Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chlorophyll a-b binding protein CP29

Gene

Lhcb4

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
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. CP29 facilitates the State 1 to State 2 transition, where State I is induced by excess photosystem I (PSI) light and State 2 is induced by excess photosystem II (PSII) light.Curated1 Publication

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
Metal bindingi47Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygenBy similarity1
Binding sitei73Chlorophyll-a 1; via amide nitrogenBy similarity1
Binding sitei79Chlorophyll-a 1By similarity1
Metal bindingi137Magnesium (chlorophyll-a 1 axial ligand)By similarity1
Metal bindingi140Magnesium (chlorophyll-a 2 axial ligand)By similarity1
Binding sitei183Chlorophyll-b 3By similarity1
Metal bindingi199Magnesium (chlorophyll-b 3 axial ligand)By similarity1
Binding sitei202Chlorophyll-b 4By similarity1
Metal bindingi238Magnesium (chlorophyll-a 3 axial ligand)By similarity1
Metal bindingi241Magnesium (chlorophyll-a 4 axial ligand)By similarity1
Binding sitei243Chlorophyll-a 1By similarity1
Metal bindingi255Magnesium (chlorophyll-a 5 axial ligand)By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processPhotosynthesis
LigandChlorophyll, Chromophore, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:CHLREDRAFT_184810-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Chlorophyll a-b binding protein CP29
Alternative name(s):
Lhcbm4
Gene namesi
Name:Lhcb4Imported
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

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
Transmembranei143 – 163HelicalSequence analysisAdd BLAST21
Transmembranei176 – 196HelicalSequence analysisAdd BLAST21
Transmembranei244 – 264HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001654702 – 280Chlorophyll a-b binding protein CP291 PublicationAdd BLAST279

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylvaline2 Publications1
Modified residuei7Phosphothreonine; in State 1 and State 22 Publications1
Modified residuei17Phosphothreonine; in State 21 Publication1
Modified residuei33Phosphothreonine; in State 1 and State 21 Publication1
Modified residuei103Phosphoserine; in State 21 Publication1

Post-translational modificationi

Reversible phosphorylation plays a role in the State transition process and determines the affinity of LHCII for PSI and PSII.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ93WD2
ProMEXiQ93WD2

PTM databases

iPTMnetiQ93WD2

Expressioni

Inductioni

Repressed by high light intensity due to a transient decrease in mRNA stability. Also down-regulated at lower light intensities by low temperature or limited carbon dioxide supply.2 Publications

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-48401N
IntActiQ93WD2, 5 interactors

Structurei

3D structure databases

ProteinModelPortaliQ93WD2
SMRiQ93WD2
ModBaseiSearch...
MobiDBiSearch...

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

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEXD Eukaryota
ENOG410YYUX LUCA
KOiK08915
OMAiIWIEVIL

Family and domain databases

Gene3Di1.10.3460.10, 2 hits
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.

Q93WD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFKFPTPPG TQKKAGTTAT KPAPKATTKK VATSTGTRSG GVGYRKYQGD
60 70 80 90 100
ALWLPNTTRP EWLDGSLPGD RGFDPLGLSK PSEFVVIGVD ENDQNAAKNN
110 120 130 140 150
KGSVEAIVQA TPDEVSSENR LAPYSEVFGL ARFRECELIH GRWAMLACLG
160 170 180 190 200
ALVAEATTGV SWVEAGKVEL DGASYAGLSL PFSITQLIWI EVILVGGAEF
210 220 230 240 250
YRNSETNPEK RCYPGGVFDP LKLASEDEER AFRLKTAEIK HARLAMVSFF
260 270 280
GYGVQALSTG EGALGSLAKF ADGLNNGKGL
Length:280
Mass (Da):29,938
Last modified:January 23, 2007 - v3
Checksum:i2FCDFAF307B2E49A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051207 Genomic DNA Translation: BAB64415.1
AB051211 mRNA Translation: BAB64419.1
AY171230 mRNA Translation: AAO16494.1
RefSeqiXP_001697193.1, XM_001697141.1
UniGeneiCre.4370

Genome annotation databases

EnsemblPlantsiEDP00448; EDP00448; CHLREDRAFT_184810
GeneIDi5722671
GrameneiEDP00448; EDP00448; CHLREDRAFT_184810
KEGGicre:CHLREDRAFT_184810

Similar proteinsi

Entry informationi

Entry nameiCB29_CHLRE
AccessioniPrimary (citable) accession number: Q93WD2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 99 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health