ID   CB22_POPEU              Reviewed;          32 AA.
AC   P84990;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Chlorophyll a-b binding protein 2, chloroplastic;
DE   AltName: Full=LHCII type I CAB-2;
DE            Short=LHCP;
DE   Flags: Fragments;
OS   Populus euphratica (Euphrates poplar).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=75702;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf {ECO:0000269|Ref.1};
RA   Ferreira S.;
RT   "Molecular analysis of Populus euphratica Oliv. response to moderate heat
RT   stress.";
RL   Thesis (2006), ICAT-FCUL, Portugal.
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:0000305}.
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:P12333};
CC   -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
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:P12333}.
CC   -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC       (LHC) protein family. {ECO:0000255}.
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DR   AlphaFoldDB; P84990; -.
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.
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.
FT   CHAIN           <1..>32
FT                   /note="Chlorophyll a-b binding protein 2, chloroplastic"
FT                   /id="PRO_0000300509"
FT   BINDING         19
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|UniProtKB:P12333"
FT   BINDING         22
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|UniProtKB:P12333"
FT   BINDING         24
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_CONS        24..25
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         32
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   32 AA;  3801 MW;  1C9C3014098F6C9A CRC64;
     SAPQSIWYGP DRPKNRELEV IHSRFGEAVW FK