ID   CCAC_AMPCA              Reviewed;         102 AA.
AC   P55738;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Caroteno-chlorophyll a-c-binding protein;
DE   Flags: Fragment;
OS   Amphidinium carterae (Dinoflagellate).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Amphidiniales; Amphidiniaceae;
OC   Amphidinium.
OX   NCBI_TaxID=2961;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8502722; DOI=10.1111/j.1751-1097.1993.tb02267.x;
RA   Hiller R.G., Wrench P.M., Gooley A.P., Shoebridge G., Breton J.;
RT   "The major intrinsic light-harvesting protein of Amphidinium:
RT   characterization and relation to other light-harvesting proteins.";
RL   Photochem. Photobiol. 57:125-131(1993).
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   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:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   InterPro; IPR022796; Chloroa_b-bind.
DR   Pfam; PF00504; Chloroa_b-bind; 1.
PE   1: Evidence at protein level;
KW   Chlorophyll; Chloroplast; Chromophore; Direct protein sequencing;
KW   Magnesium; Membrane; Metal-binding; Phosphoprotein; Photosynthesis;
KW   Photosystem I; Photosystem II; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..>102
FT                   /note="Caroteno-chlorophyll a-c-binding protein"
FT                   /id="PRO_0000165480"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         36
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         39
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   NON_TER         1
FT   NON_TER         102
SQ   SEQUENCE   102 AA;  10951 MW;  66AF3E7D725FDA1E CRC64;
     XFENERGVAD PVGFFDPLGF TADGSVENFK KLAQTEIKHG RVAMLATMGY ITQEITGKLP
     GYLSPSTGVK YDDDINGVLG LIKIVPAGLW GIMIFYAALS LA