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CB21_PEA
ID   CB21_PEA                Reviewed;         228 AA.
AC   P04159; P35389;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Chlorophyll a-b binding protein AB96;
DE   AltName: Full=LHCII type I CAB-AB96;
DE            Short=LHCP;
DE   AltName: Full=Major 15;
DE   Flags: Fragment;
GN   Name=AB96;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Progress No. 9;
RX   PubMed=6296093; DOI=10.1016/s0021-9258(18)32995-8;
RA   Coruzzi G., Broglie R., Cashmore A., Chua N.-H.;
RT   "Nucleotide sequences of two pea cDNA clones encoding the small subunit of
RT   ribulose 1,5-bisphosphate carboxylase and the major chlorophyll a/b-binding
RT   thylakoid polypeptide.";
RL   J. Biol. Chem. 258:1399-1402(1983).
RN   [2]
RP   PROTEIN SEQUENCE OF 70-85, AND FUNCTION.
RC   TISSUE=Seedling;
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   -!- 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. {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   EMBL; J01253; AAA33650.1; -; mRNA.
DR   PIR; A26194; CDPM96.
DR   AlphaFoldDB; P04159; -.
DR   SMR; P04159; -.
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:0009765; P:photosynthesis, light harvesting; IEA:InterPro.
DR   InterPro; IPR001344; Chloro_AB-bd_pln.
DR   InterPro; IPR022796; Chloroa_b-bind.
DR   PANTHER; PTHR21649; PTHR21649; 1.
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..228
FT                   /note="Chlorophyll a-b binding protein AB96"
FT                   /id="PRO_0000165474"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         20
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
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         42
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
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         64
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         66
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
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         119
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250|UniProtKB:P07371"
FT   BINDING         135
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="3"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         138
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="3"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         179
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="4"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         181
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="6"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         217
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   228 AA;  24328 MW;  0312E2BDBB2168E8 CRC64;
     TTKKVASSSS PWHGPDGVKY LGPFSGESPS YLTGEFPGDY GWDTAGLSAD PETFAKNREL
     EVIHSRWAML GALGCVFPEL LSRNGVKFGE AVWFKAGSQI FSEGGLDYLG NPSLVHAQSI
     LAIWATQVIL MGAVEGYRIA GGPLGEVVDP LYPGGSFDPL GLAEVPEAFA ELKVKELKNG
     RLAMFSMFGF FVPAIVTGKG PLENLADHLA DPVNNNAWSY ATNFVPGK
 
 
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