ID A0A384LC70_ARATH Unreviewed; 290 AA. AC A0A384LC70; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 02-OCT-2024, entry version 29. DE RecName: Full=Chlorophyll a-b binding protein, chloroplastic {ECO:0000256|RuleBase:RU363080}; GN OrderedLocusNames=AXX17_At5g00570 {ECO:0000313|EMBL:OAO95122.1}; GN ORFNames=AN1_LOCUS20940 {ECO:0000313|EMBL:VYS65534.1}, C24_LOCUS20837 GN {ECO:0000313|EMBL:CAA0400007.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000313|EMBL:OAO95122.1, ECO:0000313|Proteomes:UP000078284}; RN [1] {ECO:0000313|Proteomes:UP000078284} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Landsberg erecta {ECO:0000313|Proteomes:UP000078284}; RX PubMed=27354520; DOI=10.1073/pnas.1607532113; RA Zapata L., Ding J., Willing E.M., Hartwig B., Bezdan D., Jiao W.B., RA Patel V., Velikkakam James G., Koornneef M., Ossowski S., Schneeberger K.; RT "Chromosome-level assembly of Arabidopsis thaliana Ler reveals the extent RT of translocation and inversion polymorphisms."; RL Proc. Natl. Acad. Sci. U.S.A. 113:E4052-E4060(2016). RN [2] {ECO:0000313|EMBL:OAO95122.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Leaf {ECO:0000313|EMBL:OAO95122.1}; RA Zapata L., Schneeberger K., Ossowski S.; RT "Full-length assembly of Arabidopsis thaliana Ler reveals the complement of RT translocations and inversions."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:VYS65534.1, ECO:0000313|Proteomes:UP000426265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. An-1 {ECO:0000313|Proteomes:UP000426265}, and cv. C24 RC {ECO:0000313|Proteomes:UP000434276}; RA Jiao W.-B., Schneeberger K.; RL Submitted (NOV-2019) 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. {ECO:0000256|RuleBase:RU363080}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|RuleBase:RU363080}. CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding CC (LHC) protein family. {ECO:0000256|ARBA:ARBA00007259, CC ECO:0000256|RuleBase:RU363080}. 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; CACSHJ010000096; CAA0400007.1; -; Genomic_DNA. DR EMBL; LUHQ01000005; OAO95122.1; -; Genomic_DNA. DR EMBL; CACRSJ010000110; VYS65534.1; -; Genomic_DNA. DR RefSeq; NP_195773.1; NM_120231.4. DR AlphaFoldDB; A0A384LC70; -. DR SMR; A0A384LC70; -. DR EnsemblPlants; AT5G01530.1; AT5G01530.1; AT5G01530. DR GeneID; 830325; -. DR Gramene; AT5G01530.1; AT5G01530.1; AT5G01530. DR KEGG; ath:AT5G01530; -. DR OMA; LWYPGAI; -. DR OrthoDB; 444860at2759; -. DR Proteomes; UP000078284; Chromosome 5. DR Proteomes; UP000426265; Unassembled WGS sequence. DR Proteomes; UP000434276; Unassembled WGS sequence. DR ExpressionAtlas; A0A384LC70; baseline and differential. 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: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:SF6; CHLOROPHYLL A-B BINDING PROTEIN CP29.1, CHLOROPLASTIC; 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 3: Inferred from homology; KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|PIRSR:PIRSR601344- KW 1}; Chloroplast {ECO:0000256|RuleBase:RU363080}; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|RuleBase:RU363080}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, KW ECO:0000256|RuleBase:RU363080}; KW Photosystem I {ECO:0000256|ARBA:ARBA00022836, KW ECO:0000256|RuleBase:RU363080}; KW Photosystem II {ECO:0000256|RuleBase:RU363080}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|RuleBase:RU363080}; KW Thylakoid {ECO:0000256|RuleBase:RU363080}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT BINDING 140 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR601344-1" FT BINDING 143 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601344-1" FT BINDING 145 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:0000256|PIRSR:PIRSR601344-1" FT BINDING 180 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601344-1" FT BINDING 203 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:0000256|PIRSR:PIRSR601344-1" FT BINDING 210 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:0000256|PIRSR:PIRSR601344-1" FT BINDING 242 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601344-1" FT BINDING 247 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601344-1" FT BINDING 259 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601344-1" FT BINDING 274 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601344-1" SQ SEQUENCE 290 AA; 31139 MW; 991C69CF3B773C79 CRC64; MAATSAAAAA ASSIMGTRVA PGIHPGSGRF TAVFGFGKKK AAPKKSAKKT VTTDRPLWYP GAISPDWLDG SLVGDYGFDP FGLGKPAEYL QFDIDSLDQN LAKNLAGDVI GTRTEAADAK STPFQPYSEV FGIQRFRECE LIHGRWAMLA TLGALSVEWL TGVTWQDAGK VELVDGSSYL GQPLPFSIST LIWIEVLVIG YIEFQRNAEL DSEKRLYPGG KFFDPLGLAA DPEKTAQLQL AEIKHARLAM VAFLGFAVQA AATGKGPLNN WATHLSDPLH TTIIDTFSSS //