LHR32_CHLRE
ID LHR32_CHLRE Reviewed; 259 AA.
AC P0DO18; A8J431;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Light-harvesting complex stress-related protein 3.2, chloroplastic {ECO:0000303|PubMed:19940928};
DE AltName: Full=Chlorophyll a-b binding protein LHCSR3.2 {ECO:0000305};
DE Flags: Precursor;
GN Name=LHCSR3.2 {ECO:0000303|PubMed:19940928};
GN Synonyms=LHCSR2 {ECO:0000303|PubMed:15470261},
GN LHCSR3 {ECO:0000303|PubMed:21267060};
GN ORFNames=CHLRE_08g367400v5 {ECO:0000312|EMBL:PNW79806.1},
GN CHLREDRAFT_184730 {ECO:0000312|EMBL:EDP01087.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=CC-503;
RG Chlamydomonas Annotation Team;
RG JGI Annotation Team;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Grigoriev I.V., Rokhsar D.S.;
RT "WGS assembly of Chlamydomonas reinhardtii.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION BY SULFUR DEPRIVATION.
RX PubMed=15470261; DOI=10.1128/ec.3.5.1331-1348.2004;
RA Zhang Z., Shrager J., Jain M., Chang C.W., Vallon O., Grossman A.R.;
RT "Insights into the survival of Chlamydomonas reinhardtii during sulfur
RT starvation based on microarray analysis of gene expression.";
RL Eukaryot. Cell 3:1331-1348(2004).
RN [4]
RP FUNCTION, INDUCTION BY HIGH LIGHT, AND DISRUPTION PHENOTYPE.
RX PubMed=19940928; DOI=10.1038/nature08587;
RA Peers G., Truong T.B., Ostendorf E., Busch A., Elrad D., Grossman A.R.,
RA Hippler M., Niyogi K.K.;
RT "An ancient light-harvesting protein is critical for the regulation of
RT algal photosynthesis.";
RL Nature 462:518-521(2009).
RN [5]
RP FUNCTION, AND INDUCTION BY HIGH LIGHT.
RX PubMed=21267060; DOI=10.1371/journal.pbio.1000577;
RA Bonente G., Ballottari M., Truong T.B., Morosinotto T., Ahn T.K.,
RA Fleming G.R., Niyogi K.K., Bassi R.;
RT "Analysis of LhcSR3, a protein essential for feedback de-excitation in the
RT green alga Chlamydomonas reinhardtii.";
RL PLoS Biol. 9:E1000577-E1000577(2011).
RN [6]
RP FUNCTION.
RX PubMed=23716695; DOI=10.1073/pnas.1222606110;
RA Tokutsu R., Minagawa J.;
RT "Energy-dissipative supercomplex of photosystem II associated with LHCSR3
RT in Chlamydomonas reinhardtii.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10016-10021(2013).
RN [7]
RP INDUCTION BY HIGH LIGHT.
RX PubMed=24850838; DOI=10.1093/pcp/pcu068;
RA Maruyama S., Tokutsu R., Minagawa J.;
RT "Transcriptional regulation of the stress-responsive light harvesting
RT complex genes in Chlamydomonas reinhardtii.";
RL Plant Cell Physiol. 55:1304-1310(2014).
RN [8]
RP INTERACTION WITH PSII-LHCII SUPERCOMPLEX.
RX PubMed=25699588; DOI=10.1104/pp.15.00094;
RA Xue H., Tokutsu R., Bergner S.V., Scholz M., Minagawa J., Hippler M.;
RT "PHOTOSYSTEM II SUBUNIT R is required for efficient binding of LIGHT-
RT HARVESTING COMPLEX STRESS-RELATED PROTEIN3 to photosystem II-light-
RT harvesting supercomplexes in Chlamydomonas reinhardtii.";
RL Plant Physiol. 167:1566-1578(2015).
RN [9]
RP FUNCTION.
