CB1C_ARATH
ID CB1C_ARATH Reviewed; 267 AA.
AC P04778; P83754;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Chlorophyll a-b binding protein 1, chloroplastic;
DE AltName: Full=Chlorophyll a-b protein 140;
DE Short=CAB-140;
DE AltName: Full=LHCII type I CAB-1;
DE Flags: Precursor;
GN Name=LHCB1.3; Synonyms=AB140, CAB1; OrderedLocusNames=At1g29930;
GN ORFNames=F1N18.3;
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].
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 [GENOMIC DNA] OF 1-15.
RA Mitra A., Choi H.K., An G.;
RT "Structural and functional analyses of Arabidopsis thaliana chlorophyll
RT a/b-binding protein (cab) promoters.";
RL Plant Mol. Biol. 12:169-179(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-267.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [7]
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).
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 -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; X03909; CAA27543.1; -; Genomic_DNA.
DR EMBL; AC008030; AAG10603.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31151.1; -; Genomic_DNA.
DR EMBL; AF428359; AAL16289.1; -; mRNA.
DR EMBL; AY045673; AAK74031.1; -; mRNA.
DR EMBL; AY050935; AAK93612.1; -; mRNA.
DR EMBL; AY058180; AAL25594.1; -; mRNA.
DR EMBL; AY091169; AAM14108.1; -; mRNA.
DR EMBL; X15221; CAA33290.1; -; Genomic_DNA.
DR EMBL; X15222; CAA33291.1; -; Genomic_DNA.
DR EMBL; Z17799; CAA79075.1; -; mRNA.
DR PIR; A86423; A86423.
DR RefSeq; NP_174286.1; NM_102733.3.
DR PDB; 5MDX; EM; 5.30 A; 1/2/3/5/6/7/G/N/Y/g/n/y=44-267.
DR PDB; 7OUI; EM; 2.79 A; G/N/Y/g/n/y=36-267.
DR PDBsum; 5MDX; -.
DR PDBsum; 7OUI; -.
DR AlphaFoldDB; P04778; -.
DR SMR; P04778; -.
DR BioGRID; 25106; 10.
DR IntAct; P04778; 21.
DR STRING; 3702.AT1G29930.1; -.
DR iPTMnet; P04778; -.
DR PaxDb; P04778; -.
DR PRIDE; P04778; -.
DR ProteomicsDB; 239126; -.
DR EnsemblPlants; AT1G29930.1; AT1G29930.1; AT1G29930.
DR GeneID; 839871; -.
DR Gramene; AT1G29930.1; AT1G29930.1; AT1G29930.
DR KEGG; ath:AT1G29930; -.
DR Araport; AT1G29930; -.
DR TAIR; locus:2019322; AT1G29930.
DR eggNOG; ENOG502QPU1; Eukaryota.
DR HOGENOM; CLU_057943_2_0_1; -.
DR InParanoid; P04778; -.
DR OMA; FWINSAS; -.
DR OrthoDB; 961261at2759; -.
DR PhylomeDB; P04778; -.
DR PRO; PR:P04778; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P04778; baseline and differential.
DR Genevisible; P04778; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; 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:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IBA:GO_Central.
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 1, chloroplastic"
FT /id="PRO_0000003648"
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 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 TURN 60..62
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 89..122
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 158..178
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 205..235
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:7OUI"
SQ SEQUENCE 267 AA; 28241 MW; CFA1664E9A80B0BA CRC64;
MAASTMALSS PAFAGKAVKL 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
