ID   CB22_SPIOL              Reviewed;           9 AA.
AC   Q9T2K9;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Chlorophyll a-b binding protein;
DE   AltName: Full=LHCII type II CAB;
DE            Short=LHCP;
DE   Flags: Fragment;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, ACETYLATION AT ARG-1, AND
RP   PHOSPHORYLATION AT THR-3.
RC   TISSUE=Leaf {ECO:0000269|PubMed:1894641};
RX   PubMed=1894641; DOI=10.1016/s0021-9258(19)47412-7;
RA   Michel H., Griffin P.R., Shabanowitz J., Hunt D.F., Bennett J.;
RT   "Tandem mass spectrometry identifies sites of three post-translational
RT   modifications of spinach light-harvesting chlorophyll protein II.
RT   Proteolytic cleavage, acetylation, and phosphorylation.";
RL   J. Biol. Chem. 266:17584-17591(1991).
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
CC       {ECO:0000269|PubMed:1894641}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:1894641}.
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   iPTMnet; Q9T2K9; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
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   Acetylation; Chlorophyll; Chloroplast; Chromophore;
KW   Direct protein sequencing; Magnesium; Membrane; Metal-binding;
KW   Phosphoprotein; Photosynthesis; Photosystem I; Photosystem II; Plastid;
KW   Thylakoid.
FT   CHAIN           1..>9
FT                   /note="Chlorophyll a-b binding protein"
FT                   /id="PRO_0000165477"
FT   MOD_RES         1
FT                   /note="N2-acetylarginine"
FT                   /evidence="ECO:0000269|PubMed:1894641"
FT   MOD_RES         3
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:1894641"
FT   NON_TER         9
FT                   /evidence="ECO:0000303|PubMed:1894641"
SQ   SEQUENCE   9 AA;  1042 MW;  6B5D6DC5B322D1B4 CRC64;
     RRTVKSAPQ