P07371 · CB22_PEA
- ProteinChlorophyll a-b binding protein AB80, chloroplastic
- GeneAB80
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids269 (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.
May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.
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 | 61 | Mg (UniProtKB | ChEBI) of chlorophyll b 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: Y | ||||||
Binding site | 83 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 89 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 102 | Mg (UniProtKB | ChEBI) of chlorophyll a 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 105 | Mg (UniProtKB | ChEBI) of chlorophyll a 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 107 | chlorophyll b 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 140 | chlorophyll a 3 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 150 | chlorophyll a 3 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 156 | Mg (UniProtKB | ChEBI) of chlorophyll b 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: V | ||||||
Binding site | 160 | chlorophyll b 3 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 168 | chlorophyll b 4 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 168 | chlorophyll b 5 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 176 | Mg (UniProtKB | ChEBI) of chlorophyll b 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 179 | chlorophyll b 4 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 185 | chlorophyll b 2 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 216 | chlorophyll a 5 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 217 | Mg (UniProtKB | ChEBI) of chlorophyll a 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 220 | Mg (UniProtKB | ChEBI) of chlorophyll a 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: N | ||||||
Binding site | 222 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 234 | Mg (UniProtKB | ChEBI) of chlorophyll a 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: Q | ||||||
Binding site | 249 | Mg (UniProtKB | ChEBI) of chlorophyll a 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 258 | chlorophyll a 6 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 265 | chlorophyll b 5 (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast thylakoid membrane | |
Cellular Component | photosystem I | |
Cellular Component | photosystem II | |
Molecular Function | chlorophyll binding | |
Molecular Function | metal ion binding | |
Biological Process | photosynthesis, light harvesting |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameChlorophyll a-b binding protein AB80, chloroplastic
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Fabeae > Pisum
Accessions
- Primary accessionP07371
- Secondary accessions
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 | 103-123 | Helical | ||||
Sequence: VIHSRWAMLGALGCVFPELLS | ||||||
Transmembrane | 155-175 | Helical | ||||
Sequence: LVHAQSILAIWATQVILMGAV | ||||||
Transmembrane | 223-243 | Helical | ||||
Sequence: LAMFSMFGFFVQAIVTGKGPL |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 102 | Decreases binding to chlorophyll-b. | ||||
Sequence: E → A | ||||||
Mutagenesis | 102 | Causes a strong decrease in LHCII complex stability; when associated with L-105. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 105 | Decreases binding to chlorophyll-a. | ||||
Sequence: H → A | ||||||
Mutagenesis | 105 | Decreases binding to chlorophyll, more chlorophyll-a than chlorophyll-b is lost. Causes a strong decrease in LHCII complex stability. | ||||
Sequence: H → F | ||||||
Mutagenesis | 105 | Decreases binding to chlorophyll, more chlorophyll-a than chlorophyll-b is lost. Causes a strong decrease in LHCII complex stability. Complex stability is reduced further; when associated with Q-102. | ||||
Sequence: H → L | ||||||
Mutagenesis | 114-115 | Decreases binding to chlorophyll-b. | ||||
Sequence: LG → VF | ||||||
Mutagenesis | 168 | Decreases binding to chlorophyll-b. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 168 | Decreases binding to chlorophyll, more chlorophyll-b than chlorophyll-a is lost. Causes a strong decrease in LHCII complex stability. | ||||
Sequence: Q → E or S | ||||||
Mutagenesis | 176 | Decreases binding to chlorophyll-b. | ||||
Sequence: E → A | ||||||
Mutagenesis | 217 | Decreases binding to chlorophyll-a. | ||||
Sequence: E → A | ||||||
Mutagenesis | 220 | Decreases binding to chlorophyll-a and possibly chlorophyll-b. | ||||
Sequence: N → A | ||||||
Mutagenesis | 234 | Decreases binding to chlorophyll. Causes a moderate decrease in LHCII complex stability. | ||||
Sequence: Q → E or S | ||||||
Mutagenesis | 234 | Decreases binding to chlorophyll-a. | ||||
Sequence: Q → L | ||||||
Mutagenesis | 249 | Decreases binding to chlorophyll-a. | ||||
Sequence: H → A | ||||||
Mutagenesis | 249 | Decreases binding to chlorophyll-a and chlorophyll-b. Causes a minor decrease in LHCII complex stability. | ||||
Sequence: H → F or L |
PTM/Processing
Features
Showing features for transit peptide, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-37 | Chloroplast | ||||
Sequence: MAASSSSSMALSSPTLAGKQLKLNPSSQELGAARFTM | ||||||
Modified residue | 38 | N2-acetylarginine | ||||
Sequence: R | ||||||
Chain | PRO_0000003680 | 38-269 | Chlorophyll a-b binding protein AB80, chloroplastic | |||
Sequence: RKSATTKKVASSGSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFSKNRELEVIHSRWAMLGALGCVFPELLSRNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLADDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWSYATNFVPGK |
Post-translational modification
Photoregulated by reversible phosphorylation of its threonine residues.
Keywords
- PTM
Interaction
Subunit
The LHC complex consists of chlorophyll a-b binding proteins.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P07371 | CAO O22265 | 7 | EBI-2353186, EBI-780656 |
Protein-protein interaction 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
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length269
- Mass (Da)28,654
- Last updated1988-04-01 v1
- ChecksumD2BD6A9EFC4BAF77
Keywords
- Technical term