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Protein

Calvin cycle protein CP12-2, chloroplastic

Gene

CP12-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

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).By similarity

Redox potential

E0 are -326 mV and -352 mV for the disulfide bonds at pH 7.9.2 Publications

Manual assertion based on experiment ini

GO - Molecular functioni

  • copper ion binding Source: UniProtKB
  • enzyme binding Source: CAFA
  • nickel cation binding Source: UniProtKB
  • protein binding, bridging Source: CAFA
  • protein-containing complex binding Source: CAFA

GO - Biological processi

  • cellular response to anoxia Source: UniProtKB
  • cellular response to cold Source: UniProtKB
  • cellular response to heat Source: UniProtKB
  • negative regulation of reductive pentose-phosphate cycle Source: TAIR
  • peptide cross-linking via L-cystine Source: TAIR
  • protein-containing complex assembly Source: CAFA
  • reductive pentose-phosphate cycle Source: TAIR
  • response to light stimulus Source: UniProtKB
  • response to sucrose Source: TAIR

Keywordsi

Biological processCalvin cycle
LigandCopper, Nickel

Enzyme and pathway databases

BioCyciARA:AT3G62410-MONOMER
MetaCyc:AT3G62410-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Calvin cycle protein CP12-2, chloroplastic
Alternative name(s):
CP12 domain-containing protein 2
Chloroplast protein 12-2
Gene namesi
Name:CP12-2
Ordered Locus Names:At3g62410
ORF Names:T12C14.110
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

AraportiAT3G62410
TAIRilocus:2096009 AT3G62410

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi75C → S: Normal under reducing conditions, but can form dimers under oxidizing conditions. Impaired formation of a ternary complex with PRK. 1 Publication1
Mutagenesisi126C → 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. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 53ChloroplastCuratedAdd BLAST53
ChainiPRO_000041743154 – 131Calvin cycle protein CP12-2, chloroplasticAdd BLAST78

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi75 ↔ 84
Disulfide bondi117 ↔ 126

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9LZP9

Expressioni

Tissue specificityi

Mostly expressed in cotyledons, leaves and flower stalks, and, to a lower extent, in flowers and stems. Barely detectable in roots and siliques.2 Publications

Developmental stagei

In flowers, expressed in the sepals and the style. In siliques, present at the base and tip.1 Publication

Inductioni

Induced by light. Repressed by darkness, cold, anaerobic treatment, heat and sucrose. Changes conformation depending on redox conditions.2 Publications

Gene expression databases

ExpressionAtlasiQ9LZP9 baseline and differential
GenevisibleiQ9LZP9 AT

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GAPA1P258564EBI-449218,EBI-1554434

GO - Molecular functioni

  • enzyme binding Source: CAFA
  • protein binding, bridging Source: CAFA

Protein-protein interaction databases

BioGridi10728, 3 interactors
IntActiQ9LZP9, 4 interactors
STRINGi3702.AT3G62410.1

Structurei

Secondary structure

1131
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi112 – 119Combined sources8
Turni124 – 126Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LJ9NMR-A54-131[»]
3QV1X-ray2.00G/H/I54-131[»]
3RVDX-ray2.70I/J/K/L/M/N54-131[»]
DisProtiDP00534
SMRiQ9LZP9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CP12 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410J0MZ Eukaryota
ENOG4112442 LUCA
HOGENOMiHOG000237802
InParanoidiQ9LZP9
OMAiAQETCAG
OrthoDBiEOG09360UU6
PhylomeDBiQ9LZP9

Family and domain databases

InterProiView protein in InterPro
IPR003823 DUF_CP12
PfamiView protein in Pfam
PF02672 CP12, 1 hit
SMARTiView protein in SMART
SM01093 CP12, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LZP9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATIATGLNI ATQRVFVTSE NRPVCLAGPV HLNNSWNLGS RTTNRMMKLQ
60 70 80 90 100
PIKAAPEGGI SDVVEKSIKE AQETCAGDPV SGECVAAWDE VEELSAAASH
110 120 130
ARDKKKADGS DPLEEYCKDN PETNECRTYD N
Length:131
Mass (Da):14,167
Last modified:October 1, 2000 - v1
Checksum:i6EFE1E1CC039B2EF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti85V → I in AAM63795 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiT48033
RefSeqiNP_191800.1, NM_116106.3
UniGeneiAt.23855
At.48798

Genome annotation databases

EnsemblPlantsiAT3G62410.1; AT3G62410.1; AT3G62410
GeneIDi825414
GrameneiAT3G62410.1; AT3G62410.1; AT3G62410
KEGGiath:AT3G62410

Similar proteinsi

Entry informationi

Entry nameiCP122_ARATH
AccessioniPrimary (citable) accession number: Q9LZP9
Secondary accession number(s): Q8LC81
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: October 1, 2000
Last modified: April 25, 2018
This is version 104 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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