CP121_ARATH
ID CP121_ARATH Reviewed; 124 AA.
AC O22914; Q8RYE5; Q941E3;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Calvin cycle protein CP12-1, chloroplastic;
DE AltName: Full=CP12 domain-containing protein 1;
DE AltName: Full=Chloroplast protein 12-1;
DE Flags: Precursor;
GN Name=CP12-1; OrderedLocusNames=At2g47400; ORFNames=T8I13.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
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., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION BY SUCROSE.
RC STRAIN=cv. Columbia;
RX PubMed=15533878; DOI=10.1093/jxb/eri020;
RA Marri L., Sparla F., Pupillo P., Trost P.;
RT "Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate
RT dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana.";
RL J. Exp. Bot. 56:73-80(2005).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY LIGHT AND HEAT.
RC STRAIN=cv. Columbia;
RX PubMed=18974062; DOI=10.1093/jxb/ern236;
RA Singh P., Kaloudas D., Raines C.A.;
RT "Expression analysis of the Arabidopsis CP12 gene family suggests novel
RT roles for these proteins in roots and floral tissues.";
RL J. Exp. Bot. 59:3975-3985(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISULFIDE BOND.
RX PubMed=20399532; DOI=10.1016/j.jplph.2010.02.008;
RA Marri L., Pesaresi A., Valerio C., Lamba D., Pupillo P., Trost P.,
RA Sparla F.;
RT "In vitro characterization of Arabidopsis CP12 isoforms reveals common
RT biochemical and molecular properties.";
RL J. Plant Physiol. 167:939-950(2010).
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:20399532}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) are -326 mV and -350 mV for the disulfide bonds at pH 7.9.
CC {ECO:0000269|PubMed:20399532};
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:20399532}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20399532}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, hypocotyl, cotyledons,
CC leaves, stems, and flower stalks. Barely detectable in roots and
CC siliques. Present in root tips and lateral roots. Accumulates in the
CC cotyledons of etiolated seedlings. {ECO:0000269|PubMed:15533878,
CC ECO:0000269|PubMed:18974062}.
CC -!- DEVELOPMENTAL STAGE: In flowers, expressed in the sepals and the style.
CC In siliques, present in the tip and the base, in funiculus and in
CC mature seeds. Present in both dried and imbibed seeds, especially in
CC the seed coat and micropyle. {ECO:0000269|PubMed:18974062}.
CC -!- INDUCTION: Insensitive to light/darkness, anaerobic treatment and heat,
CC but repressed by sucrose. {ECO:0000269|PubMed:15533878,
CC ECO:0000269|PubMed:18974062}.
CC -!- PTM: Contains two disulfide bonds; only the oxidized protein, with two
CC disulfide bonds, is active in complex formation. The C-terminal
CC disulfide is involved in the interaction with GAPDH and the N-terminal
CC disulfide mediates the binding of PRK with this binary complex.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CP12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63839.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002337; AAB63839.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10836.1; -; Genomic_DNA.
DR EMBL; AY052217; AAK97687.1; -; mRNA.
DR EMBL; AY062839; AAL32917.1; -; mRNA.
DR EMBL; AY114595; AAM47914.1; -; mRNA.
DR EMBL; AY143796; AAN28735.1; -; mRNA.
DR PIR; G84914; G84914.
DR RefSeq; NP_566100.2; NM_130308.3.
DR AlphaFoldDB; O22914; -.
DR SMR; O22914; -.
DR BioGRID; 4688; 3.
DR IntAct; O22914; 4.
DR STRING; 3702.AT2G47400.1; -.
DR iPTMnet; O22914; -.
DR PaxDb; O22914; -.
DR PRIDE; O22914; -.
DR ProteomicsDB; 220301; -.
DR EnsemblPlants; AT2G47400.1; AT2G47400.1; AT2G47400.
DR GeneID; 819353; -.
DR Gramene; AT2G47400.1; AT2G47400.1; AT2G47400.
DR KEGG; ath:AT2G47400; -.
DR Araport; AT2G47400; -.
DR TAIR; locus:2065220; AT2G47400.
DR eggNOG; ENOG502S5GB; Eukaryota.
DR HOGENOM; CLU_137076_0_0_1; -.
DR InParanoid; O22914; -.
DR OMA; EEYCNDN; -.
DR OrthoDB; 1634668at2759; -.
DR PhylomeDB; O22914; -.
DR PRO; PR:O22914; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22914; baseline and differential.
DR Genevisible; O22914; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0016151; F:nickel cation binding; ISS:UniProtKB.
DR GO; GO:0080153; P:negative regulation of reductive pentose-phosphate cycle; IDA:TAIR.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
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; Disulfide bond; Nickel; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 48..124
FT /note="Calvin cycle protein CP12-1, chloroplastic"
FT /id="PRO_0000417430"
FT REGION 90..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 68..77
FT /evidence="ECO:0000250"
FT DISULFID 110..119
FT /evidence="ECO:0000250"
FT CONFLICT 119
FT /note="C -> Y (in Ref. 3; AAK97687/AAN28735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 13487 MW; 0F42F25482AE9A54 CRC64;
MTTIAAAGLN VATPRVVVRP VARVLGPVRL NYPWKFGSMK RMVVVKATSE GEISEKVEKS
IQEAKETCAD DPVSGECVAA WDEVEELSAA ASHARDKKKA GGSDPLEEYC NDNPETDECR
TYDN
