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Q9LZP9 (CP122_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Calvin cycle protein CP12-2, chloroplastic
Alternative name(s):
CP12 domain-containing protein 2
Chloroplast protein 12-2
Gene names
Name:CP12-2
Ordered Locus Names:At3g62410
ORF Names:T12C14.110
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length131 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues. Ref.7 Ref.11

Subunit structure

Monomer. Component of a complex that contains two dimers of PRK, two tetramers of GAPDH and CP12. CP12 associates with GAPDH, causing its conformation to change. This GAPDH/CP12 complex binds PRK to form a half-complex (one unit). This unit probably dimerizes due partially to interactions between the enzymes of each unit. Ref.7 Ref.8 Ref.11

Subcellular location

Plastidchloroplast Ref.5 Ref.10 Ref.11 Ref.12.

Tissue specificity

Mostly expressed in cotyledons, leaves and flower stalks, and, to a lower extent, in flowers and stems. Barely detectable in roots and siliques. Ref.6 Ref.9

Developmental stage

In flowers, expressed in the sepals and the style. In siliques, present at the base and tip. Ref.9

Induction

Induced by light. Repressed by darkness, cold, anaerobic treatment, heat and sucrose. Changes conformation depending on redox conditions. Ref.6 Ref.9

Post-translational modification

Contains two disulfide bonds; only the oxidized protein, with two disulfide bonds, is active in complex formation. The C-terminal disulfide is involved in the interaction with GAPDH and the N-terminal disulfide mediates the binding of PRK with this binary complex.

Miscellaneous

Binds copper and nickel ions. Copper ions catalyze the oxidation of reduced thiol groups and thus promote formation of the disulfide bonds required for linker activity By similarity.

Sequence similarities

Belongs to the CP12 family.

Biophysicochemical properties

Redox potential:

E0 are -326 mV and -352 mV for the disulfide bonds at pH 7.9. Ref.8 Ref.11

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GAPAP258564EBI-449218,EBI-1554434

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5454Chloroplast By similarity
Chain55 – 13177Calvin cycle protein CP12-2, chloroplastic
PRO_0000417431

Amino acid modifications

Disulfide bond75 ↔ 84 Ref.8 Ref.11
Disulfide bond117 ↔ 126 Ref.8 Ref.11

Experimental info

Mutagenesis751C → S: Normal under reducing conditions, but can form dimers under oxidizing conditions. Impaired formation of a ternary complex with PRK. Ref.8
Mutagenesis1261C → S: Normal under reducing conditions, but can form dimers under oxidizing conditions. Impaired interaction with GAPDH and loss of formation of a ternary complex with PRK. Ref.8
Sequence conflict851V → I in AAM63795. Ref.4

Secondary structure

..... 131
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9LZP9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6EFE1E1CC039B2EF

FASTA13114,167
        10         20         30         40         50         60 
MATIATGLNI ATQRVFVTSE NRPVCLAGPV HLNNSWNLGS RTTNRMMKLQ PIKAAPEGGI 

        70         80         90        100        110        120 
SDVVEKSIKE AQETCAGDPV SGECVAAWDE VEELSAAASH ARDKKKADGS DPLEEYCKDN 

       130 
PETNECRTYD N 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana."
Marri L., Sparla F., Pupillo P., Trost P.
J. Exp. Bot. 56:73-80(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION BY DARKNESS AND SUCROSE.
Strain: cv. Columbia.
[7]"Reconstitution and properties of the recombinant glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of Arabidopsis."
Marri L., Trost P., Pupillo P., Sparla F.
Plant Physiol. 139:1433-1443(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, PTM.
[8]"Spontaneous assembly of photosynthetic supramolecular complexes as mediated by the intrinsically unstructured protein CP12."
Marri L., Trost P., Trivelli X., Gonnelli L., Pupillo P., Sparla F.
J. Biol. Chem. 283:1831-1838(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-131, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF CYS-75 AND CYS-126.
[9]"Expression analysis of the Arabidopsis CP12 gene family suggests novel roles for these proteins in roots and floral tissues."
Singh P., Kaloudas D., Raines C.A.
J. Exp. Bot. 59:3975-3985(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY LIGHT; HEAT AND COLD.
Strain: cv. Columbia.
[10]"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"In vitro characterization of Arabidopsis CP12 isoforms reveals common biochemical and molecular properties."
Marri L., Pesaresi A., Valerio C., Lamba D., Pupillo P., Trost P., Sparla F.
J. Plant Physiol. 167:939-950(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BOND.
[12]"Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering."
Olinares P.D., Ponnala L., van Wijk K.J.
Mol. Cell. Proteomics 9:1594-1615(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL162507 Genomic DNA. Translation: CAB82955.1.
CP002686 Genomic DNA. Translation: AEE80349.1.
AY096645 mRNA. Translation: AAM20142.1.
AY114023 mRNA. Translation: AAM45071.1.
AY086744 mRNA. Translation: AAM63795.1.
IPIIPI00535044.
PIRT48033.
RefSeqNP_191800.1. NM_116106.2.
UniGeneAt.23855.
At.48798.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LJ9NMR-A54-131[»]
3QV1X-ray2.00G/H/I54-131[»]
3RVDX-ray2.70I/J/K/L/M/N54-131[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9LZP9. 4 interactions.
STRING3702.AT3G62410.1-P.

Proteomic databases

PRIDEQ9LZP9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G62410.1; AT3G62410.1; AT3G62410.
GeneID825414.
KEGGath:AT3G62410.

Organism-specific databases

TAIRAt3g62410.

Phylogenomic databases

eggNOGNOG08802.
HOGENOMHOG000237802.
InParanoidQ9LZP9.
OMANIATQRV.
PhylomeDBQ9LZP9.
ProtClustDBPLN00204.

Enzyme and pathway databases

BioCycARA:AT3G62410-MONOMER.
MetaCyc:AT3G62410-MONOMER.

Gene expression databases

ArrayExpressQ9LZP9.
GenevestigatorQ9LZP9.

Family and domain databases

InterProIPR003823. DUF_CP12.
[Graphical view]
PfamPF02672. CP12. 1 hit.
[Graphical view]
SMARTSM01093. CP12. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCP122_ARATH
AccessionPrimary (citable) accession number: Q9LZP9
Secondary accession number(s): Q8LC81
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: October 1, 2000
Last modified: April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families