RX PubMed=27150505; DOI=10.1016/j.bbabio.2016.04.285;
RA Liguori N., Novoderezhkin V., Roy L.M., van Grondelle R., Croce R.;
RT "Excitation dynamics and structural implication of the stress-related
RT complex LHCSR3 from the green alga Chlamydomonas reinhardtii.";
RL Biochim. Biophys. Acta 1857:1514-1523(2016).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ASP-117; GLU-221 AND GLU-224.
RX PubMed=26817847; DOI=10.1074/jbc.m115.704601;
RA Ballottari M., Truong T.B., De Re E., Erickson E., Stella G.R.,
RA Fleming G.R., Bassi R., Niyogi K.K.;
RT "Identification of pH-sensing sites in the light harvesting complex stress-
RT related 3 protein essential for triggering non-photochemical quenching in
RT Chlamydomonas reinhardtii.";
RL J. Biol. Chem. 291:7334-7346(2016).
RN [11]
RP INDUCTION BY HIGH LIGHT.
RX PubMed=27358399; DOI=10.1074/jbc.m116.737312;
RA Correa-Galvis V., Redekop P., Guan K., Griess A., Truong T.B., Wakao S.,
RA Niyogi K.K., Jahns P.;
RT "Photosystem II subunit PsbS is involved in the induction of LHCSR protein-
RT dependent energy dissipation in Chlamydomonas reinhardtii.";
RL J. Biol. Chem. 291:17478-17487(2016).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27626383; DOI=10.1038/nature19358;
RA Petroutsos D., Tokutsu R., Maruyama S., Flori S., Greiner A., Magneschi L.,
RA Cusant L., Kottke T., Mittag M., Hegemann P., Finazzi G., Minagawa J.;
RT "A blue-light photoreceptor mediates the feedback regulation of
RT photosynthesis.";
RL Nature 537:563-566(2016).
RN [13]
RP INTERACTION WITH PSII-LHCII SUPERCOMPLEX.
RX PubMed=28257778; DOI=10.1016/j.bbabio.2017.02.015;
RA Semchonok D.A., Sathish Yadav K.N., Xu P., Drop B., Croce R., Boekema E.J.;
RT "Interaction between the photoprotective protein LHCSR3 and C2S2
RT photosystem II supercomplex in Chlamydomonas reinhardtii.";
RL Biochim. Biophys. Acta 1858:379-385(2017).
RN [14]
RP INTERACTION WITH PSII-LHCII SUPERCOMPLEX.
RX PubMed=28972177; DOI=10.1074/jbc.m117.805192;
RA Kim E., Akimoto S., Tokutsu R., Yokono M., Minagawa J.;
RT "Fluorescence lifetime analyses reveal how the high light-responsive
RT protein LHCSR3 transforms PSII light-harvesting complexes into an energy-
RT dissipative state.";
RL J. Biol. Chem. 292:18951-18960(2017).
RN [15]
RP FUNCTION, INDUCTION BY HIGH LIGHT, AND DISRUPTION PHENOTYPE.
RX PubMed=27693674; DOI=10.1016/j.molp.2016.09.005;
RA Chaux F., Johnson X., Auroy P., Beyly-Adriano A., Te I., Cuine S.,
RA Peltier G.;
RT "PGRL1 and LHCSR3 compensate for each other in controlling photosynthesis
RT and avoiding photosystem I photoinhibition during high light acclimation of
RT Chlamydomonas cells.";
RL Mol. Plant 10:216-218(2017).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28233792; DOI=10.1038/srep43145;
RA Roach T., Na C.S.;
RT "LHCSR3 affects de-coupling and re-coupling of LHCII to PSII during state
RT transitions in Chlamydomonas reinhardtii.";
RL Sci. Rep. 7:43145-43145(2017).
RN [17]
RP FUNCTION.
