CB23_POLMU
ID CB23_POLMU Reviewed; 265 AA.
AC P15195;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chlorophyll a-b binding protein type 1 member F3, chloroplastic;
DE AltName: Full=Chlorophyll a-b binding protein type I F3;
DE Short=CAB-F3;
DE AltName: Full=LHCP;
DE Flags: Precursor;
GN Name=CABF3;
OS Polystichum munitum (Western swordfern) (Aspidium munitum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Polypodiineae; Dryopteridaceae;
OC Dryopteridoideae; Polystichum.
OX NCBI_TaxID=3279;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2404274; DOI=10.1073/pnas.87.1.195;
RA Pichersky E., Soltis D., Soltis P.;
RT "Defective chlorophyll a/b-binding protein genes in the genome of a
RT homosporous fern.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:195-199(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.
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; M34396; AAA68425.1; -; Genomic_DNA.
DR PIR; A34805; A34805.
DR AlphaFoldDB; P15195; -.
DR SMR; P15195; -.
DR PRIDE; P15195; -.
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 3: Inferred from homology;
KW Chlorophyll; Chloroplast; Chromophore; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Photosynthesis; Photosystem I; Photosystem II; Plastid;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 37..265
FT /note="Chlorophyll a-b binding protein type 1 member F3,
FT chloroplastic"
FT /id="PRO_0000003693"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 57
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 79
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
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 101
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 103
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 152
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|UniProtKB:P12333"
FT BINDING 156
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 172
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 175
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 213
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 216
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 218
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 230
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 245
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 254
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
SQ SEQUENCE 265 AA; 28113 MW; E0C1707F5F3E1F7B CRC64;
MATSTAALTS TFSGQQLKPV NELSRKVGAG EARVQMMAPK SKAPSGSIWY GSDRPLYLGP
FSGSPPSYLS GEFPGDYGWD TAGLSADPET FAKNRELEVI HSRWAMLGAL GCVTPELLAK
NGVKFGEAVW FKAGSQIFAE GGLDYLGNPS LVHAQSILAI WACQVILMGA VEGYRVAGGP
LGEVEDPIYP GGSFDPLGLA DDPEAFAELK VKELKNGRLA MFSMFGFFVQ AIVTGKGPIE
NLSDHLADPA VNNAWAYATN FTPGK
