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P0CJ48

- CB1A_ARATH

UniProt

P0CJ48 - CB1A_ARATH

Protein

Chlorophyll a-b binding protein 2, chloroplastic

Gene

LHCB1.1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 30 (01 Oct 2014)
      Sequence version 1 (11 Jan 2011)
      Previous versions | rss
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    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

    Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi58 – 581Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygenBy similarity
    Binding sitei80 – 801Chlorophyll-a 1; via amide nitrogenBy similarity
    Binding sitei86 – 861Chlorophyll-a 1By similarity
    Metal bindingi99 – 991Magnesium (chlorophyll-a 1 axial ligand)By similarity
    Metal bindingi102 – 1021Magnesium (chlorophyll-a 2 axial ligand)By similarity
    Binding sitei104 – 1041Chlorophyll-b 2By similarity
    Binding sitei137 – 1371Chlorophyll-a 3By similarity
    Binding sitei147 – 1471Chlorophyll-a 3; via amide nitrogenBy similarity
    Metal bindingi153 – 1531Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygenBy similarity
    Binding sitei157 – 1571Chlorophyll-b 3By similarity
    Binding sitei165 – 1651Chlorophyll-b 4 or chlorophyll-b 5By similarity
    Metal bindingi173 – 1731Magnesium (chlorophyll-b 3 axial ligand)By similarity
    Binding sitei176 – 1761Chlorophyll-b 4By similarity
    Binding sitei183 – 1831Chlorophyll-b 2; via amide nitrogenBy similarity
    Binding sitei214 – 2141Chlorophyll-a 5By similarity
    Metal bindingi215 – 2151Magnesium (chlorophyll-a 3 axial ligand)By similarity
    Metal bindingi218 – 2181Magnesium (chlorophyll-a 4 axial ligand)By similarity
    Binding sitei220 – 2201Chlorophyll-a 1By similarity
    Metal bindingi232 – 2321Magnesium (chlorophyll-a 5 axial ligand)By similarity
    Metal bindingi247 – 2471Magnesium (chlorophyll-a 6 axial ligand)By similarity
    Binding sitei256 – 2561Chlorophyll-a 6; via amide nitrogenBy similarity
    Binding sitei263 – 2631Chlorophyll-b 5; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. chlorophyll binding Source: TAIR
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. photosynthesis, light harvesting Source: InterPro
    2. protein-chromophore linkage Source: UniProtKB-KW
    3. response to blue light Source: TAIR
    4. response to far red light Source: TAIR
    5. response to fructose Source: TAIR
    6. response to red light Source: TAIR

    Keywords - Biological processi

    Photosynthesis

    Keywords - Ligandi

    Chlorophyll, Chromophore, Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:LHCB1.1
    Synonyms:AB165, CAB2, LHCP-B
    Ordered Locus Names:At1g29920
    ORF Names:F1N18.4
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G29920.

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. chloroplast Source: TAIR
    3. chloroplast thylakoid membrane Source: TAIR
    4. integral component of membrane Source: UniProtKB-KW
    5. photosystem I Source: UniProtKB-KW
    6. photosystem II Source: UniProtKB-KW
    7. thylakoid Source: TAIR

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi197 – 2004DPLG → AAAA: Loss of interaction with CAO/cpSRP43, but no effect on interaction with LTD. 1 Publication
    Mutagenesisi199 – 1991L → K: Loss of targeting to the thylakoid. 2 Publications
    Mutagenesisi210 – 2123ELK → AAA: Loss of interaction with LTD, but no effect on interaction with CAO/cpSRP43. 1 Publication
    Mutagenesisi220 – 2234RLAM → AAAA: Loss of interaction with LTD, but no effect on interaction with CAO/cpSRP43. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535Chloroplast1 PublicationAdd
    BLAST
    Chaini36 – 267232Chlorophyll a-b binding protein 2, chloroplasticPRO_0000003647Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei36 – 361N2-acetylarginine1 Publication
    Modified residuei38 – 381Phosphothreonine1 Publication

    Post-translational modificationi

    Photoregulated by reversible phosphorylation of its threonine residues.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP0CJ48.

