CB1A_ARATH
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 03-AUG-2022, entry version 74.
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; OrderedLocusNames=At1g29920;
GN 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}.
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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 PDBsum; 4YZH; -.
DR AlphaFoldDB; P0CJ48; -.
DR SMR; P0CJ48; -.
DR BioGRID; 25104; 19.
DR BioGRID; 25105; 14.
DR IntAct; P0CJ48; 1.
DR STRING; 3702.AT1G29910.1; -.
DR TCDB; 3.E.2.2.3; the photosynthetic reaction center (prc) family.
DR iPTMnet; P0CJ48; -.
DR PaxDb; P0CJ48; -.
DR PRIDE; P0CJ48; -.
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; locus:2019372; AT1G29920.
DR eggNOG; ENOG502QPU1; Eukaryota.
DR HOGENOM; CLU_057943_2_0_1; -.
DR InParanoid; P0CJ48; -.
DR OMA; WAYATQF; -.
DR OrthoDB; 961261at2759; -.
DR PhylomeDB; P0CJ48; -.
DR PRO; PR:P0CJ48; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0CJ48; baseline and differential.
DR Genevisible; P0CJ48; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0009768; P:photosynthesis, light harvesting in photosystem I; IBA:GO_Central.
DR GO; GO:0009750; P:response to fructose; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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 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
