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Q9SQL2 (CB24_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chlorophyll a-b binding protein P4, chloroplastic
Alternative name(s):
LHCI type III CAB-P4
Gene names
Name:lhcA-P4
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3

May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen. Ref.3

Cofactor

Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin By similarity. UniProtKB P07371

Subunit structure

The LHC complex consists of chlorophyll a-b binding proteins.

Subcellular location

Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein.

Induction

Down-regulated by UV-B. Ref.1

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.

Post-translational modification

Photoregulated by reversible phosphorylation of its threonine residues By similarity. UniProtKB P07371

Sequence similarities

Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 252Chlorophyll a-b binding protein P4, chloroplasticPRO_0000310860

Regions

Transmembrane101 – 12121Helical; Potential
Transmembrane134 – 15421Helical; Potential

Sites

Metal binding561Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygen By similarity UniProtKB P27521
Metal binding951Magnesium (chlorophyll-a 1 axial ligand) By similarity UniProtKB P07371
Metal binding1431Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygen By similarity UniProtKB P27521
Metal binding1531Magnesium (chlorophyll-b 3 axial ligand) By similarity UniProtKB P27521
Metal binding2041Magnesium (chlorophyll-a 3 axial ligand) By similarity UniProtKB P07371
Metal binding2071Magnesium (chlorophyll-a 4 axial ligand) By similarity UniProtKB P07371
Metal binding2211Magnesium (chlorophyll-a 5 axial ligand) By similarity UniProtKB P07371
Metal binding2361Magnesium (chlorophyll-a 6 axial ligand) By similarity UniProtKB P07371
Binding site761Chlorophyll-a 1; via amide nitrogen By similarity UniProtKB P27521
Binding site1001Chlorophyll-b 2 By similarity UniProtKB P07371
Binding site1371Chlorophyll-b 3 By similarity UniProtKB P27521
Binding site1561Chlorophyll-b 4 By similarity UniProtKB P27521
Binding site2031Chlorophyll-a 5 By similarity UniProtKB P07371
Binding site2091Chlorophyll-a 1 By similarity UniProtKB P07371

Experimental info

Sequence conflict1281A → D in ABN49455. Ref.2
Sequence conflict1491S → F in ABN49455. Ref.2

Secondary structure

1 ................................. 252
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9SQL2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 00B7D26C82F6667A

FASTA25227,229
        10         20         30         40         50         60 
MATVTTQASA AIFGPCGLKS RFLGGSSGKL NRGVAFRPVG CSPSASFKVE AKKGEWLPGL 

        70         80         90        100        110        120 
ASPGYLTGSL PGDNGFDPLG LAEDPENLRW FVQAELVNGR WAMLGVAGML LPEVFTSIGI 

       130        140        150        160        170        180 
INVPKWYAAG KEEYFASSST LFVIEFILSH YVEIRRWQDI KNPGSVNQDP IFKQYSLPAG 

       190        200        210        220        230        240 
EVGYPGGIFN PLNFAPTLEA KEKEIANGRL AMLAFLGFII QHNVTGKGPF DNLLQHISDP 

       250 
WHNTIVQTLG GN

« Hide

References

[1]"Molecular markers for UV-B stress in plants: alteration of the expression of four classes of genes in Pisum sativum and the formation of high molecular mass RNA adducts."
Brosche M., Fant C., Bergkvist S.W., Strid H., Svensk A., Olsson O., Strid A.
Biochim. Biophys. Acta 1447:185-198(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Strain: cv. Greenfeast.
Tissue: Leaf.
[2]"Interacting partner of calcineurin B-like interacting protein kinase (CIPK) (partial homolog of photosystem I light harvesting chlorophyll a/b binding protein) from Pisum sativum."
Gupta S., Tuteja N.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-252.
[3]"Dicyclohexylcarbodiimide-binding proteins related to the short circuit of the proton-pumping activity of photosystem II. Identified as light-harvesting chlorophyll-a/b-binding proteins."
Jahns P., Junge W.
Eur. J. Biochem. 193:731-736(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 110-124, FUNCTION.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF002248 mRNA. Translation: AAF13731.1.
EF208907 mRNA. Translation: ABN49455.1.
PIRT51616.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YO9model-41-252[»]
2O01X-ray3.40485-249[»]
2WSCX-ray3.3041-252[»]
2WSEX-ray3.4941-252[»]
2WSFX-ray3.4841-252[»]
3LW5X-ray3.30481-247[»]
ProteinModelPortalQ9SQL2.
SMRQ9SQL2. Positions 85-249.
ModBaseSearch...

Proteomic databases

ProMEXQ9SQL2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.3460.10. 1 hit.
InterProIPR001344. Chloro_AB-bd_pln.
IPR022796. Chloroa_b-bind.
IPR023329. Chlorophyll_a/b-bd_dom.
[Graphical view]
PANTHERPTHR21649. PTHR21649. 1 hit.
PfamPF00504. Chloroa_b-bind. 1 hit.
[Graphical view]
SUPFAMSSF103511. SSF103511. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9SQL2.

Entry information

Entry nameCB24_PEA
AccessionPrimary (citable) accession number: Q9SQL2
Secondary accession number(s): A3F6K3, P35386
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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