LHSR1_CHLRE
ID LHSR1_CHLRE Reviewed; 253 AA.
AC P93664;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Light-harvesting complex stress-related protein 1, chloroplastic {ECO:0000303|PubMed:19940928};
DE AltName: Full=Chlorophyll a-b binding protein LHCSR1 {ECO:0000305};
DE Flags: Precursor;
GN Name=LHCSR1 {ECO:0000303|PubMed:19940928};
GN Synonyms=LI818 {ECO:0000303|PubMed:8980495};
GN ORFNames=CHLRE_08g365900v5 {ECO:0000312|EMBL:PNW79770.1},
GN CHLREDRAFT_184724 {ECO:0000312|EMBL:EDP01074.1};
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 [MRNA], AND INDUCTION BY LIGHT.
RC STRAIN=CC-620;
RX PubMed=8980495; DOI=10.1007/bf00019098;
RA Savard F., Richard C., Guertin M.;
RT "The Chlamydomonas reinhardtii LI818 gene represents a distant relative of
RT the cabI/II genes that is regulated during the cell cycle and in response
RT to illumination.";
RL Plant Mol. Biol. 32:461-473(1996).
RN [2]
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 [3]
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 [4]
RP SUBCELLULAR LOCATION, AND INDUCTION BY LIGHT.
RX PubMed=10794530; DOI=10.1023/a:1006340308077;
RA Richard C., Ouellet H., Guertin M.;
RT "Characterization of the LI818 polypeptide from the green unicellular alga
RT Chlamydomonas reinhardtii.";
RL Plant Mol. Biol. 42:303-316(2000).
RN [5]
RP INDUCTION BY HIGH LIGHT.
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=27335457; DOI=10.1073/pnas.1605380113;
RA Dinc E., Tian L., Roy L.M., Roth R., Goodenough U., Croce R.;
RT "LHCSR1 induces a fast and reversible pH-dependent fluorescence quenching
RT in LHCII in Chlamydomonas reinhardtii cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7673-7678(2016).
RN [8]
RP FUNCTION.
RX PubMed=29555769; DOI=10.1073/pnas.1720574115;
RA Kosuge K., Tokutsu R., Kim E., Akimoto S., Yokono M., Ueno Y., Minagawa J.;
RT "LHCSR1-dependent fluorescence quenching is mediated by excitation energy
RT transfer from LHCII to photosystem I in Chlamydomonas reinhardtii.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3722-3727(2018).
RN [9]
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:27335457, PubMed:29555769, PubMed:30782831). Is able to
CC sense luminal acidification of the thylakoid membranes, which occurs
CC along with elevated electron flow caused by excess light, and to induce
CC a large, fast, and reversible pH-dependent quenching in LHCII-
CC containing membranes (PubMed:27335457). Mediates excitation energy
CC transfer from light-harvesting complex II (LHCII) to photosystem I
CC (PSI), rather than photosystem II (PSII), at low pH, which mimics the
CC acidified lumen of the thylakoid membranes in high light-exposed
CC chloroplasts (PubMed:29555769, PubMed:30782831). Activates PSI-
CC dependent fluorescence quenching in addition to dissipating excitation
CC energy in LHCII to avoid photooxidative stress under excess light
CC (PubMed:29555769, PubMed:30782831). {ECO:0000269|PubMed:27335457,
CC ECO:0000269|PubMed:29555769, ECO:0000269|PubMed:30782831}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:10794530}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Transiently induced by transition from dark to light (at
CC protein level) (PubMed:8980495, PubMed:10794530). Induced by high light
CC stress (at protein level) (PubMed:19940928, PubMed:24850838).
CC {ECO:0000269|PubMed:10794530, ECO:0000269|PubMed:19940928,
CC ECO:0000269|PubMed:24850838, ECO:0000269|PubMed:8980495}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000255|RuleBase:RU363080}.
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DR EMBL; X95326; CAA64632.1; -; mRNA.
DR EMBL; DS496136; EDP01074.1; -; Genomic_DNA.
DR EMBL; CM008969; PNW79770.1; -; Genomic_DNA.
DR PIR; T08175; T08175.
DR RefSeq; XP_001696125.1; XM_001696073.1.
DR AlphaFoldDB; P93664; -.
DR SMR; P93664; -.
DR STRING; 3055.EDP01074; -.
DR PaxDb; P93664; -.
DR PRIDE; P93664; -.
DR ProMEX; P93664; -.
DR EnsemblPlants; PNW79770; PNW79770; CHLRE_08g365900v5.
DR GeneID; 5721658; -.
DR Gramene; PNW79770; PNW79770; CHLRE_08g365900v5.
DR KEGG; cre:CHLRE_08g365900v5; -.
DR eggNOG; ENOG502RXY6; Eukaryota.
DR HOGENOM; CLU_057943_3_1_1; -.
DR InParanoid; P93664; -.
DR OMA; DYTPGDY; -.
DR OrthoDB; 991539at2759; -.
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: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:0010196; P:nonphotochemical quenching; IMP:UniProtKB.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IBA:GO_Central.
DR GO; GO:0009644; P:response to high light intensity; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..253
FT /note="Light-harvesting complex stress-related protein 1,
FT chloroplastic"
FT /id="PRO_0000447656"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 45
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 60
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 81
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 84
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 86
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 124
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 141
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 144
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 190
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 191
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 194
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 196
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 208
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"
SQ SEQUENCE 253 AA; 27557 MW; 985274D58C5BBF1D CRC64;
MAMMMRKAAA VPASSRRSVA VNSVSGKRTV SGKAGAPVPE DVLAYAKTLP GVTAPFDNVF
DPAGFLATAS VKDVRRWRES EITHGRVAML AALGFIVGEQ LQDFPLFFNF DGRVSGPAIY
HFQQIGQGFW EPLLIAIGVA ESYRVAVGWA TPTGTGFNSL KDDYEPGDLG FDPLGLKPTD
PEELKTLQTK ELNNGRLAMI AIAAFVAQEL VEQTEIFEHL VLRFEKEVIL ELEDVERDLG
LPLTPLPDNL KAI
