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P0CJ48 (CB1A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chlorophyll a-b binding protein 2, chloroplastic
Alternative name(s):
Chlorophyll a-b protein 165
Short name=CAB-165
LHCII type I CAB-2
Gene names
Name:LHCB1.1
Synonyms:AB165, CAB2, LHCP-B
Ordered Locus Names:At1g29920
ORF Names:F1N18.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Interacts (via T14 domain) with LTD. Interacts with CAO/cpSRP43 during its post-translational targeting to the thylakoid. Ref.7 Ref.9

Subcellular location

Plastidchloroplast 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.

The L18 domain (188-205) is required for the transit complex formation with CAO/cpSRP43 and the targeting to the thylakoid.

The T14 domain (211-224) is required for the interaction with LTD and the translocation across the envelope.

Post-translational modification

Photoregulated by reversible phosphorylation of its threonine residues By similarity.

Sequence similarities

Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.

Ontologies

Keywords
   Biological processPhotosynthesis
   Cellular componentChloroplast
Membrane
Photosystem I
Photosystem II
Plastid
Thylakoid
   DomainTransit peptide
Transmembrane
Transmembrane helix
   LigandChlorophyll
Chromophore
Magnesium
Metal-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processphotosynthesis, light harvesting

Inferred from electronic annotation. Source: InterPro

protein-chromophore linkage

Inferred from electronic annotation. Source: UniProtKB-KW

response to blue light

Inferred from expression pattern PubMed 18820083. Source: TAIR

response to far red light

Inferred from expression pattern PubMed 18820083. Source: TAIR

response to fructose

Inferred from expression pattern PubMed 21253566. Source: TAIR

response to red light

Inferred from expression pattern PubMed 18820083. Source: TAIR

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209. Source: TAIR

chloroplast thylakoid membrane

Inferred from direct assay PubMed 14729914PubMed 15322131. Source: TAIR

integral component of 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

thylakoid

Inferred from direct assay PubMed 18633119. Source: TAIR

   Molecular_functionchlorophyll binding

Traceable author statement PubMed 2204948. Source: TAIR

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Chloroplast Ref.6
Chain36 – 267232Chlorophyll a-b binding protein 2, chloroplastic
PRO_0000003647

Regions

Transmembrane100 – 12021Helical; Potential
Transmembrane152 – 17221Helical; Potential
Transmembrane221 – 24121Helical; Potential
Region221 – 2244Interaction with LTD
Motif197 – 2004Required for interaction with CAO/cpSRP43

Sites

Metal binding581Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygen By similarity
Metal binding991Magnesium (chlorophyll-a 1 axial ligand) By similarity
Metal binding1021Magnesium (chlorophyll-a 2 axial ligand) By similarity
Metal binding1531Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygen By similarity
Metal binding1731Magnesium (chlorophyll-b 3 axial ligand) By similarity
Metal binding2151Magnesium (chlorophyll-a 3 axial ligand) By similarity
Metal binding2181Magnesium (chlorophyll-a 4 axial ligand) By similarity
Metal binding2321Magnesium (chlorophyll-a 5 axial ligand) By similarity
Metal binding2471Magnesium (chlorophyll-a 6 axial ligand) By similarity
Binding site801Chlorophyll-a 1; via amide nitrogen By similarity
Binding site861Chlorophyll-a 1 By similarity
Binding site1041Chlorophyll-b 2 By similarity
Binding site1371Chlorophyll-a 3 By similarity
Binding site1471Chlorophyll-a 3; via amide nitrogen By similarity
Binding site1571Chlorophyll-b 3 By similarity
Binding site1651Chlorophyll-b 4 or chlorophyll-b 5 By similarity
Binding site1761Chlorophyll-b 4 By similarity
Binding site1831Chlorophyll-b 2; via amide nitrogen By similarity
Binding site2141Chlorophyll-a 5 By similarity
Binding site2201Chlorophyll-a 1 By similarity
Binding site2561Chlorophyll-a 6; via amide nitrogen By similarity
Binding site2631Chlorophyll-b 5; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue361N2-acetylarginine
Modified residue381Phosphothreonine Ref.6

Experimental info

Mutagenesis197 – 2004DPLG → AAAA: Loss of interaction with CAO/cpSRP43, but no effect on interaction with LTD.
Mutagenesis1991L → K: Loss of targeting to the thylakoid. Ref.7
Mutagenesis210 – 2123ELK → AAA: Loss of interaction with LTD, but no effect on interaction with CAO/cpSRP43. Ref.9
Mutagenesis220 – 2234RLAM → AAAA: Loss of interaction with LTD, but no effect on interaction with CAO/cpSRP43. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P0CJ48 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: CEF0664E98F0B0BA

