ID   CB222_PEA               Reviewed;          18 AA.
AC   P35387;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Chlorophyll a-b binding protein 22, chloroplastic;
DE   AltName: Full=LHCII type I CAB-22;
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}
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   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..>18
FT                   /note="Chlorophyll a-b binding protein 22, chloroplastic"
FT                   /id="PRO_0000310861"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:2174365"
FT   NON_TER         18
FT                   /evidence="ECO:0000303|PubMed:2174365"
SQ   SEQUENCE   18 AA;  1743 MW;  75D6ACD85152A97F CRC64;
     LAVPGILVPE ALGLGNXV