GNL3_DROME
ID GNL3_DROME Reviewed; 581 AA.
AC Q8MT06; A4V308; B6IDZ0; Q9VEN7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Guanine nucleotide-binding protein-like 3 homolog;
DE AltName: Full=Nucleostemin 1;
DE AltName: Full=Nucleostemin homolog;
GN Name=Ns1; ORFNames=CG3983;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18628395; DOI=10.1101/gad.1670508;
RA Kaplan D.D., Zimmermann G., Suyama K., Meyer T., Scott M.P.;
RT "A nucleostemin family GTPase, NS3, acts in serotonergic neurons to
RT regulate insulin signaling and control body size.";
RL Genes Dev. 22:1877-1893(2008).
CC -!- FUNCTION: May play a role in regulating cellular proliferation.
CC {ECO:0000269|PubMed:18628395}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:18628395}.
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 -!- DISRUPTION PHENOTYPE: Impaired embryonic development resulting in a
CC profoundly reduced rate of larval hatching.
CC {ECO:0000269|PubMed:18628395}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AE014297; AAF55384.3; -; Genomic_DNA.
DR EMBL; AY118455; AAM49824.1; -; mRNA.
DR EMBL; BT050580; ACJ23464.1; -; mRNA.
DR RefSeq; NP_732199.2; NM_169742.3.
DR AlphaFoldDB; Q8MT06; -.
DR SMR; Q8MT06; -.
DR BioGRID; 67100; 16.
DR IntAct; Q8MT06; 2.
DR STRING; 7227.FBpp0082867; -.
DR iPTMnet; Q8MT06; -.
DR PaxDb; Q8MT06; -.
DR PRIDE; Q8MT06; -.
DR DNASU; 42060; -.
DR EnsemblMetazoa; FBtr0083426; FBpp0082867; FBgn0038473.
DR GeneID; 42060; -.
DR KEGG; dme:Dmel_CG3983; -.
DR UCSC; CG3983-RA; d. melanogaster.
DR CTD; 42060; -.
DR FlyBase; FBgn0038473; Ns1.
DR VEuPathDB; VectorBase:FBgn0038473; -.
DR eggNOG; KOG2484; Eukaryota.
DR GeneTree; ENSGT00940000166920; -.
DR HOGENOM; CLU_011106_5_3_1; -.
DR InParanoid; Q8MT06; -.
DR OMA; NWIKYFR; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q8MT06; -.
DR Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 42060; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42060; -.
DR PRO; PR:Q8MT06; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038473; Expressed in adult abdomen and 26 other tissues.
DR Genevisible; Q8MT06; DM.
DR GO; GO:0001652; C:granular component; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:FlyBase.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR014813; Gnl3_N_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08701; GN3L_Grn1; 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 Coiled coil; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..581
FT /note="Guanine nucleotide-binding protein-like 3 homolog"
FT /id="PRO_0000122451"
FT DOMAIN 141..325
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 64..108
FT /evidence="ECO:0000255"
FT COMPBIAS 1..46
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 274..281
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 318..321
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 94
FT /note="F -> I (in Ref. 3; AAM49824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 65985 MW; 77065E7A0430EEB7 CRC64;
MALKRLKTKK SKRLTGRLKH KIEKKVRDHN KKERRAAKKN PKKGSKKQKL IQIPNICPFK
DDILKEVEEA KQRQEAERLA RREAFKAERE QNKFKTLESM VEDADMRSTV HGIMHENDAQ
DQDEKKYKNA VTKEQSLKQY FKEFRKVIEN ADVVLEVVDA RDPLGTRCNE VERAVRGAPG
NKRLVLVLNK ADLVPRENLN NWIKYFRRSG PVTAFKASTQ DQANRLGRRK LREMKTEKAM
QGSVCIGAEL LMSMLGNYCR NKGIKTSIRV GVVGIPNVGK SSIINSLTRG RSCMVGSTPG
VTKSMQEVEL DSKIKLIDCP GIVFTSGGEN SHAVLKNAQR VGDVKDPFTI AESVLKRASK
EYFCTMYDIT NYDTFEEFFA KKAARMGKFL KKGVPDVVAA ARSVLNDWNT GKIKYCTQPP
EVQEGQSVHI SASIVHSEAR EFDVENFESM ETEILEHCAV KTDDIMEITS TGPLEIRQPR
EEAEPADKIT ASLVIDEKEK PAKGRKRKLD EEKEKVDPSL LLEENQSLNK GIKQMQKLKK
KQNVRNEKKI SKITDVLDSF SLGPSSSKAE KYDFDEDYVI E
