CB29_CHLRE
ID CB29_CHLRE Reviewed; 280 AA.
AC Q93WD2;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Chlorophyll a-b binding protein CP29;
DE AltName: Full=Lhcbm4;
GN Name=Lhcb4 {ECO:0000312|EMBL:BAB64419.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1] {ECO:0000312|EMBL:BAB64419.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=2137 {ECO:0000269|PubMed:11522911}, and
RC IAM C-9 {ECO:0000269|PubMed:11522911};
RX PubMed=11522911; DOI=10.1093/pcp/pce115;
RA Teramoto H., Ono T.-A., Minagawa J.;
RT "Identification of Lhcb gene family encoding the light-harvesting
RT chlorophyll-a/b proteins of photosystem II in Chlamydomonas reinhardtii.";
RL Plant Cell Physiol. 42:849-856(2001).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND REPRESSION BY LIGHT.
RC STRAIN=137c / CC-125 {ECO:0000312|EMBL:AAO16494.1};
RA Durnford D.G., Price J.A., McKim S.M., Sarchfield M.L.;
RT "Light-harvesting complex gene expression is controlled by both
RT transcriptional and post-transcriptional mechanisms during photoacclimation
RT in Chlamydomonas reinhardtii.";
RL Physiol. Plantarum 118:193-205(2003).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-13, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-7,
RP AND ACETYLATION AT VAL-2.
RC STRAIN=cw92 {ECO:0000269|PubMed:15094049};
RX PubMed=15094049; DOI=10.1016/s0014-5793(04)00323-0;
RA Turkina M.V., Villarejo A., Vener A.V.;
RT "The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii
RT is not removed but undergoes acetylation and phosphorylation.";
RL FEBS Lett. 564:104-108(2004).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-13; 15-25; 31-38 AND 72-132, FUNCTION,
RP PHOSPHORYLATION AT THR-7; THR-17; THR-33 AND SER-103, AND ACETYLATION AT
RP VAL-2.
RX PubMed=16156798; DOI=10.1111/j.1742-4658.2005.04894.x;
RA Kargul J., Turkina M.V., Nield J., Benson S., Vener A.V., Barber J.;
RT "Light-harvesting complex II protein CP29 binds to photosystem I of
RT Chlamydomonas reinhardtii under State 2 conditions.";
RL FEBS J. 272:4797-4806(2005).
RN [5] {ECO:0000305}
RP REPRESSION.
RC STRAIN=IAM C-9 {ECO:0000269|PubMed:12226512};
RX PubMed=12226512; DOI=10.1104/pp.004622;
RA Teramoto H., Nakamori A., Minagawa J., Ono T.-A.;
RT "Light-intensity-dependent expression of Lhc gene family encoding light-
RT harvesting chlorophyll-a/b proteins of photosystem II in Chlamydomonas
RT reinhardtii.";
RL Plant Physiol. 130:325-333(2002).
CC -!- FUNCTION: The light-harvesting complex (LHC) functions as a light
CC receptor, it captures and delivers excitation energy to photosystems
CC with which it is closely associated. CP29 facilitates the State 1 to
CC State 2 transition, where State I is induced by excess photosystem I
CC (PSI) light and State 2 is induced by excess photosystem II (PSII)
CC light. {ECO:0000269|PubMed:16156798, ECO:0000305}.
CC -!- COFACTOR:
CC Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and
CC carotenoids such as lutein and neoxanthin.
CC {ECO:0000250|UniProtKB:P12333};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:15094049}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15094049}.
CC -!- INDUCTION: Repressed by high light intensity due to a transient
CC decrease in mRNA stability. Also down-regulated at lower light
CC intensities by low temperature or limited carbon dioxide supply.
CC {ECO:0000269|PubMed:12226512, ECO:0000269|Ref.2}.
CC -!- DOMAIN: The N-terminus of the protein extends into the stroma where it
CC is involved with adhesion of granal membranes and post-translational
CC modifications; both are believed to mediate the distribution of
CC excitation energy between photosystems I and II.
CC -!- PTM: Reversible phosphorylation plays a role in the State transition
CC process and determines the affinity of LHCII for PSI and PSII.