RX PubMed=31042040; DOI=10.1021/acs.jpclett.9b01184;
RA de la Cruz Valbuena G., Camargo F.V., Borrego-Varillas R., Perozeni F.,
RA D'Andrea C., Ballottari M., Cerullo G.;
RT "Molecular mechanisms of nonphotochemical quenching in the LHCSR3 protein
RT of Chlamydomonas reinhardtii.";
RL J. Phys. Chem. Lett. 10:2500-2505(2019).
RN [18]
RP FUNCTION.
RX PubMed=30782831; DOI=10.1073/pnas.1809812116;
RA Girolomoni L., Cazzaniga S., Pinnola A., Perozeni F., Ballottari M.,
RA Bassi R.;
RT "LHCSR3 is a nonphotochemical quencher of both photosystems in
RT Chlamydomonas reinhardtii.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:4212-4217(2019).
CC -!- FUNCTION: Required for non-photochemical quenching (NPQ), a mechanism
CC that converts and dissipates the harmful excess absorbed light energy
CC into heat and protect the photosynthetic apparatus from photo-oxidative
CC damage (PubMed:19940928, PubMed:21267060, PubMed:23716695,
CC PubMed:26817847, PubMed:27626383, PubMed:27693674, PubMed:28233792,
CC PubMed:31042040, PubMed:30782831). NPQ includes dissipating excess
CC light energy to heat (qE) and the reversible coupling of LHCII to
CC photosystems (state transitions or qT), which are considered separate
CC NPQ mechanisms (PubMed:28233792). Is responsible for most of the excess
CC light energy to heat dissipation (qE), also known as energy-dependent
CC chlorophyll fluorescence quenching activity of chlorophyll excited
CC states (PubMed:21267060, PubMed:28233792). Involved in a de-coupling
CC and re-coupling of energy transfer to photosystem II (PSII) during qT
CC (PubMed:28233792). Binds chlorophyll a and b (PubMed:21267060,
CC PubMed:27150505). Is able to sense luminal acidification of the
CC thylakoid membranes, which occurs along with elevated electron flow
CC caused by excess light (PubMed:21267060, PubMed:26817847,
CC PubMed:31042040). Establishes interactions with photosystem II (PSII)
CC antenna components upon lumen acidification, and protonation of lumen-
CC exposed, negatively charged residues both in LHCSR3 and in PSII antenna
CC components (PubMed:26817847). Mediates excitation energy transfer from
CC light-harvesting complex II (LHCII) to photosystem I (PSI), rather than
CC photosystem II (PSII), at low pH, which mimics the acidified lumen of
CC the thylakoid membranes in high light-exposed chloroplasts
CC (PubMed:30782831). Activates PSI-dependent fluorescence quenching in
CC addition to dissipating excitation energy in LHCII to avoid
CC photooxidative stress under excess light (PubMed:30782831). Contributes
CC with PGRL1 to the regulation of electron flow upstream of photosystem I
CC (PSI), and limits the accumulation of electrons on the PSI acceptor
CC side, thus avoiding PSI photoinhibition (PubMed:27693674).
CC {ECO:0000269|PubMed:19940928, ECO:0000269|PubMed:21267060,
CC ECO:0000269|PubMed:23716695, ECO:0000269|PubMed:26817847,
CC ECO:0000269|PubMed:27150505, ECO:0000269|PubMed:27626383,
CC ECO:0000269|PubMed:27693674, ECO:0000269|PubMed:28233792,
CC ECO:0000269|PubMed:30782831, ECO:0000269|PubMed:31042040}.
CC -!- SUBUNIT: Interacts with the photosystem II-light-harvesting complex II
CC (PSII-LHCII) supercomplex to form PSII-LHCII-LHCSR3 supercomplex.
CC {ECO:0000269|PubMed:25699588, ECO:0000269|PubMed:28257778,
CC ECO:0000269|PubMed:28972177}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced by sulfur deprivation (PubMed:15470261). Induced by
CC high light stress (at protein level) (PubMed:19940928, PubMed:21267060,
CC PubMed:24850838, PubMed:27358399, PubMed:27693674).
