LSG12_ARATH
ID LSG12_ARATH Reviewed; 589 AA.
AC Q9SJF1;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=GTPase LSG1-2 {ECO:0000303|PubMed:25319368};
DE Short=AtLSG1-2 {ECO:0000303|PubMed:25319368};
DE AltName: Full=DAR GTPase 7 {ECO:0000303|PubMed:16849600};
DE AltName: Full=Protein YEAST LSG1 ORTHOLOG 2 {ECO:0000303|PubMed:25319368};
GN Name=LSG1-2 {ECO:0000303|PubMed:25319368};
GN Synonyms=DPG7 {ECO:0000303|PubMed:16849600};
GN OrderedLocusNames=At1g08410 {ECO:0000312|Araport:AT1G08410};
GN ORFNames=T27G7.9 {ECO:0000312|EMBL:AAF22888.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DOMAIN, AND GENE FAMILY.
RX PubMed=9573393; DOI=10.1016/s0378-1119(98)00088-2;
RA Fu G., Melville S., Brewster S., Warner J., Barker D.C.;
RT "Analysis of the genomic organisation of a small chromosome of Leishmania
RT braziliensis M2903 reveals two genes encoding GTP-binding proteins, one of
RT which belongs to a new G-protein family and is an antigen.";
RL Gene 210:325-333(1998).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16849600; DOI=10.1534/genetics.106.060657;
RA Hill T.A., Broadhvest J., Kuzoff R.K., Gasser C.S.;
RT "Arabidopsis SHORT INTEGUMENTS 2 is a mitochondrial DAR GTPase.";
RL Genetics 174:707-718(2006).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, 3D-STRUCTURE MODELING, AND DISRUPTION PHENOTYPE.
RX PubMed=25319368; DOI=10.1111/tpj.12703;
RA Weis B.L., Missbach S., Marzi J., Bohnsack M.T., Schleiff E.;
RT "The 60S associated ribosome biogenesis factor LSG1-2 is required for 40S
RT maturation in Arabidopsis thaliana.";
RL Plant J. 80:1043-1056(2014).
CC -!- FUNCTION: GTPase involved in ribosome biogenesis (Probable). Binds to
CC 23S rRNA and associates with 60S pre-ribosomes (PubMed:25319368).
CC Involved in early cotyledon and leaf development (PubMed:25319368).
CC {ECO:0000269|PubMed:25319368}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.13 min(-1). {ECO:0000269|PubMed:25319368};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25319368}. Nucleus
CC {ECO:0000269|PubMed:25319368}. Note=The C-terminus is sufficient for
CC the targeting into the nucleus. {ECO:0000269|PubMed:25319368}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. {ECO:0000305};
CC Name=1;
CC IsoId=Q9SJF1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the highest expression in
CC reproductive and strongly dividing tissues.
CC {ECO:0000269|PubMed:25319368}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern. {ECO:0000305}.
CC -!- DOMAIN: The DARXP motif is also sometime designated as G6 region.
CC {ECO:0000305|PubMed:9573393}.
CC -!- DISRUPTION PHENOTYPE: No effect on the association with 60S pre-
CC ribosomes, but altered rRNA processing and accumulation of 18S rRNA
CC precursors (PubMed:25319368). Embryo and leaf developmental defects
CC (PubMed:25319368). Severe delay in development of the first true
CC rosette leaves and frequent fused or triple cotyledons
CC (PubMed:25319368). Lsg1-1 and lsg1-2 double mutants are lethal, when
CC homozygous (PubMed:25319368). {ECO:0000269|PubMed:25319368}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AC006932; AAF22888.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28286.1; -; Genomic_DNA.
DR EMBL; BT023444; AAY56435.1; -; mRNA.
DR EMBL; BT030367; ABO38780.1; -; mRNA.
DR RefSeq; NP_172317.1; NM_100714.3. [Q9SJF1-1]
DR AlphaFoldDB; Q9SJF1; -.
DR SMR; Q9SJF1; -.
DR STRING; 3702.AT1G08410.1; -.
DR PaxDb; Q9SJF1; -.
DR PRIDE; Q9SJF1; -.
DR ProteomicsDB; 238679; -. [Q9SJF1-1]
DR EnsemblPlants; AT1G08410.1; AT1G08410.1; AT1G08410. [Q9SJF1-1]
DR GeneID; 837361; -.
DR Gramene; AT1G08410.1; AT1G08410.1; AT1G08410. [Q9SJF1-1]
DR KEGG; ath:AT1G08410; -.
DR Araport; AT1G08410; -.
DR TAIR; locus:2201861; AT1G08410.
DR eggNOG; KOG1424; Eukaryota.
DR HOGENOM; CLU_011072_10_0_1; -.
DR InParanoid; Q9SJF1; -.
DR OMA; VNKADMM; -.
DR OrthoDB; 839833at2759; -.
DR PhylomeDB; Q9SJF1; -.
DR PRO; PR:Q9SJF1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SJF1; baseline and differential.
DR Genevisible; Q9SJF1; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; 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; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:TAIR.
DR GO; GO:0048825; P:cotyledon development; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0090070; P:positive regulation of ribosome biogenesis; IMP:TAIR.
DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:TAIR.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:TAIR.
DR GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR043358; GNL1-like.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45709; PTHR45709; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTP-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..589
FT /note="GTPase LSG1-2"
FT /id="PRO_0000432560"
FT DOMAIN 158..366
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..209
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 237..239
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 315..322
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 341..345
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 359..362
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 495..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 176..180
FT /note="DARXP motif"
FT MOTIF 534..541
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 539..557
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206..209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 318..323
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
SQ SEQUENCE 589 AA; 66743 MW; 91361B19E17C6EFF CRC64;
MGKSEKTSLG RSLVKHHNHM IQESKDKGKY YKNLQKKVLE SVTEVSDIDA IIEQAEEAER
LYTINHSSST PLSINLDTNS SSSVIAAEEW REQQKIEEAL HASSLQVPRR PPWTPEMSVE
ELDANEKQAF LNWRRMLVSL EENEKLVLTP FEKNLDIWRQ LWRVLERSDL IVMVVDARDP
LFYRCPDLEA YAQEIDEHKK IMLLVNKADL LPTDVREKWA EYFRLNNILF VFWSAIAATA
TLEGKVLKEQ WRQPDNLQKT DDPDIMIYGR DELLSRLQFE AQEIVKVRNS RAASVSSQSW
TGEYQRDQAV VGFVGYPNVG KSSTINALVG QKRTGVTSTP GKTKHFQTLI ISDELMLCDC
PGLVFPSFSS SRYEMIASGV LPIDRMTEHR EAIQVVADKV PRRVIESVYN ISLPKPKTYE
RQSRPPHAAE LLKSYCASRG YVASSGLPDE TKAARLILKD YIGGKLPHYA MPPGMPQADE
PDIEDTQELE DILEGSESDD SAVGDETENE QVPGIDDVLD DLSSFDLANG LKSSKKVTAK
KQTASHKQHK KPQRKKDRTW RVQNTEDGDG MPSVKVFQKP ANTGPLTMR
