ID CB1A_ARATH Reviewed; 267 AA. AC P0CJ48; P04777; P83754; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=Chlorophyll a-b binding protein 2, chloroplastic; DE AltName: Full=Chlorophyll a-b protein 165; DE Short=CAB-165; DE AltName: Full=LHCII type I CAB-2; DE Flags: Precursor; GN Name=LHCB1.1; Synonyms=AB165, CAB2, LHCP-B; GN OrderedLocusNames=At1g29920; ORFNames=F1N18.4; 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; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=3012462; DOI=10.1093/nar/14.10.4051; RA Leutwiler L.S., Meyerowitz E.M., Tobin E.M.; RT "Structure and expression of three light-harvesting chlorophyll a/b-binding RT protein genes in Arabidopsis thaliana."; RL Nucleic Acids Res. 14:4051-4064(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP PROTEIN SEQUENCE OF 36-43, IDENTIFICATION BY MASS SPECTROMETRY, RP PHOSPHORYLATION AT THR-38, AND ACETYLATION AT ARG-36. RC STRAIN=cv. Columbia; RX PubMed=11113141; DOI=10.1074/jbc.m009394200; RA Vener A.V., Harms A., Sussman M.R., Vierstra R.D.; RT "Mass spectrometric resolution of reversible protein phosphorylation in RT photosynthetic membranes of Arabidopsis thaliana."; RL J. Biol. Chem. 276:6959-6966(2001). RN [7] RP INTERACTION WITH CAO/CPSRP43, AND MUTAGENESIS OF LEU-199. RX PubMed=18621669; DOI=10.1126/science.1158640; RA Stengel K.F., Holdermann I., Cain P., Robinson C., Wild K., Sinning I.; RT "Structural basis for specific substrate recognition by the chloroplast RT signal recognition particle protein cpSRP43."; RL Science 321:253-256(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19376835; DOI=10.1104/pp.109.138677; RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., RA Grossmann J., Gruissem W., Baginsky S.; RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel RT chloroplast kinase substrates and phosphorylation networks."; RL Plant Physiol. 150:889-903(2009). RN [9] RP INTERACTION WITH LTD, AND MUTAGENESIS OF 197-ASP--GLY-200; 210-GLU--LYS-212 RP AND 220-ARG--MET-223. RX PubMed=21505433; DOI=10.1038/ncomms1278; RA Ouyang M., Li X., Ma J., Chi W., Xiao J., Zou M., Chen F., Lu C., Zhang L.; RT "LTD is a protein required for sorting light-harvesting chlorophyll-binding RT proteins to the chloroplast SRP pathway."; RL Nat. Commun. 2:277-277(2011). 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 Interacts (via T14 domain) with LTD. Interacts with CAO/cpSRP43 during CC its post-translational targeting to the thylakoid. CC {ECO:0000269|PubMed:18621669, ECO:0000269|PubMed:21505433}. 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 -!- DOMAIN: The L18 domain (188-205) is required for the transit complex CC formation with CAO/cpSRP43 and the targeting to the thylakoid. CC -!- DOMAIN: The T14 domain (211-224) is required for the interaction with CC LTD and the translocation across the envelope. 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 --------------------------------------------------------------------------- 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; X03907; CAA27540.1; -; Genomic_DNA. DR EMBL; AC008030; AAG10604.1; -; Genomic_DNA. DR EMBL; CP002684; AEE31150.1; -; Genomic_DNA. DR EMBL; AY052237; AAK97707.1; -; mRNA. DR EMBL; AY054198; AAL06859.1; -; mRNA. DR EMBL; AY060500; AAL31113.1; -; mRNA. DR EMBL; AY062814; AAL32892.1; -; mRNA. DR EMBL; AY081572; AAM10134.1; -; mRNA. DR EMBL; AY128345; AAM91548.1; -; mRNA. DR EMBL; BT000726; AAN31868.1; -; mRNA. DR EMBL; AY086905; AAM63949.1; -; mRNA. DR PIR; A29280; A29280. DR RefSeq; NP_564339.1; NM_102731.3. DR RefSeq; NP_564340.1; NM_102732.3. DR PDB; 4YZH; X-ray; 2.00 A; B=36-50. DR PDB; 8J6Z; EM; 2.79 A; x/y=1-267. DR PDBsum; 4YZH; -. DR PDBsum; 8J6Z; -. DR AlphaFoldDB; P0CJ48; -. DR EMDB; EMD-36021; -. DR SMR; P0CJ48; -. DR BioGRID; 25104; 19. DR BioGRID; 25105; 14. DR IntAct; P0CJ48; 1. DR STRING; 3702.P0CJ48; -. DR TCDB; 3.E.2.2.3; the photosynthetic reaction center (prc) family. DR iPTMnet; P0CJ48; -. DR PaxDb; 3702-AT1G29910-1; -. DR DNASU; 839869; -. DR EnsemblPlants; AT1G29910.1; AT1G29910.1; AT1G29910. DR EnsemblPlants; AT1G29920.1; AT1G29920.1; AT1G29920. DR GeneID; 839869; -. DR GeneID; 839870; -. DR Gramene; AT1G29910.1; AT1G29910.1; AT1G29910. DR Gramene; AT1G29920.1; AT1G29920.1; AT1G29920. DR KEGG; ath:AT1G29910; -. DR KEGG; ath:AT1G29920; -. DR Araport; AT1G29920; -. DR TAIR; AT1G29920; CAB2. DR eggNOG; ENOG502QPU1; Eukaryota. DR HOGENOM; CLU_057943_2_0_1; -. DR InParanoid; P0CJ48; -. DR OMA; KRYHIES; -. DR OrthoDB; 1009557at2759; -. DR PhylomeDB; P0CJ48; -. DR PRO; PR:P0CJ48; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; P0CJ48; baseline and differential. DR GO; GO:0048046; C:apoplast; HDA:TAIR. DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR. DR GO; GO:0005634; C:nucleus; HDA:TAIR. DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW. DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW. DR GO; GO:0009579; C:thylakoid; HDA:TAIR. DR GO; GO:0016168; F:chlorophyll binding; TAS:TAIR. