LST81_ARATH
ID LST81_ARATH Reviewed; 305 AA.
AC Q9LV27; B9DFE0;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Target of rapamycin complex subunit LST8-1 {ECO:0000305};
DE Short=TORC subunit LST8 homolog 1 {ECO:0000305};
DE AltName: Full=Lethal with SEC13 protein 8 homolog 1 {ECO:0000305};
GN Name=LST8-1 {ECO:0000303|PubMed:22307851};
GN OrderedLocusNames=At3g18140 {ECO:0000312|Araport:AT3G18140};
GN ORFNames=MRC8.12 {ECO:0000312|EMBL:BAB02026.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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 FUNCTION, SUBUNIT, INTERACTION WITH TOR, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22307851; DOI=10.1105/tpc.111.091306;
RA Moreau M., Azzopardi M., Clement G., Dobrenel T., Marchive C., Renne C.,
RA Martin-Magniette M.-L., Taconnat L., Renou J.-P., Robaglia C., Meyer C.;
RT "Mutations in the Arabidopsis homolog of LST8/GbetaL, a partner of the
RT target of Rapamycin kinase, impair plant growth, flowering, and metabolic
RT adaptation to long days.";
RL Plant Cell 24:463-481(2012).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26459592; DOI=10.1016/j.bbrc.2015.10.028;
RA Kravchenko A., Citerne S., Jehanno I., Bersimbaev R.I., Veit B., Meyer C.,
RA Leprince A.S.;
RT "Mutations in the Arabidopsis Lst8 and Raptor genes encoding partners of
RT the TOR complex, or inhibition of TOR activity decrease abscisic acid (ABA)
RT synthesis.";
RL Biochem. Biophys. Res. Commun. 467:992-997(2015).
CC -!- FUNCTION: Component of TORC1 complex, which is an essential cell growth
CC regulator that controls plant development. Acts by activating
CC transcription, protein synthesis and ribosome biogenesis, and
CC inhibiting mRNA degradation and autophagy (Probable). Involved in
CC regulating amino acid accumulation and the synthesis of myo-inositol
CC and raffinose during plant adaptation to long days (PubMed:22307851).
CC Involved in the regulation of plant growth and abscisic acid (ABA)
CC accumulation. Acts as positive regulation of the ABA biosynthetic genes
CC ZEP, NCED3 and AAO3, and negative regulator of the ABA catabolic genes
CC CYP707A2 and CYP707A3 (PubMed:26459592). {ECO:0000269|PubMed:22307851,
CC ECO:0000269|PubMed:26459592, ECO:0000305|PubMed:22307851,
CC ECO:0000305|PubMed:26459592}.
CC -!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of at
CC least RAPTOR, LST8 and TOR (Probable). Interacts with TOR
CC (PubMed:22307851). {ECO:0000269|PubMed:22307851,
CC ECO:0000305|PubMed:22307851, ECO:0000305|PubMed:26459592}.
CC -!- INTERACTION:
CC Q9LV27; P49677: IAA1; NbExp=4; IntAct=EBI-4453099, EBI-630505;
CC Q9LV27; O23160: MYB73; NbExp=3; IntAct=EBI-4453099, EBI-25506855;
CC Q9LV27; Q05762: THY-1; NbExp=6; IntAct=EBI-4453099, EBI-4455031;
CC Q9LV27; Q84MB2: TIFY8; NbExp=4; IntAct=EBI-4453099, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:22307851}.
CC -!- TISSUE SPECIFICITY: Expressed in the root central cylinder, root tips,
CC emerging lateral roots, vasculature of cotyledons, leaf stomata, leaf
CC stipules, anthers, pollen, filaments, and vasculature of petals and
CC sepals. {ECO:0000269|PubMed:22307851}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth and unable to flower under short
CC day conditions. Retarded growth, bushy rosettes, development of
CC multiple apical meristems and unable to flower under long day
CC conditions. {ECO:0000269|PubMed:22307851}.
CC -!- SIMILARITY: Belongs to the WD repeat LST8 family. {ECO:0000305}.
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DR EMBL; AB020749; BAB02026.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76052.1; -; Genomic_DNA.
DR EMBL; BT002312; AAN86145.1; -; mRNA.
DR EMBL; AK316732; BAH19457.1; -; mRNA.
DR EMBL; AY087463; AAM65008.1; -; mRNA.
DR RefSeq; NP_188442.1; NM_112696.3.
DR AlphaFoldDB; Q9LV27; -.
DR SMR; Q9LV27; -.
DR IntAct; Q9LV27; 94.
DR STRING; 3702.AT3G18140.1; -.
DR PaxDb; Q9LV27; -.
DR PRIDE; Q9LV27; -.
DR ProteomicsDB; 238487; -.
DR EnsemblPlants; AT3G18140.1; AT3G18140.1; AT3G18140.
DR GeneID; 821339; -.
DR Gramene; AT3G18140.1; AT3G18140.1; AT3G18140.
DR KEGG; ath:AT3G18140; -.
DR Araport; AT3G18140; -.
DR TAIR; locus:2092722; AT3G18140.
DR eggNOG; KOG0315; Eukaryota.
DR HOGENOM; CLU_000288_57_5_1; -.
DR InParanoid; Q9LV27; -.
DR OMA; VQRNYKH; -.
DR OrthoDB; 779909at2759; -.
DR PhylomeDB; Q9LV27; -.
DR PRO; PR:Q9LV27; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LV27; baseline and differential.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
DR GO; GO:0048571; P:long-day photoperiodism; IMP:TAIR.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:1900088; P:regulation of inositol biosynthetic process; IMP:TAIR.
DR GO; GO:1900091; P:regulation of raffinose biosynthetic process; IMP:TAIR.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037588; MLST8.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19842; PTHR19842; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Endosome; Growth regulation; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..305
FT /note="Target of rapamycin complex subunit LST8-1"
FT /id="PRO_0000444992"
FT REPEAT 1..30
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 33..71
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 76..115
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 117..156
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 160..199
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 209..248
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 251..292
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT CONFLICT 99
FT /note="D -> E (in Ref. 4; BAH19457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 34310 MW; DE4F5E1D185EC8D5 CRC64;
MSQPSVILAT ASYDHTIRFW EAETGRCYRT IQYPDSHVNR LEITPDKHYL AAACNPHIRL
FDVNSNSPQP VMTYDSHTNN VMAVGFQCDA KWMYSGSEDG TVKIWDLRAP GCQKEYESVA
AVNTVVLHPN QTELISGDQN GNIRVWDLRA NSCSCELVPE VDTAVRSLTV MWDGTMVVAA
NNRGTCYVWR LLRGKQTMTE FEPLHKLQAH NGHILKCLLS PANKYLATAS SDKTVKIWNV
DGFKLEKVLT GHQRWVWDCV FSVDGEFLVT ASSDMTARLW SMPAGKEVKV YQGHHKATVC
CALHD
