LSG1_RAT
ID LSG1_RAT Reviewed; 655 AA.
AC Q5BJT6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Large subunit GTPase 1 homolog;
DE EC=3.6.1.-;
GN Name=Lsg1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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 -!- 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; BC091338; AAH91338.1; -; mRNA.
DR RefSeq; NP_001013439.1; NM_001013421.1.
DR AlphaFoldDB; Q5BJT6; -.
DR SMR; Q5BJT6; -.
DR STRING; 10116.ENSRNOP00000002354; -.
DR jPOST; Q5BJT6; -.
DR PaxDb; Q5BJT6; -.
DR PRIDE; Q5BJT6; -.
DR Ensembl; ENSRNOT00000002354; ENSRNOP00000002354; ENSRNOG00000001727.
DR GeneID; 288029; -.
DR KEGG; rno:288029; -.
DR UCSC; RGD:1309089; rat.
DR CTD; 55341; -.
DR RGD; 1309089; Lsg1.
DR eggNOG; KOG1424; Eukaryota.
DR GeneTree; ENSGT00940000156442; -.
DR InParanoid; Q5BJT6; -.
DR OMA; VNKADMM; -.
DR OrthoDB; 839833at2759; -.
DR PhylomeDB; Q5BJT6; -.
DR TreeFam; TF105747; -.
DR PRO; PR:Q5BJT6; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001727; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q5BJT6; RN.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
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; -; 1.
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 2: Evidence at transcript level;
KW Cytoplasm; Endoplasmic reticulum; GTP-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..655
FT /note="Large subunit GTPase 1 homolog"
FT /id="PRO_0000324556"
FT DOMAIN 164..441
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..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..323
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
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 390..397
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 434..437
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 MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H089"
SQ SEQUENCE 655 AA; 74403 MW; F91E42DDC58BE407 CRC64;
MGRRRAPGGG SLGRVLIRHQ TQRSRSHRHT DSWLHTSELN DGYDWGRLNL QSVTEQSSLE
DFLATAELAG TEFVAEKLNI KFVPPEARTG LLSFEESQRI KRLHEENRQF LCIPRRPNWD
RKTSPEELKQ AEKDNFLKWR RQLVRLEEEQ KLILTPFERN LDFWRQLWRV IERSDIVVQI
VDARNPLLFR CEDLECYVKE IDAAKENVIL INKADLLTAE QRVAWAVHFE KEGVKVIFWS
ALAETVHLNG DSKDEVNSVA GEANSSESED SSLDGNEIPH RDLFLLSEES ESDDDDSEYE
DCQEDEEEDW QTCSEEDSNP EEGQEEGGCD RDQKEHGPED SEAQSRASPE NSQMSNKSHL
VSKQELLELF KKLHTGKKVK DGQLTVGLVG YPNVGKSSTI NTIMGNKKVS VSATPGHTKH
FQTLYVEPGL CLCDCPGLVM PSFVSTKAEM ICSGILPIDQ MRDHVPPVSL VCQNIPRRVL
EATYGINIIK PGEDEDPYRP PTSEELLTAY GCMRGFMTAH GQPDQPRSAR YILKDYVRGK
LLYCHPPPGK DPVAFQHQHR QLLENKIKGE ELRLQPGKTQ KAKQVENVVD KTFFHQENVR
ALTKGVQAVM GYKPGSGLVT AAAASAENVP GKPWKKHGNR NKKEKSRRLY RHLDV
