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Protein

Chlorophyll a-b binding protein P4, chloroplastic

Gene

lhcA-P4

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.Curated1 Publication
May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.1 Publication

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi56Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygenBy similarity1
Binding sitei76Chlorophyll-a 1; via amide nitrogenBy similarity1
Metal bindingi95Magnesium (chlorophyll-a 1 axial ligand)By similarity1
Binding sitei100Chlorophyll-b 2By similarity1
Binding sitei137Chlorophyll-b 3By similarity1
Metal bindingi143Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygenBy similarity1
Metal bindingi153Magnesium (chlorophyll-b 3 axial ligand)By similarity1
Binding sitei156Chlorophyll-b 4By similarity1
Binding sitei203Chlorophyll-a 5By similarity1
Metal bindingi204Magnesium (chlorophyll-a 3 axial ligand)By similarity1
Metal bindingi207Magnesium (chlorophyll-a 4 axial ligand)By similarity1
Binding sitei209Chlorophyll-a 1By similarity1
Metal bindingi221Magnesium (chlorophyll-a 5 axial ligand)By similarity1
Metal bindingi236Magnesium (chlorophyll-a 6 axial ligand)By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Photosynthesis

Keywords - Ligandi

Chlorophyll, Chromophore, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Chlorophyll a-b binding protein P4, chloroplastic
Alternative name(s):
LHCI type III CAB-P4
Gene namesi
Name:lhcA-P4Imported
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei101 – 121HelicalSequence analysisAdd BLAST21
Transmembranei134 – 154HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Photosystem I, Photosystem II, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000310860? – 252Chlorophyll a-b binding protein P4, chloroplastic
Transit peptidei1 – ?ChloroplastCurated

Post-translational modificationi

Photoregulated by reversible phosphorylation of its threonine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ9SQL2.

Expressioni

Inductioni

Down-regulated by UV-B.1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-60296N.

Structurei

Secondary structure

1252
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 60Combined sources5
Helixi85 – 117Combined sources33
Helixi126 – 128Combined sources3
Beta strandi129 – 132Combined sources4
Beta strandi134 – 136Combined sources3
Helixi138 – 161Combined sources24
Turni163 – 165Combined sources3
Beta strandi169 – 175Combined sources7
Helixi180 – 183Combined sources4
Helixi187 – 189Combined sources3
Beta strandi190 – 192Combined sources3
Helixi198 – 225Combined sources28
Helixi229 – 238Combined sources10
Turni240 – 242Combined sources3
Helixi245 – 248Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4RKUX-ray3.00453-248[»]
4XK8X-ray2.804/954-249[»]
4Y28X-ray2.8041-252[»]
ProteinModelPortaliQ9SQL2.
SMRiQ9SQL2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SQL2.

Family & Domainsi

Domaini

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.Curated

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.10.3460.10. 1 hit.
InterProiIPR001344. Chloro_AB-bd_pln.
IPR022796. Chloroa_b-bind.
IPR023329. Chlorophyll_a/b-bd_dom.
[Graphical view]
PANTHERiPTHR21649. PTHR21649. 1 hit.
PfamiPF00504. Chloroa_b-bind. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SQL2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVTTQASA AIFGPCGLKS RFLGGSSGKL NRGVAFRPVG CSPSASFKVE
60 70 80 90 100
AKKGEWLPGL ASPGYLTGSL PGDNGFDPLG LAEDPENLRW FVQAELVNGR
110 120 130 140 150
WAMLGVAGML LPEVFTSIGI INVPKWYAAG KEEYFASSST LFVIEFILSH
160 170 180 190 200
YVEIRRWQDI KNPGSVNQDP IFKQYSLPAG EVGYPGGIFN PLNFAPTLEA
210 220 230 240 250
KEKEIANGRL AMLAFLGFII QHNVTGKGPF DNLLQHISDP WHNTIVQTLG

GN
Length:252
Mass (Da):27,229
Last modified:May 1, 2000 - v1
Checksum:i00B7D26C82F6667A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti128A → D in ABN49455 (Ref. 2) Curated1
Sequence conflicti149S → F in ABN49455 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF002248 mRNA. Translation: AAF13731.1.
EF208907 mRNA. Translation: ABN49455.1.
PIRiT51616.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF002248 mRNA. Translation: AAF13731.1.
EF208907 mRNA. Translation: ABN49455.1.
PIRiT51616.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4RKUX-ray3.00453-248[»]
4XK8X-ray2.804/954-249[»]
4Y28X-ray2.8041-252[»]
ProteinModelPortaliQ9SQL2.
SMRiQ9SQL2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60296N.

Proteomic databases

PRIDEiQ9SQL2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SQL2.

Family and domain databases

Gene3Di1.10.3460.10. 1 hit.
InterProiIPR001344. Chloro_AB-bd_pln.
IPR022796. Chloroa_b-bind.
IPR023329. Chlorophyll_a/b-bd_dom.
[Graphical view]
PANTHERiPTHR21649. PTHR21649. 1 hit.
PfamiPF00504. Chloroa_b-bind. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCB24_PEA
AccessioniPrimary (citable) accession number: Q9SQL2
Secondary accession number(s): A3F6K3, P35386
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.