CB24_PEA
ID CB24_PEA Reviewed; 252 AA.
AC Q9SQL2; A3F6K3; P35386;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Chlorophyll a-b binding protein P4, chloroplastic;
DE AltName: Full=LHCI type III CAB-P4;
DE Flags: Precursor;
GN Name=lhcA-P4 {ECO:0000312|EMBL:AAF13731.1};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF13731.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Greenfeast {ECO:0000269|PubMed:10542315};
RC TISSUE=Leaf {ECO:0000312|EMBL:AAF13731.1};
RX PubMed=10542315; DOI=10.1016/s0167-4781(99)00154-2;
RA Brosche M., Fant C., Bergkvist S.W., Strid H., Svensk A., Olsson O.,
RA Strid A.;
RT "Molecular markers for UV-B stress in plants: alteration of the expression
RT of four classes of genes in Pisum sativum and the formation of high
RT molecular mass RNA adducts.";
RL Biochim. Biophys. Acta 1447:185-198(1999).
RN [2] {ECO:0000312|EMBL:ABN49455.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-252.
RA Gupta S., Tuteja N.;
RT "Interacting partner of calcineurin B-like interacting protein kinase
RT (CIPK) (partial homolog of photosystem I light harvesting chlorophyll a/b
RT binding protein) from Pisum sativum.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 110-124, AND FUNCTION.
RC TISSUE=Seedling {ECO:0000269|PubMed:2174365};
RX PubMed=2174365; DOI=10.1111/j.1432-1033.1990.tb19393.x;
RA Jahns P., Junge W.;
RT "Dicyclohexylcarbodiimide-binding proteins related to the short circuit of
RT the proton-pumping activity of photosystem II. Identified as light-
RT harvesting chlorophyll-a/b-binding proteins.";
RL Eur. J. Biochem. 193:731-736(1990).
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. {ECO:0000269|PubMed:2174365,
CC ECO:0000305}.
CC -!- FUNCTION: May channel protons produced in the catalytic Mn center of
CC water oxidation into the thylakoid lumen. {ECO:0000269|PubMed:2174365}.
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:P07371};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- INDUCTION: Down-regulated by UV-B. {ECO:0000269|PubMed:10542315}.
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. {ECO:0000305}.
CC -!- PTM: Photoregulated by reversible phosphorylation of its threonine
CC residues. {ECO:0000250|UniProtKB:P07371}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF002248; AAF13731.1; -; mRNA.
DR EMBL; EF208907; ABN49455.1; -; mRNA.
DR PIR; T51616; T51616.
DR PDB; 2O01; X-ray; 3.40 A; 4=85-249.
DR PDB; 2WSC; X-ray; 3.30 A; 4=1-252.
DR PDB; 2WSE; X-ray; 3.49 A; 4=1-252.
DR PDB; 2WSF; X-ray; 3.48 A; 4=1-252.
DR PDB; 3LW5; X-ray; 3.30 A; 4=81-247.
DR PDB; 4RKU; X-ray; 3.00 A; 4=53-248.
DR PDB; 4XK8; X-ray; 2.80 A; 4/9=54-249.
DR PDB; 4Y28; X-ray; 2.80 A; 4=1-252.
DR PDB; 5L8R; X-ray; 2.60 A; 4=52-249.
DR PDB; 6YAC; EM; 2.50 A; 4=52-249.
DR PDB; 6YEZ; EM; 2.70 A; 4=52-249.
DR PDB; 6ZOO; EM; 2.74 A; 4=52-249.
DR PDB; 6ZXS; X-ray; 3.00 A; 4=52-249.
DR PDB; 7DKZ; X-ray; 2.39 A; 4=52-249.
DR PDBsum; 2O01; -.
DR PDBsum; 2WSC; -.
DR PDBsum; 2WSE; -.
DR PDBsum; 2WSF; -.
DR PDBsum; 3LW5; -.
DR PDBsum; 4RKU; -.
DR PDBsum; 4XK8; -.
DR PDBsum; 4Y28; -.
DR PDBsum; 5L8R; -.
DR PDBsum; 6YAC; -.
DR PDBsum; 6YEZ; -.
DR PDBsum; 6ZOO; -.
DR PDBsum; 6ZXS; -.
DR PDBsum; 7DKZ; -.
DR AlphaFoldDB; Q9SQL2; -.
DR SMR; Q9SQL2; -.
DR DIP; DIP-60296N; -.
DR IntAct; Q9SQL2; 3.
DR PRIDE; Q9SQL2; -.
DR EvolutionaryTrace; Q9SQL2; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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; Chlorophyll; Chloroplast; Chromophore;
KW Direct protein sequencing; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Photosynthesis; Photosystem I; Photosystem II; Plastid;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN ?..252
FT /note="Chlorophyll a-b binding protein P4, chloroplastic"
FT /id="PRO_0000310860"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 56
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 76
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27521"
FT BINDING 95
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:P07371"
FT BINDING 100
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 137
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P27521"
FT BINDING 143
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 153
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:P27521"
FT BINDING 156
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P27521"
FT BINDING 203
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 204
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:P07371"
FT BINDING 207
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:P07371"
FT BINDING 209
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 221
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:P07371"
FT BINDING 236
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT CONFLICT 128
FT /note="A -> D (in Ref. 2; ABN49455)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="S -> F (in Ref. 2; ABN49455)"
FT /evidence="ECO:0000305"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:5L8R"
FT HELIX 85..117
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 126..131
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4XK8"
FT HELIX 138..161
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2WSC"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2WSC"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4RKU"
FT HELIX 198..225
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:7DKZ"
SQ SEQUENCE 252 AA; 27229 MW; 00B7D26C82F6667A CRC64;
MATVTTQASA AIFGPCGLKS RFLGGSSGKL NRGVAFRPVG CSPSASFKVE AKKGEWLPGL
ASPGYLTGSL PGDNGFDPLG LAEDPENLRW FVQAELVNGR WAMLGVAGML LPEVFTSIGI
INVPKWYAAG KEEYFASSST LFVIEFILSH YVEIRRWQDI KNPGSVNQDP IFKQYSLPAG
EVGYPGGIFN PLNFAPTLEA KEKEIANGRL AMLAFLGFII QHNVTGKGPF DNLLQHISDP
WHNTIVQTLG GN