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003729; F:mRNA binding; IDA:TAIR. DR GO; GO:0009765; P:photosynthesis, light harvesting; IEA:InterPro. DR GO; GO:0009750; P:response to fructose; IEP:TAIR. 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:SF186; CHLOROPHYLL A-B BINDING PROTEIN 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. DR Genevisible; P0CJ48; AT. 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 Reference proteome; Thylakoid; Transit peptide; Transmembrane; KW Transmembrane helix. FT TRANSIT 1..35 FT /note="Chloroplast" FT /evidence="ECO:0000269|PubMed:11113141" FT CHAIN 36..267 FT /note="Chlorophyll a-b binding protein 2, chloroplastic" FT /id="PRO_0000003647" FT TRANSMEM 100..120 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 152..172 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 221..241 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 221..224 FT /note="Interaction with LTD" FT /evidence="ECO:0000269|PubMed:21505433" FT MOTIF 197..200 FT /note="Required for interaction with CAO/cpSRP43" FT BINDING 58 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 80 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 86 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 99 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 102 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 104 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 137 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 147 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 153 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 157 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 165 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 165 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="5" FT /evidence="ECO:0000250|UniProtKB:P07371" FT BINDING 173 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 176 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 183 FT /ligand="chlorophyll b" FT /ligand_id="ChEBI:CHEBI:61721" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 214 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="5" FT /evidence="ECO:0000250" 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:0000250|UniProtKB:P12333" 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:0000250|UniProtKB:P12333" FT BINDING 220 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="1" FT /evidence="ECO:0000250" 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:0000250|UniProtKB:P12333" 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:0000250|UniProtKB:P12333" FT BINDING 256 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="6" FT /evidence="ECO:0000250" FT BINDING 263 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:0000269|PubMed:11113141" FT MOD_RES 38 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:11113141" FT MUTAGEN 197..200 FT /note="DPLG->AAAA: Loss of interaction with CAO/cpSRP43, FT but no effect on interaction with LTD." FT /evidence="ECO:0000269|PubMed:21505433" FT MUTAGEN 199 FT /note="L->K: Loss of targeting to the thylakoid." FT /evidence="ECO:0000269|PubMed:18621669" FT MUTAGEN 210..212 FT /note="ELK->AAA: Loss of interaction with LTD, but no FT effect on interaction with CAO/cpSRP43." FT /evidence="ECO:0000269|PubMed:21505433" FT MUTAGEN 220..223 FT /note="RLAM->AAAA: Loss of interaction with LTD, but no FT effect on interaction with CAO/cpSRP43." FT /evidence="ECO:0000269|PubMed:21505433" SQ SEQUENCE 267 AA; 28227 MW; CEF0664E98F0B0BA CRC64; MAASTMALSS PAFAGKAVNL SPAASEVLGS GRVTMRKTVA KPKGPSGSPW YGSDRVKYLG PFSGESPSYL TGEFPGDYGW DTAGLSADPE TFARNRELEV IHSRWAMLGA LGCVFPELLA RNGVKFGEAV WFKAGSQIFS DGGLDYLGNP SLVHAQSILA IWATQVILMG AVEGYRVAGN GPLGEAEDLL YPGGSFDPLG LATDPEAFAE LKVKELKNGR LAMFSMFGFF VQAIVTGKGP IENLADHLAD PVNNNAWAFA TNFVPGK //