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Entry version 105 (29 Sep 2021)
Sequence version 1 (01 Aug 1992)
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Protein

Chlorophyll a-b binding protein of LHCII type III, chloroplastic

Gene

LHBC

Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Note: 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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi58Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei80Chlorophyll-a 1; via amide nitrogenBy similarity1
Binding sitei86Chlorophyll-a 1By similarity1
Metal bindingi99Magnesium (chlorophyll-a 1 axial ligand)By similarity1
Metal bindingi102Magnesium (chlorophyll-a 2 axial ligand)By similarity1
Binding sitei104Chlorophyll-b 2By similarity1
Binding sitei138Chlorophyll-a 3By similarity1
Binding sitei148Chlorophyll-a 3; via amide nitrogenBy similarity1
Metal bindingi154Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygenBy similarity1
Binding sitei158Chlorophyll-b 3By similarity1
Binding sitei166Chlorophyll-b 4By similarity1
Binding sitei166Chlorophyll-b 5By similarity1
Metal bindingi174Magnesium (chlorophyll-b 3 axial ligand)By similarity1
Binding sitei177Chlorophyll-b 4By similarity1
Binding sitei215Chlorophyll-a 5By similarity1
Metal bindingi216Magnesium (chlorophyll-a 3 axial ligand)By similarity1
Metal bindingi219Magnesium (chlorophyll-a 4 axial ligand)By similarity1
Binding sitei221Chlorophyll-a 1By similarity1
Metal bindingi233Magnesium (chlorophyll-a 5 axial ligand)By similarity1
Metal bindingi248Magnesium (chlorophyll-a 6 axial ligand)By similarity1
Binding sitei257Chlorophyll-a 6; via amide nitrogenBy similarity1
Binding sitei264Chlorophyll-b 5; via carbonyl oxygenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processPhotosynthesis
LigandChlorophyll, Chromophore, Magnesium, Metal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Chlorophyll a-b binding protein of LHCII type III, chloroplastic
Short name:
CAB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LHBC
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHordeum vulgare (Barley)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri4513 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Transmembranei153 – 173HelicalSequence analysisAdd BLAST21
Transmembranei222 – 242HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 45ChloroplastSequence analysisAdd BLAST45
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000370846 – 268Chlorophyll a-b binding protein of LHCII type III, chloroplasticAdd BLAST223

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Photoregulated by reversible phosphorylation of its threonine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P27523

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P27523, baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P27523

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.3460.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001344, Chloro_AB-bd_pln
IPR022796, Chloroa_b-bind
IPR023329, Chlorophyll_a/b-bd_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR21649, PTHR21649, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00504, Chloroa_b-bind, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P27523-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASTIMAAAS RAVVAKTPFL SGQGRAASAS PLRDIAAATN GRITMGNDLW
60 70 80 90 100
YGPDRVKYLG PFSAQTPSYL NGEFPGDYGW DTAGLSADPE AFARNRALEV
110 120 130 140 150
IHGRWAMLGA LGCVFPEVLQ KWVGVEFKEP VWFKAGSQIF SEGGLDYLGN
160 170 180 190 200
PNLVHAQSIL AVLGFQVLLM GLVEGFRING LDGVGEGNDL YPGGQYFDPL
210 220 230 240 250
GLADDPVTFA ELKVKEIKNG RLAMFSMFGF FVQAIVTGKG PLENLFDHLD
260
DPVANNAWVF ATKFAPGS
Length:268
Mass (Da):28,759
Last modified:August 1, 1992 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5E48C106FC5BCAFD
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X63197 mRNA Translation: CAA44881.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S22482, CDBH3

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
HORVU.MOREX.r2.2HG0111260.1; HORVU.MOREX.r2.2HG0111260.1; HORVU.MOREX.r2.2HG0111260
HORVU.MOREX.r2.2HG0111260.1.mrna1; HORVU.MOREX.r2.2HG0111260.1.mrna1; HORVU.MOREX.r2.2HG0111260.1

Gramene; a comparative resource for plants

More...
Gramenei
HORVU.MOREX.r2.2HG0111260.1; HORVU.MOREX.r2.2HG0111260.1; HORVU.MOREX.r2.2HG0111260
HORVU.MOREX.r2.2HG0111260.1.mrna1; HORVU.MOREX.r2.2HG0111260.1.mrna1; HORVU.MOREX.r2.2HG0111260.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63197 mRNA Translation: CAA44881.1
PIRiS22482, CDBH3

3D structure databases

SMRiP27523
ModBaseiSearch...

Proteomic databases

PRIDEiP27523

Genome annotation databases

EnsemblPlantsiHORVU.MOREX.r2.2HG0111260.1; HORVU.MOREX.r2.2HG0111260.1; HORVU.MOREX.r2.2HG0111260
HORVU.MOREX.r2.2HG0111260.1.mrna1; HORVU.MOREX.r2.2HG0111260.1.mrna1; HORVU.MOREX.r2.2HG0111260.1
GrameneiHORVU.MOREX.r2.2HG0111260.1; HORVU.MOREX.r2.2HG0111260.1; HORVU.MOREX.r2.2HG0111260
HORVU.MOREX.r2.2HG0111260.1.mrna1; HORVU.MOREX.r2.2HG0111260.1.mrna1; HORVU.MOREX.r2.2HG0111260.1

Gene expression databases

ExpressionAtlasiP27523, baseline and differential

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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCB23_HORVU
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P27523
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 29, 2021
This is version 105 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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