    Interactioni

    Subunit structurei

    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.2 Publications

    Protein-protein interaction databases

    BioGridi25104. 13 interactions.
    25105. 8 interactions.
    IntActiP0CJ48. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP0CJ48.
    SMRiP0CJ48. Positions 48-267.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei100 – 12021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei152 – 17221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei221 – 24121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni221 – 2244Interaction with LTD

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi197 – 2004Required for interaction with CAO/cpSRP43

    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.
    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.

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOGENOMiHOG000238032.
    KOiK08912.
    PhylomeDBiP0CJ48.

    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]
    SUPFAMiSSF103511. SSF103511. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0CJ48-1 [UniParc]FASTAAdd to Basket

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    MAASTMALSS PAFAGKAVNL SPAASEVLGS GRVTMRKTVA KPKGPSGSPW    50
    YGSDRVKYLG PFSGESPSYL TGEFPGDYGW DTAGLSADPE TFARNRELEV 100
    IHSRWAMLGA LGCVFPELLA RNGVKFGEAV WFKAGSQIFS DGGLDYLGNP 150
    SLVHAQSILA IWATQVILMG AVEGYRVAGN GPLGEAEDLL YPGGSFDPLG 200
    LATDPEAFAE LKVKELKNGR LAMFSMFGFF VQAIVTGKGP IENLADHLAD 250
    PVNNNAWAFA TNFVPGK 267
    Length:267
    Mass (Da):28,227
    Last modified:January 11, 2011 - v1
    Checksum:iCEF0664E98F0B0BA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA29280.
    RefSeqiNP_564339.1. NM_102731.2.
    NP_564340.1. NM_102732.2.
    UniGeneiAt.10812.
    At.24351.
    At.27031.
    At.32199.
    At.43708.
    At.49175.
    At.66422.
    At.70617.
    At.71449.
    At.71528.
    At.71547.

    Genome annotation databases

    EnsemblPlantsiAT1G29910.1; AT1G29910.1; AT1G29910.
    AT1G29920.1; AT1G29920.1; AT1G29920.
    GeneIDi839869.
    839870.
    KEGGiath:AT1G29910.
    ath:AT1G29920.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A29280.
    RefSeqi NP_564339.1. NM_102731.2.
    NP_564340.1. NM_102732.2.
    UniGenei At.10812.
    At.24351.
    At.27031.
    At.32199.
    At.43708.
    At.49175.
    At.66422.
    At.70617.
    At.71449.
    At.71528.
    At.71547.

    3D structure databases

    ProteinModelPortali P0CJ48.
    SMRi P0CJ48. Positions 48-267.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 25104. 13 interactions.
    25105. 8 interactions.
    IntActi P0CJ48. 1 interaction.

    Proteomic databases

    PRIDEi P0CJ48.

    Protocols and materials databases

    DNASUi 839869.
    839870.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G29910.1 ; AT1G29910.1 ; AT1G29910 .
    AT1G29920.1 ; AT1G29920.1 ; AT1G29920 .
    GeneIDi 839869.
    839870.
    KEGGi ath:AT1G29910.
    ath:AT1G29920.

    Organism-specific databases

    TAIRi AT1G29920.

    Phylogenomic databases

    HOGENOMi HOG000238032.
    KOi K08912.
    PhylomeDBi P0CJ48.

    Family and domain databases

    Gene3Di 1.10.3460.10. 1 hit.
    InterProi IPR001344. Chloro_AB-bd_pln.
    IPR022796. Chloroa_b-bind.
    IPR023329. Chlorophyll_a/b-bd_dom.
    [Graphical view ]
    PANTHERi PTHR21649. PTHR21649. 1 hit.
    Pfami PF00504. Chloroa_b-bind. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103511. SSF103511. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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.

    Entry informationi

    Entry nameiCB1A_ARATH
    AccessioniPrimary (citable) accession number: P0CJ48
    Secondary accession number(s): P04777, P83754
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2011
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 30 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3