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Protein

Calvin cycle protein CP12-1, chloroplastic

Gene

CP12-1

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.1 Publication

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 -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

Keywordsi

Biological processCalvin cycle
LigandCopper, 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

AraportiAT2G47400
TAIRilocus:2065220 AT2G47400

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

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

ExpressionAtlasiO22914 baseline and differential
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

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
OMAiEEYCNDN
OrthoDBiEOG09360UU6
PhylomeDBiO22914

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.

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

Similar proteinsi

Entry informationi

Entry nameiCP121_ARATH
AccessioniPrimary (citable) accession number: O22914
Secondary accession number(s): Q8RYE5, Q941E3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: January 1, 1998
Last modified: April 25, 2018
This is version 102 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

Complete proteome, Reference proteome

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