Q9C639 · LHCA5_ARATH
- ProteinPhotosystem I chlorophyll a/b-binding protein 5, chloroplastic
- GeneLHCA5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids256 (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 (PubMed:15563470, PubMed:21806943).
Seems involved in the function of the photosystem I in low light conditions, when other LHCA proteins are less abundant (PubMed:15356385).
Required, together with LHCA6, for the formation of a full-size NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI) that triggers cyclic and chlororespiratory electron transport in chloroplast thylakoids, especially under stress conditions (e.g. increased light intensity) (Probable) (PubMed:19903870, PubMed:21278308).
Seems involved in the function of the photosystem I in low light conditions, when other LHCA proteins are less abundant (PubMed:15356385).
Required, together with LHCA6, for the formation of a full-size NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI) that triggers cyclic and chlororespiratory electron transport in chloroplast thylakoids, especially under stress conditions (e.g. increased light intensity) (Probable) (PubMed:19903870, PubMed:21278308).
Miscellaneous
Light emission at 684 nm upon excitation at 410 and 470 nm.
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 | 49 | Mg (UniProtKB | ChEBI) of chlorophyll b 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: W | ||||||
Binding site | 69 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 88 | Mg (UniProtKB | ChEBI) of chlorophyll a 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 93 | chlorophyll b 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 147 | Mg (UniProtKB | ChEBI) of chlorophyll b 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 150 | chlorophyll b 4 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 205 | chlorophyll a 5 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 206 | Mg (UniProtKB | ChEBI) of chlorophyll a 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: E | ||||||
Binding site | 209 | Mg (UniProtKB | ChEBI) of chlorophyll a 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: N | ||||||
Binding site | 211 | chlorophyll a 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 223 | Mg (UniProtKB | ChEBI) of chlorophyll a 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: Q | ||||||
Binding site | 238 | Mg (UniProtKB | ChEBI) of chlorophyll a 6 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast thylakoid membrane | |
Cellular Component | photosystem I antenna complex | |
Molecular Function | chlorophyll binding | |
Molecular Function | metal ion binding | |
Molecular Function | pigment binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | photosynthesis, light harvesting in photosystem I | |
Biological Process | response to cold | |
Biological Process | response to high light intensity | |
Biological Process | response to low light intensity stimulus |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended namePhotosystem I chlorophyll a/b-binding protein 5, chloroplastic
- Short namesLhca5
- 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 accessionQ9C639
- 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 | 94-113 | Helical | ||||
Sequence: FAMLGVAGILFTDLLRTTGI | ||||||
Transmembrane | 129-146 | Helical | ||||
Sequence: FASTKTLIVVQFLLMGFA | ||||||
Transmembrane | 212-232 | Helical | ||||
Sequence: LAMMAMLGFFVQASVTHTGPI |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Slightly lower NDH activity in immature leaves. Smaller version of the NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI) supercomplex (PubMed:19903870).
In the double mutant lhca5 lhca6, drastic reduction of NDH subunits accumulation upon increased light intensity (PubMed:21278308).
In the double mutant lhca5 lhca6, drastic reduction of NDH subunits accumulation upon increased light intensity (PubMed:21278308).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 31 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-32 | Chloroplast | ||||
Sequence: MAVVLRGGITGGFLHHRRDASSVITRRISSVK | ||||||
Modified residue | 33 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000435449 | 33-256 | Photosystem I chlorophyll a/b-binding protein 5, chloroplastic | |||
Sequence: AAGGGINPTVAVERATWLPGLNPPPYLDGNLAGDYGFDPLGLGEDPESLKWYVQAELVHSRFAMLGVAGILFTDLLRTTGIRNLPVWYEAGAVKFDFASTKTLIVVQFLLMGFAETKRYMDFVSPGSQAKEGSFFFGLEAALEGLEPGYPGGPLLNPLGLAKDVQNAHDWKLKEIKNGRLAMMAMLGFFVQASVTHTGPIDNLVEHLSNPWHKTIIQTLFTSTS |
Post-translational modification
Photoregulated by reversible phosphorylation of its threonine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Induced by high light (HL) but repressed by low light (LL). Slightly inhibited by cold.
Gene expression databases
Interaction
Subunit
The LHC complex consists of chlorophyll a-b binding proteins (PubMed:19139095).
Homodimer. Heterodimer with LHCA2 and, possibly, LHCA3 (PubMed:15356385, PubMed:17107674).
Can substitute to LHCA4 to form a complex with LHCA1 (PubMed:15563470, PubMed:21806943).
Binds pigments (PubMed:15563470).
Element of the NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI) (PubMed:19903870).
Homodimer. Heterodimer with LHCA2 and, possibly, LHCA3 (PubMed:15356385, PubMed:17107674).
Can substitute to LHCA4 to form a complex with LHCA1 (PubMed:15563470, PubMed:21806943).
Binds pigments (PubMed:15563470).
Element of the NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI) (PubMed:19903870).
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
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length256
- Mass (Da)27,802
- Last updated2001-06-01 v1
- ChecksumA68A682632C01631
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 131 | in Ref. 1; AAD28768 | ||||
Sequence: S → C | ||||||
Sequence conflict | 170 | in Ref. 6; AAM65689 | ||||
Sequence: L → I | ||||||
Sequence conflict | 197 | in Ref. 6; AAM65689 | ||||
Sequence: Q → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF134121 EMBL· GenBank· DDBJ | AAD28768.1 EMBL· GenBank· DDBJ | mRNA | ||
AC083835 EMBL· GenBank· DDBJ | AAG50618.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE32117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE32118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY062097 EMBL· GenBank· DDBJ | AAL32974.1 EMBL· GenBank· DDBJ | mRNA | ||
AY090263 EMBL· GenBank· DDBJ | AAL90924.1 EMBL· GenBank· DDBJ | mRNA | ||
AK221694 EMBL· GenBank· DDBJ | BAD95402.1 EMBL· GenBank· DDBJ | mRNA | ||
AY088144 EMBL· GenBank· DDBJ | AAM65689.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316926 EMBL· GenBank· DDBJ | BAH19631.1 EMBL· GenBank· DDBJ | mRNA |