CB11_SOLLC
ID CB11_SOLLC Reviewed; 246 AA.
AC P12360;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Chlorophyll a-b binding protein 6A, chloroplastic;
DE AltName: Full=LHCI type I CAB-6A;
DE AltName: Full=Light-harvesting complex I 26 kDa protein;
DE Flags: Precursor;
GN Name=CAB6A;
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 [MRNA].
RX PubMed=3321058; DOI=10.1073/pnas.84.24.8844;
RA Hoffman N.E., Pichersky E., Malik V.S., Castresana C., Ko K., Darr S.C.,
RA Cashmore A.R.;
RT "A cDNA clone encoding a photosystem I protein with homology to photosystem
RT II chlorophyll a/b-binding polypeptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8844-8848(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX AGRICOLA=IND91054590; DOI=10.1007/BF00166457;
RA Pichersky E., Hoffman N.E., Bernatzky R., Piechulla B., Tanksley S.D.,
RA Cashmore A.R.;
RT "Molecular characterization and genetic mapping of DNA sequences encoding
RT the type I chlorophyll a/b-binding polypeptide of photosystem I in
RT Lycopersicon esculentum (tomato).";
RL Plant Mol. Biol. 9:205-216(1987).
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; J03558; AAA34186.1; -; mRNA.
DR EMBL; M17633; AAA34140.1; -; Genomic_DNA.
DR PIR; S00443; S00443.
DR PIR; S06329; S06329.
DR RefSeq; NP_001234032.2; NM_001247103.2.
DR AlphaFoldDB; P12360; -.
DR SMR; P12360; -.
DR STRING; 4081.Solyc05g056070.2.1; -.
DR PaxDb; P12360; -.
DR PRIDE; P12360; -.
DR GeneID; 544310; -.
DR KEGG; sly:544310; -.
DR eggNOG; ENOG502QTYF; Eukaryota.
DR InParanoid; P12360; -.
DR OrthoDB; 1457167at2759; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P12360; baseline and differential.
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: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 2: Evidence at transcript level;
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..45
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 46..246
FT /note="Chlorophyll a-b binding protein 6A, chloroplastic"
FT /id="PRO_0000003710"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 49
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 69
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
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 91
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 93
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 134
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 154
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 157
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 192
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 195
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 197
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 209
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 225
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"
FT CONFLICT 33
FT /note="Y -> S (in Ref. 2; AAA34140)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="F -> S (in Ref. 2; AAA34140)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="S -> P (in Ref. 2; AAA34140)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="I -> F (in Ref. 2; AAA34140)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="L -> P (in Ref. 2; AAA34140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 26575 MW; 4FC2651B6E84F32F CRC64;
MASNTLMSCG IPAVCPSFLS STKSKFAAAM PVYVGATNFM SRFSMSADWM PGQPRPSYLD
GSAPGDFGFD SLGLGEVPAN LERYKESELI HCRWAMLAVP GIIVPEALGL GNWVKAQEWA
AIPGGQATYL GQPVPWGTLP TILAIEFLAI AFVEHQRSME KDSEKKKYPG GAFDPLGYSK
DPAKFEELKV KEIKNGRLAL LAIVGFCVQQ SAYLGTGPLE NLATHLADPW HNNIGDVIIP
KGIFPN