FASTA26728,227
        10         20         30         40         50         60 
MAASTMALSS PAFAGKAVNL SPAASEVLGS GRVTMRKTVA KPKGPSGSPW YGSDRVKYLG 

        70         80         90        100        110        120 
PFSGESPSYL TGEFPGDYGW DTAGLSADPE TFARNRELEV IHSRWAMLGA LGCVFPELLA 

       130        140        150        160        170        180 
RNGVKFGEAV WFKAGSQIFS DGGLDYLGNP SLVHAQSILA IWATQVILMG AVEGYRVAGN 

       190        200        210        220        230        240 
GPLGEAEDLL YPGGSFDPLG LATDPEAFAE LKVKELKNGR LAMFSMFGFF VQAIVTGKGP 

       250        260 
IENLADHLAD PVNNNAWAFA TNFVPGK 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of three light-harvesting chlorophyll a/b-binding protein genes in Arabidopsis thaliana."
Leutwiler L.S., Meyerowitz E.M., Tobin E.M.
Nucleic Acids Res. 14:4051-4064(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana."
Vener A.V., Harms A., Sussman M.R., Vierstra R.D.
J. Biol. Chem. 276:6959-6966(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-43, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-38, ACETYLATION AT ARG-36.
Strain: cv. Columbia.
[7]"Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43."
Stengel K.F., Holdermann I., Cain P., Robinson C., Wild K., Sinning I.
Science 321:253-256(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CAO/CPSRP43, MUTAGENESIS OF LEU-199.
[8]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"LTD is a protein required for sorting light-harvesting chlorophyll-binding proteins to the chloroplast SRP pathway."
Ouyang M., Li X., Ma J., Chi W., Xiao J., Zou M., Chen F., Lu C., Zhang L.
Nat. Commun. 2:277-277(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LTD, MUTAGENESIS OF 197-ASP--GLY-200; 210-GLU--LYS-212 AND 220-ARG--MET-223.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03907 Genomic DNA. Translation: CAA27540.1.
AC008030 Genomic DNA. Translation: AAG10604.1.
CP002684 Genomic DNA. Translation: AEE31150.1.
AY052237 mRNA. Translation: AAK97707.1.
AY054198 mRNA. Translation: AAL06859.1.
AY060500 mRNA. Translation: AAL31113.1.
AY062814 mRNA. Translation: AAL32892.1.
AY081572 mRNA. Translation: AAM10134.1.
AY128345 mRNA. Translation: AAM91548.1.
BT000726 mRNA. Translation: AAN31868.1.
AY086905 mRNA. Translation: AAM63949.1.
PIRA29280.
RefSeqNP_564339.1. NM_102731.2.
NP_564340.1. NM_102732.2.
UniGeneAt.10812.
At.24351.
At.27031.
At.32199.
At.43708.
At.49175.
At.66422.
At.70617.
At.71449.
At.71528.
At.71547.

3D structure databases

ProteinModelPortalP0CJ48.
SMRP0CJ48. Positions 48-267.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid25104. 13 interactions.
25105. 8 interactions.
IntActP0CJ48. 1 interaction.

Proteomic databases

PRIDEP0CJ48.

Protocols and materials databases

DNASU839869.
839870.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G29910.1; AT1G29910.1; AT1G29910.
AT1G29920.1; AT1G29920.1; AT1G29920.
GeneID839869.
839870.
KEGGath:AT1G29910.
ath:AT1G29920.

Organism-specific databases

TAIRAT1G29920.

Phylogenomic databases

HOGENOMHOG000238032.
KOK08912.
PhylomeDBP0CJ48.

Family and domain databases

Gene3D1.10.3460.10. 1 hit.
InterProIPR001344. Chloro_AB-bd_pln.
IPR022796. Chloroa_b-bind.
IPR023329. Chlorophyll_a/b-bd_dom.
[Graphical view]
PANTHERPTHR21649. PTHR21649. 1 hit.
PfamPF00504. Chloroa_b-bind. 1 hit.
[Graphical view]
SUPFAMSSF103511. SSF103511. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCB1A_ARATH
AccessionPrimary (citable) accession number: P0CJ48
Secondary accession number(s): P04777, P83754
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names