CB23C_PEA
ID CB23C_PEA Reviewed; 22 AA.
AC Q7M1L0; P35390;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Chlorophyll a-b binding protein 3c, chloroplastic;
DE AltName: Full=LHCII type I CAB-3c;
DE Flags: Fragment;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1] {ECO:0000305, ECO:0000312|PIR:S13977}
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Seedling {ECO:0000269|PubMed:2174365};
RX PubMed=2174365; DOI=10.1111/j.1432-1033.1990.tb19393.x;
RA Jahns P., Junge W.;
RT "Dicyclohexylcarbodiimide-binding proteins related to the short circuit of
RT the proton-pumping activity of photosystem II. Identified as light-
RT harvesting chlorophyll-a/b-binding proteins.";
RL Eur. J. Biochem. 193:731-736(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. {ECO:0000269|PubMed:2174365,
CC ECO:0000305}.
CC -!- FUNCTION: May channel protons produced in the catalytic Mn center of
CC water oxidation into the thylakoid lumen. {ECO:0000269|PubMed:2174365}.
CC -!- COFACTOR:
CC Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and
CC carotenoids such as lutein and neoxanthin.
CC {ECO:0000250|UniProtKB:P07371};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
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. {ECO:0000305}.
CC -!- PTM: Photoregulated by reversible phosphorylation of its threonine
CC residues. {ECO:0000250|UniProtKB:P07371}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000255}.
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DR PIR; S13977; S13977.
DR AlphaFoldDB; Q7M1L0; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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.
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.
FT CHAIN <1..>22
FT /note="Chlorophyll a-b binding protein 3c, chloroplastic"
FT /id="PRO_0000310858"
FT NON_TER 1
FT /evidence="ECO:0000312|PIR:S13977"
FT NON_TER 22
FT /evidence="ECO:0000312|PIR:S13977"
SQ SEQUENCE 22 AA; 2213 MW; A8F4EA16DEA5B4A8 CRC64;
LGALGCVFPE LLSGNGVKFG YA