LIIP1_ARATH
ID LIIP1_ARATH Reviewed; 342 AA.
AC Q9C5J9; Q9LV96;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Small GTPase LIP1 {ECO:0000303|PubMed:17683937};
DE AltName: Full=Protein LIGHT INSENSITIVE PERIOD 1 {ECO:0000303|PubMed:17683937};
GN Name=LIP1 {ECO:0000303|PubMed:17683937};
GN OrderedLocusNames=At5g64813 {ECO:0000312|Araport:AT5G64813};
GN ORFNames=MXK3.3 {ECO:0000312|EMBL:BAA97293.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17683937; DOI=10.1016/j.cub.2007.07.018;
RA Kevei E., Gyula P., Feher B., Toth R., Viczian A., Kircher S., Rea D.,
RA Dorjgotov D., Schaefer E., Millar A.J., Kozma-Bognar L., Nagy F.;
RT "Arabidopsis thaliana circadian clock is regulated by the small GTPase
RT LIP1.";
RL Curr. Biol. 17:1456-1464(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=23144185; DOI=10.1104/pp.112.203356;
RA Terecskei K., Toth R., Gyula P., Kevei E., Bindics J., Coupland G.,
RA Nagy F., Kozma-Bognar L.;
RT "The circadian clock-associated small GTPase LIGHT INSENSITIVE PERIOD1
RT suppresses light-controlled endoreplication and affects tolerance to salt
RT stress in Arabidopsis.";
RL Plant Physiol. 161:278-290(2013).
CC -!- FUNCTION: Functional small GTPase that acts as a negative factor
CC controlling the light-dependent period shortening of circadian rhythms
CC and light-induced phase resetting during the subjective night
CC (PubMed:17683937). May protect the clock from excessive or mistimed
CC light (PubMed:17683937). Suppresses red and blue light-mediated
CC photomorphogenesis and is required for light-controlled inhibition of
CC endoreplication and tolerance to salt stress (PubMed:23144185). The
CC entrainment of the circadian clock is independent from the other
CC pleiotropic effects (PubMed:23144185). Could be a regulator of seedling
CC establishment (PubMed:23144185). {ECO:0000269|PubMed:17683937,
CC ECO:0000269|PubMed:23144185}.
CC -!- INTERACTION:
CC Q9C5J9; O49403: HSFA4A; NbExp=4; IntAct=EBI-4449491, EBI-25511393;
CC Q9C5J9; Q38845: PP2AA1; NbExp=4; IntAct=EBI-4449491, EBI-1645478;
CC Q9C5J9; Q8GXW1: RGL2; NbExp=3; IntAct=EBI-4449491, EBI-963665;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17683937,
CC ECO:0000269|PubMed:23144185}. Cytoplasm {ECO:0000269|PubMed:17683937,
CC ECO:0000269|PubMed:23144185}. Note=The localization is not affected by
CC light, but the nuclear localization is essential for the circadian
CC function. {ECO:0000269|PubMed:17683937, ECO:0000269|PubMed:23144185}.
CC -!- INDUCTION: Not regulated by the circadian clock.
CC {ECO:0000269|PubMed:17683937}.
CC -!- DISRUPTION PHENOTYPE: Short-period phenotype even in darkness and short
CC hypocotyls in response to red and blue light but not to far-red light
CC (PubMed:17683937). Altered cell shape and increased ploidy levels at
CC the seedling stage (PubMed:23144185). Hypersensitivity to salt stress
CC (PubMed:23144185). {ECO:0000269|PubMed:17683937,
CC ECO:0000269|PubMed:23144185}.
CC -!- MISCELLANEOUS: Has a GTPase activity despite the replacement of the
CC highly conserved Glu-94 for His. {ECO:0000269|PubMed:17683937}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97293.1; Type=Erroneous gene model prediction; Note=The predicted gene At5g64810 has been split into 3 genes: At5g64810, At5g64813 and At5g64816.; Evidence={ECO:0000305};
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DR EMBL; AB019236; BAA97293.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97954.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70069.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70070.1; -; Genomic_DNA.
DR EMBL; AF360203; AAK25913.1; -; mRNA.
DR EMBL; AY040050; AAK64108.1; -; mRNA.
DR RefSeq; NP_001318878.1; NM_001345650.1.
DR RefSeq; NP_001331706.1; NM_001345651.1.
DR RefSeq; NP_568996.1; NM_125878.3.
DR AlphaFoldDB; Q9C5J9; -.
DR SMR; Q9C5J9; -.
DR BioGRID; 21845; 6.
DR IntAct; Q9C5J9; 6.
DR STRING; 3702.AT5G64813.1; -.
DR iPTMnet; Q9C5J9; -.
DR PaxDb; Q9C5J9; -.
DR PRIDE; Q9C5J9; -.
DR ProteomicsDB; 238419; -.
DR EnsemblPlants; AT5G64813.1; AT5G64813.1; AT5G64813.
DR EnsemblPlants; AT5G64813.2; AT5G64813.2; AT5G64813.
DR EnsemblPlants; AT5G64813.3; AT5G64813.3; AT5G64813.
DR GeneID; 836603; -.
DR Gramene; AT5G64813.1; AT5G64813.1; AT5G64813.
DR Gramene; AT5G64813.2; AT5G64813.2; AT5G64813.
DR Gramene; AT5G64813.3; AT5G64813.3; AT5G64813.
DR KEGG; ath:AT5G64813; -.
DR Araport; AT5G64813; -.
DR TAIR; locus:505006713; AT5G64813.
DR eggNOG; ENOG502QT3S; Eukaryota.
DR HOGENOM; CLU_061105_0_0_1; -.
DR InParanoid; Q9C5J9; -.
DR OMA; MMFWRER; -.
DR OrthoDB; 1269342at2759; -.
DR PhylomeDB; Q9C5J9; -.
DR BioCyc; ARA:AT5G64813-MON; -.
DR PRO; PR:Q9C5J9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5J9; baseline and differential.
DR Genevisible; Q9C5J9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..342
FT /note="Small GTPase LIP1"
FT /id="PRO_0000220618"
FT REGION 12..285
FT /note="Small GTPase-like"
FT REGION 274..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 90..94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 160..163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 342 AA; 37741 MW; 3F263576376AAF2E CRC64;
MKFWRERERE NKEQILAPLC GQVRVLVVGD SGVGKTSLVH LINKGSSIVR PPQTIGCTVG
VKHITYGSPA SSSSSIQGDS ERDFFVELWD VSGHERYKDC RSLFYSQING VIFVHDLSQR
RTKTSLQKWA SEVAATGTFS APLPSGGPGG LPVPYIVVGN KADIAAKEGT KGSSGNLVDA
ARHWVEKQGL LPSSSEDLPL FESFPGNGGL IAAAKETRYD KEALNKFFRM LIRRRYFSDE
LPAASPWSIS PVPTSSSQRL DEITSDDDQF YKRTSFHGDP YKYNNTIPPL PAQRNLTPPP
TLYPQQPVST PDNYTIPRYS LSSVQETTNN GSARSKRMDI NV
