LIL32_ARATH
ID LIL32_ARATH Reviewed; 258 AA.
AC Q6NKS4; Q9LTB7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Light-harvesting complex-like protein 3 isotype 2, chloroplastic {ECO:0000305};
DE AltName: Full=LHC-like protein 3 isoform 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=LIL3.2; OrderedLocusNames=At5g47110 {ECO:0000312|Araport:AT5G47110};
GN ORFNames=K14A3.6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, INTERACTION WITH GGR, AND DISRUPTION PHENOTYPE.
RX PubMed=20823244; DOI=10.1073/pnas.1004699107;
RA Tanaka R., Rothbart M., Oka S., Takabayashi A., Takahashi K., Shibata M.,
RA Myouga F., Motohashi R., Shinozaki K., Grimm B., Tanaka A.;
RT "LIL3, a light-harvesting-like protein, plays an essential role in
RT chlorophyll and tocopherol biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16721-16725(2010).
RN [5]
RP FUNCTION, INTERACTION WITH GGR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-171; ASN-174 AND ASP-189.
RX PubMed=24275650; DOI=10.1074/jbc.m113.525428;
RA Takahashi K., Takabayashi A., Tanaka A., Tanaka R.;
RT "Functional analysis of light-harvesting-like protein 3 (LIL3) and its
RT light-harvesting chlorophyll-binding motif in Arabidopsis.";
RL J. Biol. Chem. 289:987-999(2014).
RN [6]
RP FUNCTION, INTERACTION WITH LIL3.1 AND LIL3.2, AND SUBCELLULAR LOCATION.
RX PubMed=26320415; DOI=10.1016/j.febslet.2015.08.023;
RA Mork-Jansson A.E., Gargano D., Kmiec K., Furnes C., Shevela D.,
RA Eichacker L.A.;
RT "Lil3 dimerization and chlorophyll binding in Arabidopsis thaliana.";
RL FEBS Lett. 589:3064-3070(2015).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25808681; DOI=10.1111/pce.12540;
RA Lohscheider J.N., Rojas-Stuetz M.C., Rothbart M., Andersson U., Funck D.,
RA Mendgen K., Grimm B., Adamska I.;
RT "Altered levels of LIL3 isoforms in Arabidopsis lead to disturbed pigment-
RT protein assembly and chlorophyll synthesis, chlorotic phenotype and
RT impaired photosynthetic performance.";
RL Plant Cell Environ. 38:2115-2127(2015).
CC -!- FUNCTION: Light-harvesting-like protein required for biosynthesis of
CC phytylated chlorophylls and alpha-tocopherol in green seedlings.
CC Functions by anchoring geranylgeranyl reductase (GGR) in the thylakoid
CC membrane, leading to the stabilization of GGR activity
CC (PubMed:20823244, PubMed:24275650). Binds chlrophyll a in the thylakoid
CC membrane (PubMed:26320415). Plays a role in the regulation of
CC chlorophyll biosynthesis under light stress and under standard growth
CC conditions (PubMed:25808681). {ECO:0000269|PubMed:20823244,
CC ECO:0000269|PubMed:24275650, ECO:0000269|PubMed:25808681,
CC ECO:0000269|PubMed:26320415}.
CC -!- SUBUNIT: Interacts with GGR (PubMed:20823244, PubMed:24275650). Forms
CC homodimer and heterodimer with LIL3.1 (PubMed:26320415).
CC {ECO:0000269|PubMed:20823244, ECO:0000269|PubMed:24275650,
CC ECO:0000269|PubMed:26320415}.
CC -!- INTERACTION:
CC Q6NKS4; Q9CA67: CHLP; NbExp=2; IntAct=EBI-11361548, EBI-2298544;
CC Q6NKS4; Q9SYX1: LIL3.1; NbExp=3; IntAct=EBI-11361548, EBI-11361535;
CC Q6NKS4; Q6NKS4: LIL3.2; NbExp=3; IntAct=EBI-11361548, EBI-11361548;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:24275650, ECO:0000269|PubMed:25808681,
CC ECO:0000269|PubMed:26320415}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Associates with subcomplexes of LHC antenna of
CC photosystem II. {ECO:0000269|PubMed:25808681}.
