Q9LZP9 (CP122_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	131 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Plastid › chloroplast 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

Ontologies

Keywords
Biological process	Calvin cycle
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Copper Nickel
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to anoxia Inferred from expression pattern Ref.9. Source: UniProtKB cellular response to cold Inferred from expression pattern Ref.9. Source: UniProtKB cellular response to heat Inferred from expression pattern Ref.9. Source: UniProtKB negative regulation of reductive pentose-phosphate cycle Inferred from direct assay Ref.11. Source: TAIR peptide cross-linking via L-cystine Traceable author statement Ref.6. Source: TAIR reductive pentose-phosphate cycle Traceable author statement Ref.6. Source: TAIR response to light stimulus Inferred from expression pattern Ref.9. Source: UniProtKB response to sucrose stimulus Inferred from expression pattern Ref.6. Source: TAIR
Cellular_component	chloroplast stroma Inferred from direct assay PubMed 18633119. Source: TAIR protein complex Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	copper ion binding Inferred from sequence or structural similarity. Source: UniProtKB nickel cation binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GAPA	P25856	4	EBI-449218,EBI-1554434

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 54

54

Chloroplast By similarity

Chain

55 – 131

77

Calvin cycle protein CP12-2, chloroplastic

PRO_0000417431

Amino acid modifications

Disulfide bond

75 ↔ 84

Ref.8 Ref.11

Disulfide bond

117 ↔ 126

Ref.8 Ref.11

Experimental info

Mutagenesis

75

1

C → S: Normal under reducing conditions, but can form dimers under oxidizing conditions. Impaired formation of a ternary complex with PRK. Ref.8

Mutagenesis

126

1

C → 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 conflict

85

1

V → I in AAM63795. Ref.4

Secondary structure

1

.

.

.

.

.

131

Helix Strand Turn

Details...

Helix

112 – 119

8

Turn

124 – 126

3

Sequences

	Sequence		Length	Mass (Da)
	Q9LZP9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 6EFE1E1CC039B2EF	FASTA	131	14,167
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00535044.

PIR

T48033.

RefSeq

NP_191800.1. NM_116106.2.

UniGene

At.23855.
At.48798.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LJ9	NMR	-	A	54-131	[»]
3QV1	X-ray	2.00	G/H/I	54-131	[»]
3RVD	X-ray	2.70	I/J/K/L/M/N	54-131	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9LZP9. 4 interactions.

STRING

3702.AT3G62410.1-P.

Proteomic databases

PRIDE

Q9LZP9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT3G62410.1; AT3G62410.1; AT3G62410.

GeneID

825414.

KEGG

ath:AT3G62410.

Organism-specific databases

TAIR

At3g62410.

Phylogenomic databases

eggNOG

NOG08802.

HOGENOM

HOG000237802.

InParanoid

Q9LZP9.

OMA

NIATQRV.

PhylomeDB

Q9LZP9.

ProtClustDB

PLN00204.

Enzyme and pathway databases

BioCyc

ARA:AT3G62410-MONOMER.
MetaCyc:AT3G62410-MONOMER.

Gene expression databases

ArrayExpress

Q9LZP9.

Genevestigator

Q9LZP9.

Family and domain databases

InterPro

IPR003823. DUF_CP12.
[Graphical view]

Pfam

PF02672. CP12. 1 hit.
[Graphical view]

SMART

SM01093. CP12. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CP122_ARATH

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program