Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calvin cycle protein CP12-1, chloroplastic

Gene

CP12-1

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.1 Publication

Redox potential

E0 are -326 mV and -350 mV for the disulfide bonds at pH 7.9.1 Publication

Manual assertion based on experiment ini

GO - Molecular functioni

GO - Biological processi

  • negative regulation of reductive pentose-phosphate cycle Source: TAIR
  • reductive pentose-phosphate cycle Source: UniProtKB-KW
  • response to sucrose Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Calvin cycle

Keywords - Ligandi

Copper, Nickel

Names & Taxonomyi

Protein namesi
Recommended name:
Calvin cycle protein CP12-1, chloroplastic
Alternative name(s):
CP12 domain-containing protein 1
Chloroplast protein 12-1
Gene namesi
Name:CP12-1
Ordered Locus Names:At2g47400
ORF Names:T8I13.24
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G47400.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 47ChloroplastBy similarityAdd BLAST47
ChainiPRO_000041743048 – 124Calvin cycle protein CP12-1, chloroplasticAdd BLAST77

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi68 ↔ 77By similarity
Disulfide bondi110 ↔ 119By similarity

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

PaxDbiO22914.
PRIDEiO22914.

PTM databases

iPTMnetiO22914.

Expressioni

Tissue specificityi

Mostly expressed in flowers, hypocotyl, cotyledons, leaves, stems, and flower stalks. Barely detectable in roots and siliques. Present in root tips and lateral roots. Accumulates in the cotyledons of etiolated seedlings.2 Publications

Developmental stagei

In flowers, expressed in the sepals and the style. In siliques, present in the tip and the base, in funiculus and in mature seeds. Present in both dried and imbibed seeds, especially in the seed coat and micropyle.1 Publication

Inductioni

Insensitive to light/darkness, anaerobic treatment and heat, but repressed by sucrose.2 Publications

Gene expression databases

GenevisibleiO22914. AT.

Interactioni

Subunit structurei

Monomer (By similarity). 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.By similarity1 Publication

Protein-protein interaction databases

BioGridi4688. 2 interactors.
IntActiO22914. 4 interactors.
STRINGi3702.AT2G47400.1.

Structurei

3D structure databases

ProteinModelPortaliO22914.
SMRiO22914.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CP12 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410J0MZ. Eukaryota.
ENOG4112442. LUCA.
HOGENOMiHOG000237802.
InParanoidiO22914.
OMAiKRMVMSV.
OrthoDBiEOG09360UU6.
PhylomeDBiO22914.

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.

O22914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTIAAAGLN VATPRVVVRP VARVLGPVRL NYPWKFGSMK RMVVVKATSE
60 70 80 90 100
GEISEKVEKS IQEAKETCAD DPVSGECVAA WDEVEELSAA ASHARDKKKA
110 120
GGSDPLEEYC NDNPETDECR TYDN
Length:124
Mass (Da):13,487
Last modified:January 1, 1998 - v1
Checksum:i0F42F25482AE9A54
GO

Sequence cautioni

The sequence AAB63839 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti119C → Y in AAK97687 (PubMed:14593172).Curated1
Sequence conflicti119C → Y in AAN28735 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002337 Genomic DNA. Translation: AAB63839.2. Sequence problems.
CP002685 Genomic DNA. Translation: AEC10836.1.
AY052217 mRNA. Translation: AAK97687.1.
AY062839 mRNA. Translation: AAL32917.1.
AY114595 mRNA. Translation: AAM47914.1.
AY143796 mRNA. Translation: AAN28735.1.
PIRiG84914.
RefSeqiNP_566100.2. NM_130308.3.
UniGeneiAt.20118.
At.71629.

Genome annotation databases

EnsemblPlantsiAT2G47400.1; AT2G47400.1; AT2G47400.
GeneIDi819353.
GrameneiAT2G47400.1; AT2G47400.1; AT2G47400.
KEGGiath:AT2G47400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002337 Genomic DNA. Translation: AAB63839.2. Sequence problems.
CP002685 Genomic DNA. Translation: AEC10836.1.
AY052217 mRNA. Translation: AAK97687.1.
AY062839 mRNA. Translation: AAL32917.1.
AY114595 mRNA. Translation: AAM47914.1.
AY143796 mRNA. Translation: AAN28735.1.
PIRiG84914.
RefSeqiNP_566100.2. NM_130308.3.
UniGeneiAt.20118.
At.71629.

3D structure databases

ProteinModelPortaliO22914.
SMRiO22914.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4688. 2 interactors.
IntActiO22914. 4 interactors.
STRINGi3702.AT2G47400.1.

PTM databases

iPTMnetiO22914.

Proteomic databases

PaxDbiO22914.
PRIDEiO22914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G47400.1; AT2G47400.1; AT2G47400.
GeneIDi819353.
GrameneiAT2G47400.1; AT2G47400.1; AT2G47400.
KEGGiath:AT2G47400.

Organism-specific databases

TAIRiAT2G47400.

Phylogenomic databases

eggNOGiENOG410J0MZ. Eukaryota.
ENOG4112442. LUCA.
HOGENOMiHOG000237802.
InParanoidiO22914.
OMAiKRMVMSV.
OrthoDBiEOG09360UU6.
PhylomeDBiO22914.

Miscellaneous databases

PROiO22914.

Gene expression databases

GenevisibleiO22914. 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 nameiCP121_ARATH
AccessioniPrimary (citable) accession number: O22914
Secondary accession number(s): Q8RYE5, Q941E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 97 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.