CB12_SOLLC
ID CB12_SOLLC Reviewed; 270 AA.
AC P10708;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Chlorophyll a-b binding protein 7, chloroplastic;
DE AltName: Full=LHCI type II CAB-7;
DE Flags: Precursor;
GN Name=CAB7;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX AGRICOLA=IND92000604; DOI=10.1007/BF00016015;
RA Pichersky E., Tanksley S.D., Piechulla B., Stayton M.M., Dunsmuir P.;
RT "Nucleotide sequence and chromosomal location of Cab-7, the tomato gene
RT encoding the type II chlorophyll a/b-binding polypeptide of photosystem
RT I.";
RL Plant Mol. Biol. 11:69-71(1988).
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}.
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; M20241; AAA34159.1; -; Genomic_DNA.
DR EMBL; X14036; CAA32197.1; -; Genomic_DNA.
DR PIR; S07408; S07408.
DR RefSeq; NP_001296176.1; NM_001309247.1.
DR AlphaFoldDB; P10708; -.
DR SMR; P10708; -.
DR STRING; 4081.Solyc10g006230.2.1; -.
DR PaxDb; P10708; -.
DR PRIDE; P10708; -.
DR GeneID; 101264376; -.
DR KEGG; sly:101264376; -.
DR eggNOG; ENOG502QRXM; Eukaryota.
DR HOGENOM; CLU_057943_6_0_1; -.
DR InParanoid; P10708; -.
DR OrthoDB; 991539at2759; -.
DR PhylomeDB; P10708; -.
DR Proteomes; UP000004994; Unplaced.
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:0019904; F:protein domain specific binding; IEA:EnsemblPlants.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR GO; GO:0009644; P:response to high light intensity; IEA:EnsemblPlants.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR GO; GO:0009645; P:response to low light intensity stimulus; IEA:EnsemblPlants.
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 Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..270
FT /note="Chlorophyll a-b binding protein 7, chloroplastic"
FT /id="PRO_0000003711"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 68
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 88
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
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"
FT BINDING 110
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"
FT BINDING 112
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 155
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 165
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"
FT BINDING 168
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 222
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"
FT BINDING 225
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"
FT BINDING 227
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 239
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"
FT BINDING 254
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"
SQ SEQUENCE 270 AA; 29046 MW; 4A59109CC5851044 CRC64;
MASACASSTI AAVAFSSPSS RRNGSIVGTT KASFLGGRRL RVSKYSTTPT ARSATTVCVA
ADPDRPLWFP GSTPPPWLDG SLPGDFGFDP LGLASDPESL RWNQQAELVH CRWAMLGAAG
IFIPELLTKI GILNTPSWYT AGEQEYFTDT TTLFIVELVL IGWAEGRRWA DIIKPGCVNT
DPIFPNNKLT GTDVGYPGGL WFDPLGWGSG SPAKIKELRT KEIKNGRLAM LAVMGAWFQH
IYTGTGPIDN LFAHLADPGH ATIFAAFSPK
