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Protein

Calvin cycle protein CP12-2, chloroplastic

Gene

CP12-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Redox potential

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

GO - Molecular functioni

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
  • reductive pentose-phosphate cycle Source: TAIR
  • response to light stimulus Source: UniProtKB
  • response to sucrose Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Calvin cycle

Keywords - Ligandi

Copper, 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

TAIRiAT3G62410.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi75 – 751C → S: Normal under reducing conditions, but can form dimers under oxidizing conditions. Impaired formation of a ternary complex with PRK. 1 Publication
Mutagenesisi126 – 1261C → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5454ChloroplastBy similarityAdd
BLAST
Chaini55 – 13177Calvin cycle protein CP12-2, chloroplasticPRO_0000417431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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.
PRIDEiQ9LZP9.

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

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

Protein-protein interaction databases

BioGridi10728. 3 interactions.
IntActiQ9LZP9. 4 interactions.
STRINGi3702.AT3G62410.1.

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi112 – 1198Combined sources
Turni124 – 1263Combined sources

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the CP12 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410J0MZ. Eukaryota.
ENOG4112442. LUCA.
HOGENOMiHOG000237802.
InParanoidiQ9LZP9.
OMAiSRTTNRM.
OrthoDBiEOG09360UU6.
PhylomeDBiQ9LZP9.

Family and domain databases

InterProiIPR003823. DUF_CP12.
[Graphical view]
PfamiPF02672. CP12. 1 hit.
[Graphical view]
SMARTiSM01093. CP12. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851V → I in AAM63795 (Ref. 4) Curated

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_116106.2.
UniGeneiAt.23855.
At.48798.

Genome annotation databases

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

Cross-referencesi

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_116106.2.
UniGeneiAt.23855.
At.48798.

3D structure databases

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

Protein-protein interaction databases

BioGridi10728. 3 interactions.
IntActiQ9LZP9. 4 interactions.
STRINGi3702.AT3G62410.1.

Proteomic databases

PaxDbiQ9LZP9.
PRIDEiQ9LZP9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT3G62410.

Phylogenomic databases

eggNOGiENOG410J0MZ. Eukaryota.
ENOG4112442. LUCA.
HOGENOMiHOG000237802.
InParanoidiQ9LZP9.
OMAiSRTTNRM.
OrthoDBiEOG09360UU6.
PhylomeDBiQ9LZP9.

Enzyme and pathway databases

BioCyciARA:AT3G62410-MONOMER.
MetaCyc:AT3G62410-MONOMER.

Miscellaneous databases

PROiQ9LZP9.

Gene expression databases

GenevisibleiQ9LZP9. AT.

Family and domain databases

InterProiIPR003823. DUF_CP12.
[Graphical view]
PfamiPF02672. CP12. 1 hit.
[Graphical view]
SMARTiSM01093. CP12. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCP122_ARATH
AccessioniPrimary (citable) accession number: Q9LZP9
Secondary accession number(s): Q8LC81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: October 1, 2000
Last modified: September 7, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.