LSG1_MOUSE
ID LSG1_MOUSE Reviewed; 644 AA.
AC Q3UM18; Q68ED9; Q80V36;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Large subunit GTPase 1 homolog;
DE EC=3.6.1.-;
GN Name=Lsg1; Synonyms=D16Bwg1547e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Heart, Mammary gland, and Muellerian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 44-644 (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/NJ; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: GTPase required for the XPO1/CRM1-mediated nuclear export of
CC the 60S ribosomal subunit. Probably acts by mediating the release of
CC NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250}. Note=Shuttles between the Cajal
CC bodies in the nucleus and the endoplasmic reticulum. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UM18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UM18-2; Sequence=VSP_032275;
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.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. LSG1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AK135345; BAE22495.1; -; mRNA.
DR EMBL; AK145186; BAE26280.1; -; mRNA.
DR EMBL; AK146895; BAE27512.1; -; mRNA.
DR EMBL; BC043724; AAH43724.1; -; mRNA.
DR EMBL; BC080306; AAH80306.1; -; mRNA.
DR CCDS; CCDS37311.1; -. [Q3UM18-1]
DR RefSeq; NP_835170.1; NM_178069.5. [Q3UM18-1]
DR AlphaFoldDB; Q3UM18; -.
DR SMR; Q3UM18; -.
DR BioGRID; 230241; 36.
DR IntAct; Q3UM18; 2.
DR MINT; Q3UM18; -.
DR STRING; 10090.ENSMUSP00000112860; -.
DR iPTMnet; Q3UM18; -.
DR PhosphoSitePlus; Q3UM18; -.
DR EPD; Q3UM18; -.
DR MaxQB; Q3UM18; -.
DR PaxDb; Q3UM18; -.
DR PeptideAtlas; Q3UM18; -.
DR PRIDE; Q3UM18; -.
DR ProteomicsDB; 293401; -. [Q3UM18-1]
DR ProteomicsDB; 293402; -. [Q3UM18-2]
DR Antibodypedia; 46856; 46 antibodies from 16 providers.
DR DNASU; 224092; -.
DR Ensembl; ENSMUST00000117363; ENSMUSP00000112860; ENSMUSG00000022538. [Q3UM18-1]
DR GeneID; 224092; -.
DR KEGG; mmu:224092; -.
DR UCSC; uc007ywv.1; mouse. [Q3UM18-1]
DR CTD; 55341; -.
DR MGI; MGI:107236; Lsg1.
DR VEuPathDB; HostDB:ENSMUSG00000022538; -.
DR eggNOG; KOG1424; Eukaryota.
DR GeneTree; ENSGT00940000156442; -.
DR HOGENOM; CLU_011072_7_0_1; -.
DR InParanoid; Q3UM18; -.
DR OMA; VNKADMM; -.
DR OrthoDB; 839833at2759; -.
DR PhylomeDB; Q3UM18; -.
DR TreeFam; TF105747; -.
DR BioGRID-ORCS; 224092; 27 hits in 77 CRISPR screens.
DR ChiTaRS; Lsg1; mouse.
DR PRO; PR:Q3UM18; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3UM18; protein.
DR Bgee; ENSMUSG00000022538; Expressed in spermatocyte and 240 other tissues.
DR Genevisible; Q3UM18; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0051168; P:nuclear export; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR043358; GNL1-like.
DR InterPro; IPR006073; GTP-bd.
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; Endoplasmic reticulum; GTP-binding;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..644
FT /note="Large subunit GTPase 1 homolog"
FT /id="PRO_0000324555"
FT DOMAIN 164..430
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..327
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 379..386
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 423..426
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H089"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H089"
FT VAR_SEQ 146..174
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032275"
FT CONFLICT 284
FT /note="I -> F (in Ref. 1; BAE26280)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="A -> E (in Ref. 1; BAE26280)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="K -> E (in Ref. 1; BAE26280)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="P -> PE (in Ref. 1; BAE26280)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="N -> P (in Ref. 1; BAE26280)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="A -> T (in Ref. 1; BAE26280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 73157 MW; DB6962294D44EA96 CRC64;
MGRRRAPGGG SLGRVLIRQQ TQRSRSHRHT DSWLHTSELN DGYDWGRLNL QSVTEQSSLE
DFLATAELAG TEFVAEKLNI KFVPPEARTG LLSFEESQRI KKLHEENRQF LCIPRRPNWD
RKTSPEELKQ AEKDNFLKWR RQLVRLEEEQ KLILTPFERN LDFWRQLWRV IERSDIVVQI
VDARNPLLFR CEDLECYVKE IDAAKENVIL INKADLLTAE QRFAWAVHFE KEGVKVIFWS
ALAETDHLNG DLKEEVDSVA GDTNKTESES SSLDANEIPH RDLISLSEES ASDSGDSKYE
DCQEDEEEDW QTCSEEDSVP EEEEGCNADS ETQNRKNAEN QQVNNDSYLV SKQELLELFK
KLHTGKKVKD GQLTVGLVGY PNVGKSSTIN TIMGNKKVSV SATPGHTKHF QTLYVEPGLC
LCDCPGLVMP SFVSTKAEMI CNGILPIDQM RDHVPPVSLV CQNIPRRVLE VTYGINIIKP
REDEDPYRPP TSEELLTAYG CMRGFMTAHG QPDQPRSARY ILKDYVGGKL LYCHPPPGKD
PVAFQHQHQQ LLESKVKGGE LRLQPGKGRK AKQIENVVDK TFFHQENVRA LTKGVQAVMG
YKPGHGLVTA AAASAENVPG KPWKKHGNRN KKEKSRRLYK HLDV
