Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chlorophyll a-b binding protein, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 5 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.

Cofactori

Note: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygen2 Publications1
Binding sitei81Chlorophyll-a 1; via amide nitrogen1
Binding sitei87Chlorophyll-a 11
Metal bindingi100Magnesium (chlorophyll-a 1 axial ligand)2 Publications1
Metal bindingi103Magnesium (chlorophyll-a 2 axial ligand)2 Publications1
Binding sitei105Chlorophyll-b 21
Binding sitei138Chlorophyll-a 31
Binding sitei148Chlorophyll-a 3; via amide nitrogen1
Metal bindingi154Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygen2 Publications1
Binding sitei158Chlorophyll-b 31
Binding sitei166Chlorophyll-b 4 or chlorophyll-b 51
Metal bindingi174Magnesium (chlorophyll-b 3 axial ligand)2 Publications1
Binding sitei177Chlorophyll-b 41
Binding sitei183Chlorophyll-b 2; via amide nitrogen1
Binding sitei214Chlorophyll-a 51
Metal bindingi215Magnesium (chlorophyll-a 3 axial ligand)2 Publications1
Metal bindingi218Magnesium (chlorophyll-a 4 axial ligand)2 Publications1
Binding sitei220Chlorophyll-a 11
Metal bindingi232Magnesium (chlorophyll-a 5 axial ligand)2 Publications1
Metal bindingi247Magnesium (chlorophyll-a 6 axial ligand)2 Publications1
Binding sitei256Chlorophyll-a 6; via amide nitrogen1
Binding sitei263Chlorophyll-b 5; via carbonyl oxygen1

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, chloroplastic
Alternative name(s):
LHCII type I CAB
Short name:
LHCP
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei101 – 121HelicalSequence analysisAdd BLAST21
Transmembranei153 – 173HelicalSequence analysisAdd BLAST21
Transmembranei221 – 241HelicalSequence 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
Transit peptidei1 – 35Chloroplast1 PublicationAdd BLAST35
ChainiPRO_000000370036 – 267Chlorophyll a-b binding protein, chloroplasticAdd BLAST232

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36N2-acetylarginine1 Publication1
Modified residuei38Phosphothreonine1 Publication1

Post-translational modificationi

Photoregulated by reversible phosphorylation of its threonine residues.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP12333.

PTM databases

iPTMnetiP12333.

Interactioni

Subunit structurei

The LHC complex consists of chlorophyll a-b binding proteins.1 Publication

Protein-protein interaction databases

DIPiDIP-62013N.

Structurei

Secondary structure

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi51 – 53Combined sources3
Helixi61 – 63Combined sources3
Helixi90 – 121Combined sources32
Turni122 – 124Combined sources3
Turni132 – 134Combined sources3
Helixi135 – 140Combined sources6
Helixi147 – 149Combined sources3
Helixi159 – 179Combined sources21
Beta strandi187 – 190Combined sources4
Helixi194 – 196Combined sources3
Helixi205 – 236Combined sources32
Helixi240 – 249Combined sources10
Turni251 – 253Combined sources3
Helixi256 – 259Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RWTX-ray2.72A/B/C/D/E/F/G/H/I/J36-267[»]
3JCUelectron microscopy3.20G/N/Y/g/n/y1-267[»]
4LCZX-ray2.60A/B/C44-267[»]
ProteinModelPortaliP12333.
SMRiP12333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12333.

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.

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.

P12333-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSTMALSS PSLAGKAVKL GPTASEIIGE GRITMRKTAG KPKTVQSSSP
60 70 80 90 100
WYGPDRVKYL GPFSGESPSY LTGEFPGDYG WDTAGLSADP ETFAKNRELE
110 120 130 140 150
VIHCRWAMLG ALGCVFPELL ARNGVKFGEA VWFKAGSQIF SEGGLDYLGN
160 170 180 190 200
PSLVHAQSIL AIWACQVILM GAVEGYRIAG GPLGEVVDPL YPGGSFDPLG
210 220 230 240 250
LADDPEAFAE LKVKEIKNGR LAMFSMFGFF VQAIVTGKGP LENLADHLAD
260
PVNNNAWNFA TNFVPGK
Length:267
Mass (Da):28,424
Last modified:October 1, 1989 - v1
Checksum:i23474EBDA23F6545
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14341 mRNA. Translation: CAA32526.1.
PIRiJQ0020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14341 mRNA. Translation: CAA32526.1.
PIRiJQ0020.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RWTX-ray2.72A/B/C/D/E/F/G/H/I/J36-267[»]
3JCUelectron microscopy3.20G/N/Y/g/n/y1-267[»]
4LCZX-ray2.60A/B/C44-267[»]
ProteinModelPortaliP12333.
SMRiP12333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-62013N.

PTM databases

iPTMnetiP12333.

Proteomic databases

PRIDEiP12333.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP12333.

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 nameiCB2A_SPIOL
AccessioniPrimary (citable) accession number: P12333
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 2, 2016
This is version 101 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.