CC {ECO:0000269|PubMed:15094049, ECO:0000269|PubMed:16156798}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000255}.
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DR EMBL; AB051207; BAB64415.1; -; Genomic_DNA.
DR EMBL; AB051211; BAB64419.1; -; mRNA.
DR EMBL; AY171230; AAO16494.1; -; mRNA.
DR RefSeq; XP_001697193.1; XM_001697141.1.
DR PDB; 6KAC; EM; 2.70 A; R/r=1-280.
DR PDB; 6KAD; EM; 3.40 A; R/r=1-280.
DR PDB; 6KAF; EM; 3.73 A; R/r=1-280.
DR PDBsum; 6KAC; -.
DR PDBsum; 6KAD; -.
DR PDBsum; 6KAF; -.
DR AlphaFoldDB; Q93WD2; -.
DR SMR; Q93WD2; -.
DR DIP; DIP-48401N; -.
DR IntAct; Q93WD2; 5.
DR STRING; 3055.EDP00448; -.
DR iPTMnet; Q93WD2; -.
DR ProMEX; Q93WD2; -.
DR EnsemblPlants; PNW70449; PNW70449; CHLRE_17g720250v5.
DR GeneID; 5722671; -.
DR Gramene; PNW70449; PNW70449; CHLRE_17g720250v5.
DR KEGG; cre:CHLRE_17g720250v5; -.
DR eggNOG; ENOG502QRH9; Eukaryota.
DR HOGENOM; CLU_057943_0_0_1; -.
DR OMA; ERPLWYP; -.
DR OrthoDB; 1059323at2759; -.
DR BioCyc; MetaCyc:CHLREDRAFT_184810-MON; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0009503; C:thylakoid light-harvesting complex; IDA:UniProtKB.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009765; P:photosynthesis, light harvesting; IEA:InterPro.
DR InterPro; IPR001344; Chloro_AB-bd_pln.
DR InterPro; IPR022796; Chloroa_b-bind.
DR PANTHER; PTHR21649; PTHR21649; 1.
DR Pfam; PF00504; Chloroa_b-bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chlorophyll; Chloroplast; Chromophore;
KW Direct protein sequencing; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Photosynthesis; Photosystem I; Photosystem II; Plastid;
KW Thylakoid; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15094049,
FT ECO:0000269|PubMed:16156798"
FT CHAIN 2..280
FT /note="Chlorophyll a-b binding protein CP29"
FT /evidence="ECO:0000269|PubMed:15094049"
FT /id="PRO_0000165470"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 79
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 137
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 140
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 183
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 199
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 202
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 238
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 241
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="4"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 243
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 255
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000269|PubMed:15094049,
FT ECO:0000269|PubMed:16156798"
FT MOD_RES 7
FT /note="Phosphothreonine; in State 1 and State 2"
FT /evidence="ECO:0000269|PubMed:15094049,
FT ECO:0000269|PubMed:16156798"
FT MOD_RES 17
FT /note="Phosphothreonine; in State 2"
FT /evidence="ECO:0000269|PubMed:16156798"
FT MOD_RES 33
FT /note="Phosphothreonine; in State 1 and State 2"
FT /evidence="ECO:0000269|PubMed:16156798"
FT MOD_RES 103
FT /note="Phosphoserine; in State 2"
FT /evidence="ECO:0000269|PubMed:16156798"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 130..156
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 162..166
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 184..202
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 238..256
FT /evidence="ECO:0007829|PDB:6KAC"
SQ SEQUENCE 280 AA; 29938 MW; 2FCDFAF307B2E49A CRC64;
MVFKFPTPPG TQKKAGTTAT KPAPKATTKK VATSTGTRSG GVGYRKYQGD ALWLPNTTRP
EWLDGSLPGD RGFDPLGLSK PSEFVVIGVD ENDQNAAKNN KGSVEAIVQA TPDEVSSENR
LAPYSEVFGL ARFRECELIH GRWAMLACLG ALVAEATTGV SWVEAGKVEL DGASYAGLSL
PFSITQLIWI EVILVGGAEF YRNSETNPEK RCYPGGVFDP LKLASEDEER AFRLKTAEIK
HARLAMVSFF GYGVQALSTG EGALGSLAKF ADGLNNGKGL
