CB121_HORVU
ID CB121_HORVU Reviewed; 245 AA.
AC Q9SDM1; Q36717;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Chlorophyll a-b binding protein 1B-21, chloroplastic;
DE AltName: Full=LHCI type I CAB-1B-21;
DE AltName: Full=LHCI-730 chlorophyll a/b binding protein;
DE AltName: Full=Light-harvesting complex I 21 kDa protein;
DE Flags: Precursor;
GN Name=LHC Ib-21; Synonyms=LHCA1;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Klimmek F., Knoetzel J., Grimme L.H.;
RT "H. vulgare LHCI-730 chlorophyll a/b binding protein precursor (Lhca1)
RT mRNA.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-245, PROTEIN SEQUENCE OF 45-58, AND
RP INDUCTION BY LIGHT.
RX PubMed=8278496; DOI=10.1104/pp.101.1.227;
RA Anandan S., Morishige D.T., Thornber J.P.;
RT "Light-induced biogenesis of light-harvesting complex I (LHC I) during
RT chloroplast development in barley (Hordeum vulgare). Studies using cDNA
RT clones of the 21- and 20-kilodalton LHC I apoproteins.";
RL Plant Physiol. 101:227-236(1993).
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:0000250}.
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:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:8278496}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB29485.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF218305; AAF23819.1; -; mRNA.
DR EMBL; S68728; AAB29485.1; ALT_FRAME; mRNA.
DR PIR; PQ0764; PQ0764.
DR AlphaFoldDB; Q9SDM1; -.
DR SMR; Q9SDM1; -.
DR EnsemblPlants; HORVU.MOREX.r2.7HG0560430.1; HORVU.MOREX.r2.7HG0560430.1; HORVU.MOREX.r2.7HG0560430.
DR EnsemblPlants; HORVU.MOREX.r2.7HG0560430.1.mrna1; HORVU.MOREX.r2.7HG0560430.1.mrna1; HORVU.MOREX.r2.7HG0560430.1.
DR Gramene; HORVU.MOREX.r2.7HG0560430.1; HORVU.MOREX.r2.7HG0560430.1; HORVU.MOREX.r2.7HG0560430.
DR Gramene; HORVU.MOREX.r2.7HG0560430.1.mrna1; HORVU.MOREX.r2.7HG0560430.1.mrna1; HORVU.MOREX.r2.7HG0560430.1.
DR ExpressionAtlas; Q9SDM1; baseline and differential.
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; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:8278496"
FT CHAIN 45..245
FT /note="Chlorophyll a-b binding protein 1B-21,
FT chloroplastic"
FT /id="PRO_5000057682"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 48
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"
FT BINDING 68
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
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"
FT BINDING 90
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"
FT BINDING 92
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 133
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"
FT BINDING 153
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"
FT BINDING 156
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 191
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"
FT BINDING 194
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"
FT BINDING 196
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="5"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 224
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"
FT CONFLICT 25
FT /note="S -> P (in Ref. 2; AAB29485)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="D -> A (in Ref. 2; AAB29485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 26464 MW; 78C949D40C09B34F CRC64;
MASSSGLRSC SAVGVPSLLA PSSRSGRSGL PFCAYATTSG RVTMSAEWFP GQPRPAHLDG
SSPGDFGFDP LGLATVPENF ERFKESEIYH CRWAMLCVPG VLVPEALGLG NWVKAQEWAA
LPDGQATYLG NPVPWGNLPT ILAIEFLAIA FAEQQRTMEK DPEKKKYPGG AFDPLGFSKD
PAKFEELKLK EIKNGRLAML AFVGFCVQQS AYPGTGPLEN LATHLADPWH NNIGDIVIPR
NIYGP
