ID CB23_APIGR Reviewed; 264 AA. AC P92919; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Chlorophyll a-b binding protein, chloroplastic; DE AltName: Allergen=Api g 3; DE Flags: Precursor; GN Name=LHC0; OS Apium graveolens (Celery). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade; OC Apieae; Apium. OX NCBI_TaxID=4045; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Bulb; RA Hoffmann-Sommergruber K., Pec M., Ferris R., O'Riordain G., Ebner C., RA Scheiner O., Breiteneder H.; RT "Characterization of a chlorophyll ab binding protein from celery as a food RT allergen Api g 3."; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. 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. {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 -!- ALLERGEN: Causes an allergic reaction in human. CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding CC (LHC) protein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z75663; CAA99993.1; -; mRNA. DR AlphaFoldDB; P92919; -. DR SMR; P92919; -. DR Allergome; 3086; Api g 3.0101. DR Allergome; 774; Api g 3. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. 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 Gene3D; 1.10.3460.10; Chlorophyll a/b binding protein domain; 1. DR InterPro; IPR001344; Chloro_AB-bd_pln. DR InterPro; IPR022796; Chloroa_b-bind. DR PANTHER; PTHR21649:SF33; CHLOROPHYLL A-B BINDING PROTEIN 2.1, CHLOROPLASTIC-RELATED; 1. DR PANTHER; PTHR21649; CHLOROPHYLL A/B BINDING PROTEIN; 1. DR Pfam; PF00504; Chloroa_b-bind; 1. DR SUPFAM; SSF103511; Chlorophyll a-b binding protein; 1. PE 1: Evidence at protein level; KW Acetylation; Allergen; Chlorophyll; Chloroplast; Chromophore; Magnesium; KW Membrane; Metal-binding; Phosphoprotein; Photosynthesis; Photosystem I; KW Photosystem II; Plastid; Thylakoid; Transit peptide; Transmembrane; KW Transmembrane helix. FT TRANSIT 1..35 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 36..264 FT /note="Chlorophyll a-b binding protein, chloroplastic" FT /id="PRO_0000003646" FT TRANSMEM 98..118 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 150..170 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 218..238 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 56 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 78 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 97 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 100 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 102 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 135 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 145 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 151 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 155 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P07371" FT BINDING 171 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 174 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 180 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 211 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="5" FT /evidence="ECO:0000250" FT BINDING 212 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 215 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 217 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 229 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 244 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 253 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="6" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="5" FT /evidence="ECO:0000250" FT MOD_RES 36 FT /note="N2-acetylarginine" FT /evidence="ECO:0000250" FT MOD_RES 38 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" SQ SEQUENCE 264 AA; 28076 MW; 07126C7D5D86BA66 CRC64; MAASTMALSS PALAGKAVKV APSSSELFGN GRVSMRKTVK APVSDSPWYG PDRVKYLGPF SGEAPSYLTG EFPGDYGWDT AGLSADPETF AKNRELEVIH SRWAMLGALG CVFPELLARN GVKFGEAVWF KAGSQIFSEG GLDYLGNPSL VHAQSILSIW ATQVILMGAV EGYRVAGGPL GEIVDPLYPG GSFDPLGLAE DPERSAELKV KELKNGRLAM FSMFGFFVQA IVTGKGPLEN LADHLADPVN NNAWAFATNF VPGK //