CP122_ARATH
ID CP122_ARATH Reviewed; 131 AA.
AC Q9LZP9; Q8LC81;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Calvin cycle protein CP12-2, chloroplastic;
DE AltName: Full=CP12 domain-containing protein 2;
DE AltName: Full=Chloroplast protein 12-2;
DE Flags: Precursor;
GN Name=CP12-2; OrderedLocusNames=At3g62410; ORFNames=T12C14.110;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY DARKNESS AND 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 [6]
RP FUNCTION, SUBUNIT, AND PTM.
RX PubMed=16258009; DOI=10.1104/pp.105.068445;
RA Marri L., Trost P., Pupillo P., Sparla F.;
RT "Reconstitution and properties of the recombinant glyceraldehyde-3-
RT phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of
RT Arabidopsis.";
RL Plant Physiol. 139:1433-1443(2005).
RN [7]
RP STRUCTURE BY NMR OF 1-131, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP DISULFIDE BOND, AND MUTAGENESIS OF CYS-75 AND CYS-126.
RX PubMed=17947231; DOI=10.1074/jbc.m705650200;
RA Marri L., Trost P., Trivelli X., Gonnelli L., Pupillo P., Sparla F.;
RT "Spontaneous assembly of photosynthetic supramolecular complexes as
RT mediated by the intrinsically unstructured protein CP12.";
RL J. Biol. Chem. 283:1831-1838(2008).
RN [8]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY LIGHT; HEAT AND
RP COLD.
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 [9]
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 [10]
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:16258009, ECO:0000269|PubMed:20399532}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) are -326 mV and -352 mV for the disulfide bonds at pH 7.9.
CC {ECO:0000269|PubMed:17947231, ECO:0000269|PubMed:20399532};
CC -!- SUBUNIT: Monomer. Component of a complex that contains two dimers of
CC PRK, two tetramers of GAPDH and CP12. CP12 associates with GAPDH,
CC causing its conformation to change. This GAPDH/CP12 complex binds PRK
CC to form a half-complex (one unit). This unit probably dimerizes due
CC partially to interactions between the enzymes of each unit.
CC {ECO:0000269|PubMed:16258009, ECO:0000269|PubMed:17947231,
CC ECO:0000269|PubMed:20399532}.
CC -!- INTERACTION:
CC Q9LZP9; P25856: GAPA1; NbExp=4; IntAct=EBI-449218, EBI-1554434;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20399532}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in cotyledons, leaves and flower
CC stalks, and, to a lower extent, in flowers and stems. Barely detectable
CC in roots and siliques. {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 at the base and tip.
CC {ECO:0000269|PubMed:18974062}.
CC -!- INDUCTION: Induced by light. Repressed by darkness, cold, anaerobic
CC treatment, heat and sucrose. Changes conformation depending on redox
CC conditions. {ECO:0000269|PubMed:15533878, 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}.
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DR EMBL; AL162507; CAB82955.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80349.1; -; Genomic_DNA.
DR EMBL; AY096645; AAM20142.1; -; mRNA.
DR EMBL; AY114023; AAM45071.1; -; mRNA.
DR EMBL; AY086744; AAM63795.1; -; mRNA.
DR PIR; T48033; T48033.
DR RefSeq; NP_191800.1; NM_116106.3.
DR PDB; 2LJ9; NMR; -; A=54-131.
DR PDB; 3QV1; X-ray; 2.00 A; G/H/I=54-131.
DR PDB; 3RVD; X-ray; 2.70 A; I/J/K/L/M/N=54-131.
DR PDB; 6KEZ; X-ray; 3.50 A; M/N/O/P=55-131.
DR PDBsum; 2LJ9; -.
DR PDBsum; 3QV1; -.
DR PDBsum; 3RVD; -.
DR PDBsum; 6KEZ; -.
DR AlphaFoldDB; Q9LZP9; -.
DR BMRB; Q9LZP9; -.
DR SMR; Q9LZP9; -.
DR BioGRID; 10728; 3.
DR IntAct; Q9LZP9; 4.
DR STRING; 3702.AT3G62410.1; -.
DR PaxDb; Q9LZP9; -.
DR PRIDE; Q9LZP9; -.
DR ProteomicsDB; 224539; -.
DR EnsemblPlants; AT3G62410.1; AT3G62410.1; AT3G62410.
DR GeneID; 825414; -.
DR Gramene; AT3G62410.1; AT3G62410.1; AT3G62410.
DR KEGG; ath:AT3G62410; -.
DR Araport; AT3G62410; -.
DR TAIR; locus:2096009; AT3G62410.
DR eggNOG; ENOG502S5GB; Eukaryota.
DR HOGENOM; CLU_137076_0_0_1; -.
DR InParanoid; Q9LZP9; -.
DR OMA; PLETFCK; -.
DR OrthoDB; 1634668at2759; -.
DR PhylomeDB; Q9LZP9; -.
DR BioCyc; ARA:AT3G62410-MON; -.
DR BioCyc; MetaCyc:AT3G62410-MON; -.
DR PRO; PR:Q9LZP9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZP9; baseline and differential.
DR Genevisible; Q9LZP9; AT.
DR GO; GO:0009507; C:chloroplast; IDA: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:0099080; C:supramolecular complex; IDA:CAFA.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0016151; F:nickel cation binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:CAFA.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:CAFA.
DR GO; GO:0071454; P:cellular response to anoxia; IEP:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IEP:UniProtKB.
DR GO; GO:0080153; P:negative regulation of reductive pentose-phosphate cycle; IDA:TAIR.
DR GO; GO:0018316; P:peptide cross-linking via L-cystine; TAS:TAIR.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:CAFA.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; TAS:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR DisProt; DP00534; -.
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 3D-structure; Calvin cycle; Chloroplast; Copper; Disulfide bond; Nickel;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 54..131
FT /note="Calvin cycle protein CP12-2, chloroplastic"
FT /id="PRO_0000417431"
FT REGION 97..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 75..84
FT DISULFID 117..126
FT MUTAGEN 75
FT /note="C->S: Normal under reducing conditions, but can form
FT dimers under oxidizing conditions. Impaired formation of a
FT ternary complex with PRK."
FT /evidence="ECO:0000269|PubMed:17947231"
FT MUTAGEN 126
FT /note="C->S: Normal under reducing conditions, but can form
FT dimers under oxidizing conditions. Impaired interaction
FT with GAPDH and loss of formation of a ternary complex with
FT PRK."
FT /evidence="ECO:0000269|PubMed:17947231"
FT CONFLICT 85
FT /note="V -> I (in Ref. 4; AAM63795)"
FT /evidence="ECO:0000305"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:6KEZ"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:6KEZ"
FT HELIX 85..110
FT /evidence="ECO:0007829|PDB:6KEZ"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:3QV1"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3QV1"
SQ SEQUENCE 131 AA; 14167 MW; 6EFE1E1CC039B2EF CRC64;
MATIATGLNI ATQRVFVTSE NRPVCLAGPV HLNNSWNLGS RTTNRMMKLQ PIKAAPEGGI
SDVVEKSIKE AQETCAGDPV SGECVAAWDE VEELSAAASH ARDKKKADGS DPLEEYCKDN
PETNECRTYD N
