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Protein

Chlorophyll a-b binding protein, chloroplastic

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

Keywordsi

Biological processPhotosynthesis
LigandChlorophyll, 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei101 – 121HelicalSequence analysisAdd BLAST21
Transmembranei153 – 173HelicalSequence analysisAdd BLAST21
Transmembranei221 – 241HelicalSequence analysisAdd BLAST21

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

CarbonylDBiP12333
iPTMnetiP12333

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-62013N
IntActiP12333, 1 interactor

Structurei

Secondary structure

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
InterProiView protein in InterPro
IPR001344 Chloro_AB-bd_pln
IPR022796 Chloroa_b-bind
IPR023329 Chlorophyll_a/b-bd_dom_sf
PANTHERiPTHR21649 PTHR21649, 1 hit
PfamiView protein in Pfam
PF00504 Chloroa_b-bind, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCB2A_SPIOL
AccessioniPrimary (citable) accession number: P12333
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 28, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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