CB2A_SPIOL
ID CB2A_SPIOL Reviewed; 267 AA.
AC P12333;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Chlorophyll a-b binding protein, chloroplastic;
DE AltName: Full=LHCII type I CAB;
DE Short=LHCP;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=2668882; DOI=10.1093/nar/17.13.5387;
RA Mason J.G.;
RT "Nucleotide sequence of a cDNA encoding the light-harvesting chlorophyll
RT a/b binding protein from spinach.";
RL Nucleic Acids Res. 17:5387-5387(1989).
RN [2]
RP PROTEIN SEQUENCE OF 36-44, ACETYLATION AT ARG-36, AND PHOSPHORYLATION AT
RP THR-38.
RC TISSUE=Leaf;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) OF 36-267 IN COMPLEX WITH
RP CHLOROPHYLL A-B AND CAROTENOIDS, AND COFACTOR.
RX PubMed=15029188; DOI=10.1038/nature02373;
RA Liu Z., Yan H., Wang K., Kuang T., Zhang J., Gui L., An X., Chang W.;
RT "Crystal structure of spinach major light-harvesting complex at 2.72 A
RT resolution.";
RL Nature 428:287-292(2004).
RN [4] {ECO:0007744|PDB:4LCZ}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 44-267 IN COMPLEX WITH
RP CHLOROPHYLL A; CHLOROPHYLL B AND CAROTENOIDS, AND COFACTOR.
RX PubMed=24482437; DOI=10.1093/mp/ssu005;
RA Wan T., Li M., Zhao X., Zhang J., Liu Z., Chang W.;
RT "Crystal structure of a multilayer packed major light-harvesting complex:
RT implications for grana stacking in higher plants.";
RL Mol. Plant 7:916-919(2014).
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.
CC {ECO:0000305|PubMed:15029188, ECO:0000305|PubMed:24482437};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
CC {ECO:0000269|PubMed:15029188}.
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:0000269|PubMed:1894641}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; X14341; CAA32526.1; -; mRNA.
DR PIR; JQ0020; JQ0020.
DR PDB; 1RWT; X-ray; 2.72 A; A/B/C/D/E/F/G/H/I/J=36-267.
DR PDB; 3JCU; EM; 3.20 A; G/N/Y/g/n/y=1-267.
DR PDB; 4LCZ; X-ray; 2.60 A; A/B/C=44-267.
DR PDBsum; 1RWT; -.
DR PDBsum; 3JCU; -.
DR PDBsum; 4LCZ; -.
DR AlphaFoldDB; P12333; -.
DR SMR; P12333; -.
DR DIP; DIP-62013N; -.
DR IntAct; P12333; 1.
DR CarbonylDB; P12333; -.
DR iPTMnet; P12333; -.
DR EvolutionaryTrace; P12333; -.
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 3D-structure; Acetylation; Chlorophyll; Chloroplast; Chromophore;
KW Direct protein sequencing; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Photosynthesis; Photosystem I; Photosystem II; Plastid;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:1894641"
FT CHAIN 36..267
FT /note="Chlorophyll a-b binding protein, chloroplastic"
FT /id="PRO_0000003700"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 59
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:0000269|PubMed:15029188,
FT ECO:0000269|PubMed:24482437"
FT BINDING 81
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT BINDING 87
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT BINDING 100
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:0000269|PubMed:15029188,
FT ECO:0000269|PubMed:24482437"
FT BINDING 103
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:0000269|PubMed:15029188,
FT ECO:0000269|PubMed:24482437"
FT BINDING 105
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT BINDING 138
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT BINDING 148
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT BINDING 154
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:0000269|PubMed:15029188,
FT ECO:0000269|PubMed:24482437"
FT BINDING 158
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT BINDING 166
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT BINDING 166
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 174
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:0000269|PubMed:15029188,
FT ECO:0000269|PubMed:24482437"
FT BINDING 177
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT BINDING 183
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT BINDING 214
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT BINDING 215
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:0000269|PubMed:15029188,
FT ECO:0000269|PubMed:24482437"
FT BINDING 218
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:0000269|PubMed:15029188,
FT ECO:0000269|PubMed:24482437"
FT BINDING 220
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT BINDING 232
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:15029188,
FT ECO:0000269|PubMed:24482437"
FT BINDING 247
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:0000269|PubMed:15029188,
FT ECO:0000269|PubMed:24482437"
FT BINDING 256
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT BINDING 263
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT MOD_RES 36
FT /note="N2-acetylarginine"
FT /evidence="ECO:0000269|PubMed:1894641"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:1894641"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4LCZ"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4LCZ"
FT HELIX 90..121
FT /evidence="ECO:0007829|PDB:4LCZ"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4LCZ"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4LCZ"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:4LCZ"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4LCZ"
FT HELIX 159..179
FT /evidence="ECO:0007829|PDB:4LCZ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4LCZ"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:4LCZ"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 205..236
FT /evidence="ECO:0007829|PDB:4LCZ"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:4LCZ"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:4LCZ"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:1RWT"
SQ SEQUENCE 267 AA; 28424 MW; 23474EBDA23F6545 CRC64;
MASSTMALSS PSLAGKAVKL GPTASEIIGE GRITMRKTAG KPKTVQSSSP WYGPDRVKYL
GPFSGESPSY LTGEFPGDYG WDTAGLSADP ETFAKNRELE VIHCRWAMLG ALGCVFPELL
ARNGVKFGEA VWFKAGSQIF SEGGLDYLGN PSLVHAQSIL AIWACQVILM GAVEGYRIAG
GPLGEVVDPL YPGGSFDPLG LADDPEAFAE LKVKEIKNGR LAMFSMFGFF VQAIVTGKGP
LENLADHLAD PVNNNAWNFA TNFVPGK
