CC two dimers of PRK, two tetramers of GAPDH and CP12. CP12 associates
CC with GAPDH, causing its conformation to change. This GAPDH/CP12 complex
CC binds PRK to form a half-complex (one unit). This unit probably
CC dimerizes due partially to interactions between the enzymes of each
CC unit. {ECO:0000250, ECO:0000269|PubMed:12846565}.
CC -!- INTERACTION:
CC A6Q0K5; P50362: GAPA; NbExp=2; IntAct=EBI-9538486, EBI-9538536;
CC A6Q0K5; P19824: PRKA; NbExp=2; IntAct=EBI-9538486, EBI-9538490;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- PTM: Contains two disulfide bonds; only the oxidized protein, with two
CC disulfide bonds, is active in complex formation.
CC -!- MASS SPECTROMETRY: Mass=8734.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16259044};
CC -!- MISCELLANEOUS: Binds copper and nickel ions. Copper ions catalyze the
CC oxidation of reduced thiol groups and thus promote formation of the
CC disulfide bonds required for linker activity (PubMed:16259044).
CC {ECO:0000305|PubMed:16259044}.
CC -!- SIMILARITY: Belongs to the CP12 family. {ECO:0000305}.
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DR EMBL; DS496128; EDP02778.1; -; Genomic_DNA.
DR EMBL; AM748786; CAO03469.1; -; Genomic_DNA.
DR RefSeq; XP_001694345.1; XM_001694293.1.
DR AlphaFoldDB; A6Q0K5; -.
DR SASBDB; A6Q0K5; -.
DR SMR; A6Q0K5; -.
DR IntAct; A6Q0K5; 2.
DR MINT; A6Q0K5; -.
DR STRING; 3055.EDP02778; -.
DR PaxDb; A6Q0K5; -.
DR PRIDE; A6Q0K5; -.
DR ProMEX; A6Q0K5; -.
DR EnsemblPlants; PNW80155; PNW80155; CHLRE_08g380250v5.
DR GeneID; 5719874; -.
DR Gramene; PNW80155; PNW80155; CHLRE_08g380250v5.
DR KEGG; cre:CHLRE_08g380250v5; -.
DR eggNOG; ENOG502S5GB; Eukaryota.
DR HOGENOM; CLU_137076_2_1_1; -.
DR InParanoid; A6Q0K5; -.
DR OMA; VVAWDET; -.
DR OrthoDB; 1634668at2759; -.
DR GO; GO:0009507; C:chloroplast; IDA:CAFA.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0099080; C:supramolecular complex; IDA:CAFA.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0016151; F:nickel cation binding; IDA:UniProtKB.
DR GO; GO:0080153; P:negative regulation of reductive pentose-phosphate cycle; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:CAFA.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR DisProt; DP00359; -.
DR InterPro; IPR039314; CP12-like.
DR InterPro; IPR003823; CP12_dom.
DR PANTHER; PTHR33921; PTHR33921; 1.
DR SMART; SM01093; CP12; 1.
PE 1: Evidence at protein level;
KW Calvin cycle; Chloroplast; Copper; Direct protein sequencing;
KW Disulfide bond; Nickel; Plastid; Transit peptide.
FT TRANSIT 1..27
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:12846565"
FT CHAIN 28..107
FT /note="Calvin cycle protein CP12, chloroplastic"
FT /id="PRO_0000302883"
FT DISULFID 50..58
FT /evidence="ECO:0000269|PubMed:16259044"
FT DISULFID 93..102
FT /evidence="ECO:0000269|PubMed:16259044"
FT MUTAGEN 74
FT /note="H->L: No impact on metal-ion binding."
FT /evidence="ECO:0000269|PubMed:16259044"
SQ SEQUENCE 107 AA; 11433 MW; F00F432FEE5F30DD CRC64;
MMLTKSVVIS RPAVRPVSTR RAVVVRASGQ PAVDLNKKVQ DAVKEAEDAC AKGTSADCAV
AWDTVEELSA AVSHKKDAVK ADVTLTDPLE AFCKDAPDAD ECRVYED
