Q8VZ87 · CB1B_ARATH
- ProteinChlorophyll a-b binding protein 3, chloroplastic
- GeneLHCB1.2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids267 (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.
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 | 58 | Mg (UniProtKB | ChEBI) of chlorophyll b 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: Y | ||||||
Binding site | 80 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 86 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 99 | Mg (UniProtKB | ChEBI) of chlorophyll a 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 102 | Mg (UniProtKB | ChEBI) of chlorophyll a 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 104 | chlorophyll b 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 137 | chlorophyll a 3 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 147 | chlorophyll a 3 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 153 | Mg (UniProtKB | ChEBI) of chlorophyll b 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: V | ||||||
Binding site | 157 | chlorophyll b 3 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 165 | chlorophyll b 4 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 165 | chlorophyll b 5 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 173 | Mg (UniProtKB | ChEBI) of chlorophyll b 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 176 | chlorophyll b 4 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 183 | chlorophyll b 2 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 214 | chlorophyll a 5 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 215 | Mg (UniProtKB | ChEBI) of chlorophyll a 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 218 | Mg (UniProtKB | ChEBI) of chlorophyll a 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: N | ||||||
Binding site | 220 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 232 | Mg (UniProtKB | ChEBI) of chlorophyll a 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: Q | ||||||
Binding site | 247 | Mg (UniProtKB | ChEBI) of chlorophyll a 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 256 | chlorophyll a 6 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 263 | chlorophyll b 5 (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast thylakoid | |
Cellular Component | chloroplast thylakoid membrane | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Cellular Component | photosystem I | |
Cellular Component | photosystem II | |
Cellular Component | plastoglobule | |
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 3, chloroplastic
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8VZ87
- Secondary accessions
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 | 100-120 | Helical | ||||
Sequence: VIHSRWAMLGALGCVFPELLA | ||||||
Transmembrane | 152-172 | Helical | ||||
Sequence: LVHAQSILAIWATQVILMGAV | ||||||
Transmembrane | 221-241 | Helical | ||||
Sequence: LAMFSMFGFFVQAIVTGKGPI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-35 | Chloroplast | ||||
Sequence: MAASTMALSSPAFAGKAVNLSPAASEVLGSGRVTM | ||||||
Modified residue | 36 | N2-acetylarginine | ||||
Sequence: R | ||||||
Chain | PRO_0000403938 | 36-267 | Chlorophyll a-b binding protein 3, chloroplastic | |||
Sequence: RKTVAKPKGPSGSPWYGSDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFARNRELEVIHSRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSDGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRVAGNGPLGEAEDLLYPGGSFDPLGLATDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGPIENLADHLADPVNNNAWAFATNFVPGK | ||||||
Modified residue | 38 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Photoregulated by reversible phosphorylation of its threonine residues.
Keywords
- PTM
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
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length267
- Mass (Da)28,227
- Last updated2011-01-11 v2
- ChecksumCEF0664E98F0B0BA
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 181 | in Ref. 4; AAM47913/AAL38341 | ||||
Sequence: G → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X03908 EMBL· GenBank· DDBJ | CAA27541.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X03908 EMBL· GenBank· DDBJ | CAA27542.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC008030 EMBL· GenBank· DDBJ | AAG10605.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE31149.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY065165 EMBL· GenBank· DDBJ | AAL38341.1 EMBL· GenBank· DDBJ | mRNA | ||
AY114594 EMBL· GenBank· DDBJ | AAM47913.1 EMBL· GenBank· DDBJ | mRNA |