CC -!- TISSUE SPECIFICITY: Expressed in photosynthetically active tissues (at
CC protein level). {ECO:0000269|PubMed:25808681}.
CC -!- INDUCTION: Down-regulated by light. {ECO:0000269|PubMed:25808681}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutant plants lli3:1 and lli3:2 are dwarf
CC with yellowish green leaves. {ECO:0000269|PubMed:20823244}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA98106.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB025609; BAA98106.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED95472.1; -; Genomic_DNA.
DR EMBL; BT010859; AAR24226.1; -; mRNA.
DR EMBL; BT012619; AAT06438.1; -; mRNA.
DR RefSeq; NP_199522.2; NM_124082.5.
DR AlphaFoldDB; Q6NKS4; -.
DR DIP; DIP-59383N; -.
DR IntAct; Q6NKS4; 2.
DR MINT; Q6NKS4; -.
DR STRING; 3702.AT5G47110.1; -.
DR PaxDb; Q6NKS4; -.
DR PRIDE; Q6NKS4; -.
DR ProteomicsDB; 238495; -.
DR EnsemblPlants; AT5G47110.1; AT5G47110.1; AT5G47110.
DR GeneID; 834757; -.
DR Gramene; AT5G47110.1; AT5G47110.1; AT5G47110.
DR KEGG; ath:AT5G47110; -.
DR Araport; AT5G47110; -.
DR TAIR; locus:2151972; AT5G47110.
DR eggNOG; ENOG502QTY8; Eukaryota.
DR HOGENOM; CLU_094768_0_0_1; -.
DR InParanoid; Q6NKS4; -.
DR OMA; HHSTHKP; -.
DR OrthoDB; 1336763at2759; -.
DR PhylomeDB; Q6NKS4; -.
DR PRO; PR:Q6NKS4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NKS4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009503; C:thylakoid light-harvesting complex; IDA:TAIR.
DR GO; GO:0042651; C:thylakoid membrane; IDA:TAIR.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IDA:TAIR.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:1902326; P:positive regulation of chlorophyll biosynthetic process; IGI:TAIR.
DR GO; GO:1904964; P:positive regulation of phytol biosynthetic process; IDA:TAIR.
DR GO; GO:1904966; P:positive regulation of vitamin E biosynthetic process; IGI:TAIR.
PE 1: Evidence at protein level;
KW Chlorophyll; Chloroplast; Chromophore; Membrane; Photosynthesis;
KW Photosystem II; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..258
FT /note="Light-harvesting complex-like protein 3 isotype 2,
FT chloroplastic"
FT /id="PRO_0000437945"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 66..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 171
FT /note="E->A: Decreases interaction with GGR; when
FT associated with A-174 and A-189."
FT /evidence="ECO:0000269|PubMed:24275650"
FT MUTAGEN 174
FT /note="N->A: Decreases interaction with GGR; when
FT associated with A-171 and A-189."
FT /evidence="ECO:0000269|PubMed:24275650"
FT MUTAGEN 189
FT /note="D->A: Decreases interaction with GGR; when
FT associated with A-171 and A-174."
FT /evidence="ECO:0000269|PubMed:24275650"
SQ SEQUENCE 258 AA; 28601 MW; 372F5DFC5FF508D8 CRC64;
MSISMALFSP PISSSLQNPN LIPKISTSLL STKRFSLISV PRASSDNGTT SPVVEIPKPA
SVAVEEVPVK SPAESSSASE NGAVGGEATD SSTETVIKYQ NAKWVNGTWD LKQFEKDGKT
DWDSVIVSEA KRRKWLEDNP ETTSNDELVV FDTSIIPWWA WMKRYHLPEA ELLNGRAAMI
GFFMAYFVDS LTGVGLVDQM GNFFCKTLLF VAVAGVLFIR KNEDLDKLKD LFDETTLYDK
QWQAAWKEPD SSTVSSKK