CC {ECO:0000269|PubMed:15470261, ECO:0000269|PubMed:19940928,
CC ECO:0000269|PubMed:21267060, ECO:0000269|PubMed:24850838,
CC ECO:0000269|PubMed:27358399, ECO:0000269|PubMed:27693674}.
CC -!- DISRUPTION PHENOTYPE: Impaired in non-photochemical quenching (NPQ)
CC under high light conditions. {ECO:0000269|PubMed:19940928,
CC ECO:0000269|PubMed:27626383, ECO:0000269|PubMed:27693674,
CC ECO:0000269|PubMed:28233792}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; DS496136; EDP01087.1; -; Genomic_DNA.
DR EMBL; CM008969; PNW79806.1; -; Genomic_DNA.
DR RefSeq; XP_001696064.1; XM_001696012.1.
DR RefSeq; XP_001696138.1; XM_001696086.1.
DR AlphaFoldDB; P0DO18; -.
DR ProMEX; P0DO18; -.
DR EnsemblPlants; PNW79806; PNW79806; CHLRE_08g367400v5.
DR EnsemblPlants; PNW79807; PNW79807; CHLRE_08g367500v5.
DR GeneID; 5721688; -.
DR GeneID; 5721689; -.
DR Gramene; PNW79806; PNW79806; CHLRE_08g367400v5.
DR Gramene; PNW79807; PNW79807; CHLRE_08g367500v5.
DR KEGG; cre:CHLRE_08g367500v5; -.
DR OMA; WEPLIFA; -.
DR Proteomes; UP000006906; Chromosome 8.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010196; P:nonphotochemical quenching; IMP:UniProtKB.
DR GO; GO:0009765; P:photosynthesis, light harvesting; IEA:InterPro.
DR GO; GO:0009644; P:response to high light intensity; IMP:UniProtKB.
DR GO; GO:0080183; P:response to photooxidative stress; IMP:UniProtKB.
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 Chlorophyll; Chloroplast; Chromophore; Magnesium; Membrane; Metal-binding;
KW Photosynthesis; Photosystem I; Photosystem II; Plastid; Reference proteome;
KW Stress response; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..259
FT /note="Light-harvesting complex stress-related protein 3.2,
FT chloroplastic"
FT /id="PRO_0000447655"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 51
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 66
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 87
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 90
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 92
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 130
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 147
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 150
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 196
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 197
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 200
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 202
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 214
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 MUTAGEN 117
FT /note="D->N: Impaired in non-photochemical quenching (NPQ)
FT under high light conditions; when associated with Q-221 and
FT Q-224."
FT /evidence="ECO:0000269|PubMed:26817847"
FT MUTAGEN 221
FT /note="E->Q: Impaired in non-photochemical quenching (NPQ)
FT under high light conditions; when associated with N-117 and
FT Q-224."
FT /evidence="ECO:0000269|PubMed:26817847"
FT MUTAGEN 224
FT /note="E->Q: Impaired in non-photochemical quenching (NPQ)
FT under high light conditions; when associated with N-117 and
FT Q-221."
FT /evidence="ECO:0000269|PubMed:26817847"
SQ SEQUENCE 259 AA; 28224 MW; 92E52D0F1A95157C CRC64;
MLANVVSRKA SGLRQTPARA TVAVKSVSGR RTTAAEPQTA APVAAEDVFA YTKNLPGVTA
PFEGVFDPAG FLATASIKDV RRWRESEITH GRVAMLAALG FVVGEQLQDF PLFFNWDGRV
SGPAIYHFQQ IGQGFWEPLL IAIGVAESYR VAVGWATPTG TGFNSLKDDY EPGDLGFDPL
GLKPTDPEEL KVMQTKELNN GRLAMIAIAA FVAQELVEQT EIFEHLALRF EKEAILELDD
IERDLGLPVT PLPDNLKSL
