CB21_MAIZE
ID CB21_MAIZE Reviewed; 262 AA.
AC P12329;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Chlorophyll a-b binding protein 1, chloroplastic;
DE AltName: Full=LHCII type I CAB-1;
DE Short=LHCP;
DE Flags: Precursor;
GN Name=CAB1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. B37;
RX PubMed=2651890; DOI=10.1007/bf00427040;
RA Sullivan T.D., Christensen A.H., Quail P.H.;
RT "Isolation and characterization of a maize chlorophyll a/b binding protein
RT gene that produces high levels of mRNA in the dark.";
RL Mol. Gen. Genet. 215:431-440(1989).
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.
CC -!- COFACTOR:
CC Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and
CC carotenoids such as lutein and neoxanthin. {ECO:0000250};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; X14794; CAA32900.1; -; Genomic_DNA.
DR PIR; S04453; S04453.
DR RefSeq; NP_001147639.1; NM_001154167.1.
DR PDB; 5ZJI; EM; 3.30 A; X/Z=31-262.
DR PDBsum; 5ZJI; -.
DR AlphaFoldDB; P12329; -.
DR SMR; P12329; -.
DR IntAct; P12329; 1.
DR STRING; 4577.AC207722.2_FGP009; -.
DR PaxDb; P12329; -.
DR PRIDE; P12329; -.
DR GeneID; 100281248; -.
DR KEGG; zma:100281248; -.
DR MaizeGDB; 61648; -.
DR eggNOG; ENOG502QPU1; Eukaryota.
DR HOGENOM; CLU_057943_2_0_1; -.
DR OMA; AYRTGIS; -.
DR OrthoDB; 961261at2759; -.
DR Proteomes; UP000007305; Chromosome 7.
DR Genevisible; P12329; ZM.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IBA:GO_Central.
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:0009768; P:photosynthesis, light harvesting in photosystem I; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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 Magnesium; Membrane; Metal-binding; Phosphoprotein; Photosynthesis;
KW Photosystem I; Photosystem II; Plastid; Reference proteome; Thylakoid;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..30
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 31..262
FT /note="Chlorophyll a-b binding protein 1, chloroplastic"
FT /id="PRO_0000003670"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 54
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|UniProtKB:P12333"
FT BINDING 76
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
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:P12333"
FT BINDING 98
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 100
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 149
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 /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
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:P12333"
FT BINDING 172
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 210
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 213
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 215
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 227
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 BINDING 242
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:P12333"
FT BINDING 251
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT MOD_RES 31
FT /note="N2-acetylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 85..117
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 154..174
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 200..231
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:5ZJI"
SQ SEQUENCE 262 AA; 27816 MW; 4165FADFE6727853 CRC64;
MAASTMAISS TAMAGTPIKV GSFGEGRITM RKTVGKPKVA ASGSPWYGPD RVKYLGPFSG
EPPSYLTGEF PGDYGWDTAG LSADPETFAK NRELEVIHSR WAMLGALGCV FPELLSRNGV
KFGEAVWFKA GSQIFSEGGL DYLGNPSLIH AQSILAIWAC QVVLMGAVEG YRIAGGPLGE
VVDPLYPGGS FDPLGLADDP EAFAELKVKE LKNGRLAMFS MFGFFVQAIV TGKGPLENLA
DHIADPVNNN AWAYATNFVP GN
