CB22_PEA
ID CB22_PEA Reviewed; 269 AA.
AC P07371; P35389; Q53X02;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Chlorophyll a-b binding protein AB80, chloroplastic;
DE AltName: Full=LHCII type I CAB-AB80;
DE Short=LHCP;
DE Flags: Precursor;
GN Name=AB80;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Progress No. 9;
RX PubMed=16593461; DOI=10.1073/pnas.81.10.2960;
RA Cashmore A.R.;
RT "Structure and expression of a pea nuclear gene encoding a chlorophyll a/b-
RT binding polypeptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2960-2964(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Timko M.P., Kausch A.P., Hand J.M., Cashmore A.R., Herrera-Estrella L.,
RA Van den Broeck G., Van Montagu M.M.;
RT "Structure and expression of nuclear genes encoding polypeptides of the
RT photosynthetic apparatus.";
RL (In) Steinbeck K.E., Bonitz S.G., Arntzen C.J., Bogorad L. (eds.);
RL Molecular biology of the photosynthetic apparatus, pp.381-396, Cold Spring
RL Harbor Laboratory, Cold Spring Harbor (1985).
RN [3]
RP PROTEIN SEQUENCE OF 111-126, AND FUNCTION.
RC TISSUE=Seedling;
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).
RN [4]
RP CHLOROPHYLL BINDING, AND MUTAGENESIS OF GLU-102; HIS-105; GLN-168; GLN-234
RP AND HIS-249.
RX PubMed=10587443; DOI=10.1021/bi990738x;
RA Yang C., Kosemund K., Cornet C., Paulsen H.;
RT "Exchange of pigment-binding amino acids in light-harvesting chlorophyll
RT a/b protein.";
RL Biochemistry 38:16205-16213(1999).
RN [5]
RP CHLOROPHYLL BINDING, AND MUTAGENESIS OF GLU-102; HIS-105; 114-LEU-GLY-115;
RP GLN-168; GLU-176; GLU-217; ASN-220; GLN-234 AND HIS-249.
RX PubMed=10587444; DOI=10.1021/bi990739p;
RA Rogl H., Kuehlbrandt W.;
RT "Mutant trimers of light-harvesting complex II exhibit altered pigment
RT content and spectroscopic features.";
RL Biochemistry 38:16214-16222(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
RX PubMed=8107845; DOI=10.1038/367614a0;
RA Kuehlbrandt W., Wang D.N., Fujiyoshi Y.;
RT "Atomic model of plant light-harvesting complex by electron
RT crystallography.";
RL Nature 367:614-621(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (9.5 ANGSTROMS) OF 38-269 IN COMPLEX WITH CHLOROPHYLL
RP A-B AND CAROTENOIDS, AND COFACTOR.
RX PubMed=15103124; DOI=10.1107/s0907444904003233;
RA Hino T., Kanamori E., Shen J.-R., Kouyama T.;
RT "An icosahedral assembly of the light-harvesting chlorophyll a/b protein
RT complex from pea chloroplast thylakoid membranes.";
RL Acta Crystallogr. D 60:803-809(2004).
RN [8] {ECO:0007744|PDB:2BHW}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 38-269 IN COMPLEX WITH
RP CHLOROPHYLL A AND CHLOROPHYLL B.
RX PubMed=15719016; DOI=10.1038/sj.emboj.7600585;
RA Standfuss J., Terwisscha van Scheltinga A.C., Lamborghini M.,
RA Kuhlbrandt W.;
RT "Mechanisms of photoprotection and nonphotochemical quenching in pea light-
RT harvesting complex at 2.5 A resolution.";
RL EMBO J. 24:919-928(2005).
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 -!- 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:0000305|PubMed:15719016};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
CC {ECO:0000269|PubMed:15103124}.
CC -!- INTERACTION:
CC P07371; O22265: CAO; Xeno; NbExp=7; IntAct=EBI-2353186, EBI-780656;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC pass membrane protein.
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: Photoregulated by reversible phosphorylation of its threonine
CC residues.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; K02067; AAA33651.1; -; Genomic_DNA.
DR EMBL; M64619; AAA63413.1; -; Genomic_DNA.
DR PIR; A26780; CDPM80.
DR PDB; 1VCR; X-ray; 9.50 A; A=38-269.
DR PDB; 2BHW; X-ray; 2.50 A; A/B/C=38-269.
DR PDBsum; 1VCR; -.
