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LIL31_ARATH
ID   LIL31_ARATH             Reviewed;         262 AA.
AC   Q9SYX1; O23601; Q8LC02;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Light-harvesting complex-like protein 3 isotype 1, chloroplastic {ECO:0000305};
DE   AltName: Full=LHC-like protein 3 isoform 1 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=LIL3.1; OrderedLocusNames=At4g17600 {ECO:0000312|Araport:AT4G17600};
GN   ORFNames=dl4835w {ECO:0000312|EMBL:CAB10540.1};
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=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [3]
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   [4]
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   [5]
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   [6]
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   [7]
RP   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   [8]
RP   FUNCTION, INTERACTION WITH GGR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   GLU-174; ASN-177 AND ASP-192.
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   [9]
RP   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   [10]
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 (By similarity). Plays a role in the regulation of chlorophyll
CC       biosynthesis under light stress and under standard growth conditions
CC       (PubMed:25808681). {ECO:0000250|UniProtKB:Q6NKS4,
CC       ECO:0000269|PubMed:20823244, ECO:0000269|PubMed:24275650,
CC       ECO:0000269|PubMed:25808681}.
CC   -!- SUBUNIT: Interacts with GGR (PubMed:20823244, PubMed:24275650). Forms
CC       homodimer, and heterodimer with LIL3.2 (PubMed:26320415).
CC       {ECO:0000269|PubMed:20823244, ECO:0000269|PubMed:24275650,
CC       ECO:0000269|PubMed:26320415}.
CC   -!- INTERACTION:
CC       Q9SYX1; Q9CA67: CHLP; NbExp=2; IntAct=EBI-11361535, EBI-2298544;
CC       Q9SYX1; Q9SYX1: LIL3.1; NbExp=2; IntAct=EBI-11361535, EBI-11361535;
CC       Q9SYX1; Q6NKS4: LIL3.2; NbExp=3; IntAct=EBI-11361535, 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: Induced 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=CAB10540.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78763.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF134133; AAD28780.1; -; mRNA.
DR   EMBL; Z97343; CAB10540.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161546; CAB78763.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83919.1; -; Genomic_DNA.
DR   EMBL; AF375427; AAK53011.1; -; mRNA.
DR   EMBL; AY074821; AAL69517.1; -; mRNA.
DR   EMBL; AY136323; AAM96989.1; -; mRNA.
DR   EMBL; BT000402; AAN15721.1; -; mRNA.
DR   EMBL; BT000425; AAN17402.1; -; mRNA.
DR   EMBL; BT002185; AAN72196.1; -; mRNA.
DR   EMBL; AY086891; AAM63936.1; -; mRNA.
DR   PIR; G71445; G71445.
DR   PIR; T52310; T52310.
DR   RefSeq; NP_567532.1; NM_117868.6.
DR   AlphaFoldDB; Q9SYX1; -.
DR   DIP; DIP-59382N; -.
DR   IntAct; Q9SYX1; 2.
DR   MINT; Q9SYX1; -.
DR   STRING; 3702.AT4G17600.1; -.
DR   PaxDb; Q9SYX1; -.
DR   PRIDE; Q9SYX1; -.
DR   ProteomicsDB; 238559; -.
DR   EnsemblPlants; AT4G17600.1; AT4G17600.1; AT4G17600.
DR   GeneID; 827479; -.
DR   Gramene; AT4G17600.1; AT4G17600.1; AT4G17600.
DR   KEGG; ath:AT4G17600; -.
DR   Araport; AT4G17600; -.
DR   TAIR; locus:2129296; AT4G17600.
DR   eggNOG; ENOG502QTY8; Eukaryota.
DR   HOGENOM; CLU_094768_0_0_1; -.
DR   InParanoid; Q9SYX1; -.
DR   OMA; AAMMGYV; -.
DR   OrthoDB; 1336763at2759; -.
DR   PhylomeDB; Q9SYX1; -.
DR   PRO; PR:Q9SYX1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SYX1; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA: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: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:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
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.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS: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..39
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..262
FT                   /note="Light-harvesting complex-like protein 3 isotype 1,
FT                   chloroplastic"
FT                   /id="PRO_0000437944"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         174
FT                   /note="E->A: Decreases interaction with GGR; when
FT                   associated with A-177 and A-192."
FT                   /evidence="ECO:0000269|PubMed:24275650"
FT   MUTAGEN         177
FT                   /note="N->A: Decreases interaction with GGR; when
FT                   associated with A-174 and A-192."
FT                   /evidence="ECO:0000269|PubMed:24275650"
FT   MUTAGEN         192
FT                   /note="D->A: Decreases interaction with GGR; when
FT                   associated with A-174 and A-177."
FT                   /evidence="ECO:0000269|PubMed:24275650"
FT   CONFLICT        100
FT                   /note="V -> I (in Ref. 6; AAM63936)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   262 AA;  29403 MW;  DA1EA332802CCCDD CRC64;
     MALFSPPISS SSLQNPNFIP KFSFSLLSSN RFSLLSVTRA SSDSGSTSPT AAVSVEAPEP
     VEVIVKEPPQ STPAVKKEET ATAKNVAVEG EEMKTTESVV KFQDARWING TWDLKQFEKD
     GKTDWDSVIV AEAKRRKWLE ENPETTSNDE PVLFDTSIIP WWAWIKRYHL PEAELLNGRA
     AMIGFFMAYF VDSLTGVGLV DQMGNFFCKT LLFVAVAGVL FIRKNEDVDK LKNLFDETTL
     YDKQWQAAWK NDDDESLGSK KK
 
 
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