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Protein

Chlorophyll a-b binding protein AB80, chloroplastic

Gene

AB80

Organism
Pisum sativum (Garden pea)
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.1 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi61Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygenCombined sources1 Publication1
Binding sitei83Chlorophyll-a 1; via amide nitrogenCombined sources1 Publication1
Binding sitei89Chlorophyll-a 1Combined sources1 Publication1
Metal bindingi102Magnesium (chlorophyll-a 1 axial ligand)Combined sources1 Publication1
Metal bindingi105Magnesium (chlorophyll-a 2 axial ligand)Combined sources1 Publication1
Binding sitei107Chlorophyll-b 2Combined sources1 Publication1
Binding sitei140Chlorophyll-a 3Combined sources1 Publication1
Binding sitei150Chlorophyll-a 3; via amide nitrogenCombined sources1 Publication1
Metal bindingi156Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygenCombined sources1 Publication1
Binding sitei160Chlorophyll-b 3Combined sources1 Publication1
Binding sitei168Chlorophyll-b 4 or chlorophyll-b 5Combined sources1 Publication1
Metal bindingi176Magnesium (chlorophyll-b 3 axial ligand)Combined sources1 Publication1
Binding sitei179Chlorophyll-b 4Combined sources1 Publication1
Binding sitei185Chlorophyll-b 2; via amide nitrogenCombined sources1 Publication1
Binding sitei216Chlorophyll-a 5Combined sources1 Publication1
Metal bindingi217Magnesium (chlorophyll-a 3 axial ligand)Combined sources1 Publication1
Metal bindingi220Magnesium (chlorophyll-a 4 axial ligand)Combined sources1 Publication1
Binding sitei222Chlorophyll-a 1Combined sources1 Publication1
Metal bindingi234Magnesium (chlorophyll-a 5 axial ligand)Combined sources1 Publication1
Metal bindingi249Magnesium (chlorophyll-a 6 axial ligand)Combined sources1 Publication1
Binding sitei258Chlorophyll-a 6; via amide nitrogenCombined sources1 Publication1
Binding sitei265Chlorophyll-b 5; via carbonyl oxygenCombined sources1 Publication1

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 AB80, chloroplastic
Alternative name(s):
LHCII type I CAB-AB80
Short name:
LHCP
Gene namesi
Name:AB80
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeHologaleginaIRL cladeFabeaePisum

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
Transmembranei103 – 123HelicalSequence analysisAdd BLAST21
Transmembranei155 – 175HelicalSequence analysisAdd BLAST21
Transmembranei223 – 243HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi102E → A: Decreases binding to chlorophyll-b. 2 Publications1
Mutagenesisi102E → Q: Causes a strong decrease in LHCII complex stability; when associated with L-105. 2 Publications1
Mutagenesisi105H → A: Decreases binding to chlorophyll-a. 2 Publications1
Mutagenesisi105H → F: Decreases binding to chlorophyll, more chlorophyll-a than chlorophyll-b is lost. Causes a strong decrease in LHCII complex stability. 2 Publications1
Mutagenesisi105H → L: Decreases binding to chlorophyll, more chlorophyll-a than chlorophyll-b is lost. Causes a strong decrease in LHCII complex stability. Complex stability is reduced further; when associated with Q-102. 2 Publications1
Mutagenesisi114 – 115LG → VF: Decreases binding to chlorophyll-b. 1 Publication2
Mutagenesisi168Q → A: Decreases binding to chlorophyll-b. 2 Publications1
Mutagenesisi168Q → E or S: Decreases binding to chlorophyll, more chlorophyll-b than chlorophyll-a is lost. Causes a strong decrease in LHCII complex stability. 2 Publications1
Mutagenesisi176E → A: Decreases binding to chlorophyll-b. 1 Publication1
Mutagenesisi217E → A: Decreases binding to chlorophyll-a. 1 Publication1
Mutagenesisi220N → A: Decreases binding to chlorophyll-a and possibly chlorophyll-b. 1 Publication1
Mutagenesisi234Q → E or S: Decreases binding to chlorophyll. Causes a moderate decrease in LHCII complex stability. 2 Publications1
Mutagenesisi234Q → L: Decreases binding to chlorophyll-a. 2 Publications1
Mutagenesisi249H → A: Decreases binding to chlorophyll-a. 2 Publications1
Mutagenesisi249H → F or L: Decreases binding to chlorophyll-a and chlorophyll-b. Causes a minor decrease in LHCII complex stability. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 37ChloroplastCuratedAdd BLAST37
ChainiPRO_000000368038 – 269Chlorophyll a-b binding protein AB80, chloroplasticAdd BLAST232

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38N2-acetylarginineBy similarity1

Post-translational modificationi

Photoregulated by reversible phosphorylation of its threonine residues.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP07371

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CAOO222657EBI-2353186,EBI-780656From Arabidopsis thaliana.

Protein-protein interaction databases

DIPiDIP-40897N
IntActiP07371, 3 interactors

Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP07371
SMRiP07371
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07371

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.

P07371-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAASSSSSMA LSSPTLAGKQ LKLNPSSQEL GAARFTMRKS ATTKKVASSG
60 70 80 90 100
SPWYGPDRVK YLGPFSGESP SYLTGEFPGD YGWDTAGLSA DPETFSKNRE
110 120 130 140 150
LEVIHSRWAM LGALGCVFPE LLSRNGVKFG EAVWFKAGSQ IFSEGGLDYL
160 170 180 190 200
GNPSLVHAQS ILAIWATQVI LMGAVEGYRI AGGPLGEVVD PLYPGGSFDP
210 220 230 240 250
LGLADDPEAF AELKVKELKN GRLAMFSMFG FFVQAIVTGK GPLENLADHL
260
ADPVNNNAWS YATNFVPGK
Length:269
Mass (Da):28,654
Last modified:April 1, 1988 - v1
Checksum:iD2BD6A9EFC4BAF77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02067 Genomic DNA Translation: AAA33651.1
M64619 Genomic DNA Translation: AAA63413.1
PIRiA26780 CDPM80

Similar proteinsi

Entry informationi

Entry nameiCB22_PEA
AccessioniPrimary (citable) accession number: P07371
Secondary accession number(s): P35389, Q53X02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: September 12, 2018
This is version 107 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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