DR PDBsum; 2BHW; -.
DR AlphaFoldDB; P07371; -.
DR SMR; P07371; -.
DR DIP; DIP-40897N; -.
DR IntAct; P07371; 3.
DR PRIDE; P07371; -.
DR EvolutionaryTrace; P07371; -.
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; Acetylation; 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..37
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 38..269
FT /note="Chlorophyll a-b binding protein AB80, chloroplastic"
FT /id="PRO_0000003680"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 61
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:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 83
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 89
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
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:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 105
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:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 107
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 140
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 150
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 156
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:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 160
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 168
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 168
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 176
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:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 179
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 185
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 216
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 217
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:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 220
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:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 222
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 234
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:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 249
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:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 258
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT BINDING 265
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:15719016,
FT ECO:0007744|PDB:2BHW"
FT MOD_RES 38
FT /note="N2-acetylarginine"
FT /evidence="ECO:0000250"
FT MUTAGEN 102
FT /note="E->A: Decreases binding to chlorophyll-b."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 102
FT /note="E->Q: Causes a strong decrease in LHCII complex
FT stability; when associated with L-105."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 105
FT /note="H->A: Decreases binding to chlorophyll-a."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 105
FT /note="H->F: Decreases binding to chlorophyll, more
FT chlorophyll-a than chlorophyll-b is lost. Causes a strong
FT decrease in LHCII complex stability."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 105
FT /note="H->L: Decreases binding to chlorophyll, more
FT chlorophyll-a than chlorophyll-b is lost. Causes a strong
FT decrease in LHCII complex stability. Complex stability is
FT reduced further; when associated with Q-102."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 114..115
FT /note="LG->VF: Decreases binding to chlorophyll-b."
FT /evidence="ECO:0000269|PubMed:10587444"
FT MUTAGEN 168
FT /note="Q->A: Decreases binding to chlorophyll-b."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 168
FT /note="Q->E,S: Decreases binding to chlorophyll, more
FT chlorophyll-b than chlorophyll-a is lost. Causes a strong
FT decrease in LHCII complex stability."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 176
FT /note="E->A: Decreases binding to chlorophyll-b."
FT /evidence="ECO:0000269|PubMed:10587444"
FT MUTAGEN 217
FT /note="E->A: Decreases binding to chlorophyll-a."
FT /evidence="ECO:0000269|PubMed:10587444"
FT MUTAGEN 220
FT /note="N->A: Decreases binding to chlorophyll-a and
FT possibly chlorophyll-b."
FT /evidence="ECO:0000269|PubMed:10587444"
FT MUTAGEN 234
FT /note="Q->E,S: Decreases binding to chlorophyll. Causes a
FT moderate decrease in LHCII complex stability."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 234
FT /note="Q->L: Decreases binding to chlorophyll-a."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 249
FT /note="H->A: Decreases binding to chlorophyll-a."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT MUTAGEN 249
FT /note="H->F,L: Decreases binding to chlorophyll-a and
FT chlorophyll-b. Causes a minor decrease in LHCII complex
FT stability."
FT /evidence="ECO:0000269|PubMed:10587443,
FT ECO:0000269|PubMed:10587444"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2BHW"
FT HELIX 92..123
FT /evidence="ECO:0007829|PDB:2BHW"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2BHW"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2BHW"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:2BHW"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2BHW"
FT HELIX 161..181
FT /evidence="ECO:0007829|PDB:2BHW"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2BHW"
FT HELIX 207..238
FT /evidence="ECO:0007829|PDB:2BHW"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:2BHW"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:2BHW"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:2BHW"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:2BHW"
SQ SEQUENCE 269 AA; 28654 MW; D2BD6A9EFC4BAF77 CRC64;
MAASSSSSMA LSSPTLAGKQ LKLNPSSQEL GAARFTMRKS ATTKKVASSG SPWYGPDRVK
YLGPFSGESP SYLTGEFPGD YGWDTAGLSA DPETFSKNRE LEVIHSRWAM LGALGCVFPE
LLSRNGVKFG EAVWFKAGSQ IFSEGGLDYL GNPSLVHAQS ILAIWATQVI LMGAVEGYRI
AGGPLGEVVD PLYPGGSFDP LGLADDPEAF AELKVKELKN GRLAMFSMFG FFVQAIVTGK
GPLENLADHL ADPVNNNAWS YATNFVPGK
