Q9XF88 · CB4B_ARATH
- ProteinChlorophyll a-b binding protein CP29.2, chloroplastic
- GeneLHCB4.2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids287 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
Miscellaneous
This protein is phosphorylated under normal plant growth conditions, whereas phosphorylation of maize CP29 was induced only by high light in the cold.
Cofactor
Note: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 55 | Mg (UniProtKB | ChEBI) of chlorophyll b 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: W | ||||||
Binding site | 75 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 137 | Mg (UniProtKB | ChEBI) of chlorophyll a 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 140 | Mg (UniProtKB | ChEBI) of chlorophyll a 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 177 | chlorophyll a 3 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 200 | Mg (UniProtKB | ChEBI) of chlorophyll b 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 203 | chlorophyll b 4 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 239 | Mg (UniProtKB | ChEBI) of chlorophyll a 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 242 | Mg (UniProtKB | ChEBI) of chlorophyll a 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 244 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 256 | Mg (UniProtKB | ChEBI) of chlorophyll a 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: Q | ||||||
Binding site | 271 | Mg (UniProtKB | ChEBI) of chlorophyll a 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast envelope | |
Cellular Component | chloroplast thylakoid | |
Cellular Component | chloroplast thylakoid membrane | |
Cellular Component | cytosol | |
Cellular Component | photosystem I | |
Cellular Component | photosystem II | |
Cellular Component | thylakoid | |
Molecular Function | chlorophyll binding | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA binding | |
Biological Process | photosynthesis, light harvesting |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameChlorophyll a-b binding protein CP29.2, chloroplastic
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9XF88
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Plastid, chloroplast thylakoid membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 143-163 | Helical | ||||
Sequence: WAMLATLGAITVEWLTGVTWQ | ||||||
Transmembrane | 181-201 | Helical | ||||
Sequence: LPFSISTLIWIEVLVIGYIEF | ||||||
Transmembrane | 245-265 | Helical | ||||
Sequence: LAMVGFLGFAVQAAATGKGPL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-31 | Chloroplast | ||||
Sequence: MAATSTAAAASSIMGTRVVSDISSNSSRFTA | ||||||
Modified residue | 32 | N2-acetylarginine | ||||
Sequence: R | ||||||
Chain | PRO_0000003652 | 32-287 | Chlorophyll a-b binding protein CP29.2, chloroplastic | |||
Sequence: RFGFGTKKASPKKAKTVISDRPLWFPGAKSPEYLDGSLVGDYGFDPFGLGKPAEYLQFDLDSLDQNLAKNLYGEVIGTRTEAVDPKSTPFQPYSEVFGLQRFRECELIHGRWAMLATLGAITVEWLTGVTWQDAGKVELVDGSSYLGQPLPFSISTLIWIEVLVIGYIEFQRNAELDSEKRLYPGGKFFDPLGLASDPVKKAQLQLAEIKHARLAMVGFLGFAVQAAATGKGPLNNWATHLSDPLHTTIIDTFSSS | ||||||
Modified residue | 37 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 109 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 111 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Photoregulated by reversible phosphorylation of its threonine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Domain
The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Sequence similarities
Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9XF88-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length287
- Mass (Da)31,194
- Last updated1999-11-01 v1
- ChecksumCA70FF75292172D4
Q9XF88-2
- Name2
- NoteMay be due to an intron retention.
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF134127 EMBL· GenBank· DDBJ | AAD28774.1 EMBL· GenBank· DDBJ | mRNA | ||
AC010871 EMBL· GenBank· DDBJ | AAF07831.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE74697.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE74698.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY065140 EMBL· GenBank· DDBJ | AAL38316.1 EMBL· GenBank· DDBJ | mRNA | ||
AY081608 EMBL· GenBank· DDBJ | AAM10170.1 EMBL· GenBank· DDBJ | mRNA |