CB28_PEA
ID CB28_PEA Reviewed; 268 AA.
AC P27490; P35389; Q5I8X3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chlorophyll a-b binding protein 8, chloroplastic;
DE AltName: Full=LHCII type I CAB-8;
DE Flags: Precursor;
GN Name=CAB8; Synonyms=LHCB1;
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 [GENOMIC DNA].
RX PubMed=1884005; DOI=10.1007/bf00040649;
RA Alexander L., Falconet D., Fristensky B.W., White M.J., Watson J.C.,
RA Roe B.A., Thompson W.F.;
RT "Nucleotide sequence of Cab-8, a new type I gene encoding a chlorophyll
RT a/b-binding protein of LHC II in Pisum.";
RL Plant Mol. Biol. 17:523-526(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang Y.;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 110-125, 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 -!- INTERACTION:
CC P27490; Q8LBP4: ALB3; Xeno; NbExp=2; IntAct=EBI-8295162, EBI-1806831;
CC P27490; O22265: CAO; Xeno; NbExp=4; IntAct=EBI-8295162, EBI-780656;
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; X56538; CAA39883.1; -; Genomic_DNA.
DR EMBL; AY845253; AAW31511.1; -; mRNA.
DR PIR; S17429; CDPMI8.
DR PDB; 5XNL; EM; 2.70 A; 1/2/5/6/G/N/Y/g/n/y=37-268.
DR PDB; 5XNM; EM; 3.20 A; 1/2/5/6/G/N/Y/g/n/y=37-268.
DR PDB; 5XNN; EM; 3.60 A; 1/2=37-268.
DR PDB; 5XNO; EM; 3.50 A; 1/2=37-268.
DR PDB; 6YP7; EM; 3.80 A; G/N/Y/g/n/y=49-267.
DR PDBsum; 5XNL; -.
DR PDBsum; 5XNM; -.
DR PDBsum; 5XNN; -.
DR PDBsum; 5XNO; -.
DR PDBsum; 6YP7; -.
DR AlphaFoldDB; P27490; -.
DR SMR; P27490; -.
DR IntAct; P27490; 2.
DR MINT; P27490; -.
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..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..268
FT /note="Chlorophyll a-b binding protein 8, chloroplastic"
FT /id="PRO_0000003681"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
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 82
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 101
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 104
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 106
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 155
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 159
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 175
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 178
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 216
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 219
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 221
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 233
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:0000250|UniProtKB:P12333"
FT BINDING 248
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 257
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N2-acetylarginine"
FT /evidence="ECO:0000250"
FT CONFLICT 19..22
FT /note="ETSA -> KL (in Ref. 2; AAW31511)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="D -> E (in Ref. 2; AAW31511)"
FT /evidence="ECO:0000305"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 93..123
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 160..180
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 206..237
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:5XNL"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:5XNL"
SQ SEQUENCE 268 AA; 28526 MW; A1DE46C178D64DFB CRC64;
MAASSMALSS PTLTGKPVET SANPSSQELG GARFTMRKSA TTKKVASSGS PWYGPDRVKY
LGPFSGESPS YLTGEFPGDY GWDTAGLSAD PETFSKNREL EVIHSRWAML GALGCVFPEL
LSRNGVKFGE AVWFKAGSQI FSEGGLDYLG NPSLVHAQSI LAIWATQVIL MGAVEGYRIA
GGPLGEVVDP LYPGGSFDPL GLADDPEAFA ELKVKELKNG RLAMFSMFGF FVQAIVTGKG
PLENLADHLS DPVNNNAWSY ATNFVPGK
