Chlorophyll a-b binding protein, chloroplastic precursor

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P92919 (CB23_APIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Chlorophyll a-b binding protein, chloroplastic

Alternative name(s):
Allergen=Api g 3

Gene names

Name:

LHC0

Organism

Apium graveolens (Celery)

Taxonomic identifier

4045 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Apiales › Apiaceae › Apioideae › apioid superclade › Apieae › Apium

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Cofactor	Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin By similarity.
Subunit structure	The LHC complex consists of chlorophyll a-b binding proteins.
Subcellular location	Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein.
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.
Allergenic properties	Causes an allergic reaction in human.
Sequence similarities	Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.

Ontologies

Keywords
Biological process	Photosynthesis
Cellular component	Chloroplast Membrane Photosystem I Photosystem II Plastid Thylakoid
Disease	Allergen
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	Chlorophyll Chromophore Magnesium Metal-binding
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological_process	photosynthesis, light harvesting Inferred from electronic annotation. Source: InterPro protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW photosystem I Inferred from electronic annotation. Source: UniProtKB-KW photosystem II Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	chlorophyll binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 35

Chloroplast Potential

Chain

36 – 264

229

Chlorophyll a-b binding protein, chloroplastic

PRO_0000003646

Regions

Transmembrane

98 – 118

Helical; Potential

Transmembrane

150 – 170

Helical; Potential

Transmembrane

218 – 238

Helical; Potential

Sites

Metal binding

Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygen By similarity

Metal binding

Magnesium (chlorophyll-a 1 axial ligand) By similarity

Metal binding

100

Magnesium (chlorophyll-a 2 axial ligand) By similarity

Metal binding

151

Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygen By similarity

Metal binding

171

Magnesium (chlorophyll-b 3 axial ligand) By similarity

Metal binding

212

Magnesium (chlorophyll-a 3 axial ligand) By similarity

Metal binding

215

Magnesium (chlorophyll-a 4 axial ligand) By similarity

Metal binding

229

Magnesium (chlorophyll-a 5 axial ligand) By similarity

Metal binding

244

Magnesium (chlorophyll-a 6 axial ligand) By similarity

Binding site

Chlorophyll-a 1; via amide nitrogen By similarity

Binding site

Chlorophyll-a 1 By similarity

Binding site

102

Chlorophyll-b 2 By similarity

Binding site

135

Chlorophyll-a 3 By similarity

Binding site

145

Chlorophyll-a 3; via amide nitrogen By similarity

Binding site

155

Chlorophyll-b 3 By similarity

Binding site

163

Chlorophyll-b 4 or chlorophyll-b 5 By similarity

Binding site

174

Chlorophyll-b 4 By similarity

Binding site

180

Chlorophyll-b 2; via amide nitrogen By similarity

Binding site

211

Chlorophyll-a 5 By similarity

Binding site

217

Chlorophyll-a 1 By similarity

Binding site

253

Chlorophyll-a 6; via amide nitrogen By similarity

Binding site

260

Chlorophyll-b 5; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue

N2-acetylarginine By similarity

Modified residue

Phosphothreonine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P92919 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 07126C7D5D86BA66
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FASTA

264

28,076

        10         20         30         40         50         60 
MAASTMALSS PALAGKAVKV APSSSELFGN GRVSMRKTVK APVSDSPWYG PDRVKYLGPF 

        70         80         90        100        110        120 
SGEAPSYLTG EFPGDYGWDT AGLSADPETF AKNRELEVIH SRWAMLGALG CVFPELLARN 

       130        140        150        160        170        180 
GVKFGEAVWF KAGSQIFSEG GLDYLGNPSL VHAQSILSIW ATQVILMGAV EGYRVAGGPL 

       190        200        210        220        230        240 
GEIVDPLYPG GSFDPLGLAE DPERSAELKV KELKNGRLAM FSMFGFFVQA IVTGKGPLEN 

       250        260 
LADHLADPVN NNAWAFATNF VPGK

« Hide

References

[1]

"Characterization of a chlorophyll ab binding protein from celery as a food allergen Api g 3."
Hoffmann-Sommergruber K., Pec M., Ferris R., O'Riordain G., Ebner C., Scheiner O., Breiteneder H.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bulb.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z75663 mRNA. Translation: CAA99993.1.
3D structure databases
ProteinModelPortal	P92919.
SMR	P92919. Positions 46-264.
ModBase	Search...
Protein family/group databases
Allergome	3086. Api g 3.0101. 774. Api g 3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.3460.10. 1 hit.
InterPro	IPR001344. Chloro_AB-bd_pln. IPR022796. Chloroa_b-bind. IPR023329. Chlorophyll_a/b-bd_dom. [Graphical view]
PANTHER	PTHR21649. PTHR21649. 1 hit.
Pfam	PF00504. Chloroa_b-bind. 1 hit. [Graphical view]
SUPFAM	SSF103511. SSF103511. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CB23_APIGR

Accession

Primary (citable) accession number: P92919

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	May 1, 1997
Last modified:	March 6, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Allergens

Nomenclature of allergens and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents