CB23_PEA
ID CB23_PEA Reviewed; 275 AA.
AC Q32904; P35388;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Chlorophyll a-b binding protein 3, chloroplastic;
DE AltName: Full=LHCII type III CAB-3;
DE Flags: Precursor;
GN Name=lhca3 {ECO:0000312|EMBL:AAA84545.1};
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:0000312|EMBL:AAA84545.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Little Marvel {ECO:0000312|EMBL:AAA84545.1};
RC TISSUE=Seedling {ECO:0000269|PubMed:8290641};
RX PubMed=8290641; DOI=10.1104/pp.103.4.1461;
RA Morishige D.T., Anandan S., Dreyfuss B.W., Williams R.S., Ellis R.J.,
RA Thornber J.P.;
RT "A pea cDNA clone (Ihca3) encoding the 24-kilodalton light-harvesting
RT protein of photosystem I.";
RL Plant Physiol. 103:1461-1462(1993).
RN [2] {ECO:0000305, ECO:0000312|PIR:S13975}
RP PROTEIN SEQUENCE OF 236-258, 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}; Single-pass membrane protein {ECO:0000255, ECO:0000305}.
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}.
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DR EMBL; L19651; AAA84545.1; -; mRNA.
DR PIR; S13975; S13975.
DR PIR; T06411; T06411.
DR PDB; 3LW5; X-ray; 3.30 A; 3=84-255.
DR PDB; 4RKU; X-ray; 3.00 A; 3=1-275.
DR PDB; 4XK8; X-ray; 2.80 A; 3/8=55-272.
DR PDB; 4Y28; X-ray; 2.80 A; 3=1-275.
DR PDB; 5L8R; X-ray; 2.60 A; 3=1-275.
DR PDB; 6YAC; EM; 2.50 A; 3=55-275.
DR PDB; 6YEZ; EM; 2.70 A; 3=55-275.
DR PDB; 6ZOO; EM; 2.74 A; 3=55-275.
DR PDB; 6ZXS; X-ray; 3.00 A; 3=55-275.
DR PDB; 7DKZ; X-ray; 2.39 A; 3=1-275.
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; Q32904; -.
DR SMR; Q32904; -.
DR DIP; DIP-60295N; -.
DR IntAct; Q32904; 20.
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 ?..275
FT /note="Chlorophyll a-b binding protein 3, chloroplastic"
FT /id="PRO_0000310859"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 58
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 78
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27522"
FT BINDING 84
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 102
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 107
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 142
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 169
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:P27522"
FT BINDING 172
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P27522"
FT BINDING 226
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 227
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 230
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 232
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 244
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 259
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 STRAND 58..60
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 62..67
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6YEZ"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:5L8R"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6YEZ"
FT HELIX 95..115
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3LW5"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 154..177
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4Y28"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6YAC"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5L8R"
FT HELIX 217..248
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:7DKZ"
SQ SEQUENCE 275 AA; 29607 MW; 49AB86D1CE247A31 CRC64;
MATQALVSSS SLTFAAEAVR QSFRARSLPS SVGCSRKGLV RAAATPPVKQ GGVDRPLWFA
SKQSLSYLDG SLPGDYGFDP LGLSDPEGTG GFIEPRWLAY GEVINGRFAM LGAVGAIAPE
YLGKVGLIPQ ETALAWFQTG VIPPAGTYNY WADNYTLFVL EMALMGFAEH RRFQDWAKPG
SMGKQYFLGL EKGFGGSGNP AYPGGPFFNP LGFGKDEKSL KELKLKEVKN GRLAMLAILG
YFIQGLVTGV GPYQNLLDHV ADPVNNNVLT SLKFH
