CB5_ARATH
ID CB5_ARATH Reviewed; 280 AA.
AC Q9XF89; Q8LAB1;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Chlorophyll a-b binding protein CP26, chloroplastic;
DE AltName: Full=LHCB5;
DE AltName: Full=LHCIIc;
DE AltName: Full=Light-harvesting complex II protein 5;
DE Flags: Precursor;
GN Name=LHCB5; OrderedLocusNames=At4g10340; ORFNames=F24G24.140;
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 [MRNA].
RX PubMed=10366881; DOI=10.1016/s1360-1385(99)01419-3;
RA Jansson S.;
RT "A guide to the Lhc genes and their relatives in Arabidopsis.";
RL Trends Plant Sci. 4:236-240(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 SUBUNIT, INTERACTION WITH LHCB3, AND SUBCELLULAR LOCATION.
RX PubMed=16551629; DOI=10.1074/jbc.m511415200;
RA Ruban A.V., Solovieva S., Lee P.J., Ilioaia C., Wentworth M., Ganeteg U.,
RA Klimmek F., Chow W.S., Anderson J.M., Jansson S., Horton P.;
RT "Plasticity in the composition of the light harvesting antenna of higher
RT plants preserves structural integrity and biological function.";
RL J. Biol. Chem. 281:14981-14990(2006).
RN [7]
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).
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: Forms heterotrimers with LHCB3 (PubMed:16551629). The LHC
CC complex consists of chlorophyll a-b binding proteins.
CC {ECO:0000269|PubMed:16551629}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:16551629}; Multi-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}.
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; AF134129; AAD28776.1; -; mRNA.
DR EMBL; AL049488; CAB39787.1; -; Genomic_DNA.
DR EMBL; AL161517; CAB78157.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82869.1; -; Genomic_DNA.
DR EMBL; AF326900; AAG41482.1; -; mRNA.
DR EMBL; AF339718; AAK00400.1; -; mRNA.
DR EMBL; AF424597; AAL11591.1; -; mRNA.
DR EMBL; AF380631; AAK55712.1; -; mRNA.
DR EMBL; AY054126; AAL06787.1; -; mRNA.
DR EMBL; AY087939; AAM65487.1; -; mRNA.
DR PIR; T04049; T04049.
DR RefSeq; NP_192772.1; NM_117102.4.
DR PDB; 5MDX; EM; 5.30 A; S/s=49-280.
DR PDB; 7OUI; EM; 2.79 A; S/s=49-280.
DR PDBsum; 5MDX; -.
DR PDBsum; 7OUI; -.
DR AlphaFoldDB; Q9XF89; -.
DR SMR; Q9XF89; -.
DR BioGRID; 11925; 23.
DR DIP; DIP-59004N; -.
DR IntAct; Q9XF89; 2.
DR STRING; 3702.AT4G10340.1; -.
DR TCDB; 3.E.2.2.3; the photosynthetic reaction center (prc) family.
DR iPTMnet; Q9XF89; -.
DR PaxDb; Q9XF89; -.
DR PRIDE; Q9XF89; -.
DR ProteomicsDB; 223913; -.
DR EnsemblPlants; AT4G10340.1; AT4G10340.1; AT4G10340.
DR GeneID; 826626; -.
DR Gramene; AT4G10340.1; AT4G10340.1; AT4G10340.
DR KEGG; ath:AT4G10340; -.
DR Araport; AT4G10340; -.
DR TAIR; locus:2122794; AT4G10340.
DR eggNOG; ENOG502QV5A; Eukaryota.
DR HOGENOM; CLU_057943_2_2_1; -.
DR InParanoid; Q9XF89; -.
DR OMA; KFGASCG; -.
DR OrthoDB; 1228199at2759; -.
DR PhylomeDB; Q9XF89; -.
DR PRO; PR:Q9XF89; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9XF89; baseline and differential.
DR Genevisible; Q9XF89; 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:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0009783; C:photosystem II antenna complex; IMP:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0009517; C:PSII associated light-harvesting complex II; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0042651; C:thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
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:0010196; P:nonphotochemical quenching; IMP:TAIR.
DR GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IBA:GO_Central.
DR GO; GO:0010207; P:photosystem II assembly; IMP: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; Chlorophyll; Chloroplast; Chromophore; Magnesium; Membrane;
KW Metal-binding; Phosphoprotein; Photosynthesis; Photosystem I;
KW Photosystem II; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 49..280
FT /note="Chlorophyll a-b binding protein CP26, chloroplastic"
FT /id="PRO_0000003650"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 70
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"
FT BINDING 95
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 114
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"
FT BINDING 117
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"
FT BINDING 119
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
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"
FT BINDING 186
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"
FT BINDING 189
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 225
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"
FT BINDING 228
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"
FT BINDING 230
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 242
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"
FT BINDING 257
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"
FT CONFLICT 185
FT /note="A -> S (in Ref. 5; AAM65487)"
FT /evidence="ECO:0000305"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 104..137
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 171..191
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 215..245
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:7OUI"
SQ SEQUENCE 280 AA; 30157 MW; F7BD5C07C9836D10 CRC64;
MASLGVSEML GTPLNFRAVS RSSAPLASSP STFKTVALFS KKKPAPAKSK AVSETSDELA
KWYGPDRRIF LPDGLLDRSE IPEYLNGEVA GDYGYDPFGL GKKPENFAKY QAFELIHARW
AMLGAAGFII PEALNKYGAN CGPEAVWFKT GALLLDGNTL NYFGKNIPIN LVLAVVAEVV
LLGGAEYYRI TNGLDFEDKL HPGGPFDPLG LAKDPEQGAL LKVKEIKNGR LAMFAMLGFF
IQAYVTGEGP VENLAKHLSD PFGNNLLTVI AGTAERAPTL
