GNL3_CAEEL
ID GNL3_CAEEL Reviewed; 556 AA.
AC Q21086;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Guanine nucleotide-binding protein-like 3 homolog;
DE AltName: Full=Nucleostemin-1;
GN Name=nst-1 {ECO:0000312|WormBase:K01C8.9};
GN ORFNames=K01C8.9 {ECO:0000312|WormBase:K01C8.9};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RA Yang Z., Banfill M., Reinke V.;
RT "Functional genomic characterization of germline stem cells in C.
RT elegans.";
RL (In) Proceedings of the 2004 East coast worm meeting, abstract#266, Yale
RL (2004).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=18635357; DOI=10.1016/j.cub.2008.06.065;
RA Chen L., McCloskey T., Joshi P.M., Rothman J.H.;
RT "ced-4 and proto-oncogene tfg-1 antagonistically regulate cell size and
RT apoptosis in C. elegans.";
RL Curr. Biol. 18:1025-1033(2008).
CC -!- FUNCTION: May play a role in regulating cellular proliferation in both
CC germline and somatic tissues. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {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 -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a reduced body
CC length (PubMed:18635357). This phenotype in suppressed in a ced-4 n1162
CC mutant background (PubMed:18635357). {ECO:0000269|PubMed:18635357}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; BX284602; CAA88860.1; -; Genomic_DNA.
DR PIR; T23172; T23172.
DR RefSeq; NP_495749.1; NM_063348.3.
DR AlphaFoldDB; Q21086; -.
DR SMR; Q21086; -.
DR BioGRID; 39658; 5.
DR IntAct; Q21086; 1.
DR STRING; 6239.K01C8.9; -.
DR iPTMnet; Q21086; -.
DR EPD; Q21086; -.
DR PaxDb; Q21086; -.
DR PeptideAtlas; Q21086; -.
DR EnsemblMetazoa; K01C8.9.1; K01C8.9.1; WBGene00003821.
DR GeneID; 174329; -.
DR KEGG; cel:CELE_K01C8.9; -.
DR UCSC; K01C8.9; c. elegans.
DR CTD; 174329; -.
DR WormBase; K01C8.9; CE02270; WBGene00003821; nst-1.
DR eggNOG; KOG2484; Eukaryota.
DR GeneTree; ENSGT00940000166920; -.
DR HOGENOM; CLU_011106_5_3_1; -.
DR InParanoid; Q21086; -.
DR OMA; NWIKYFR; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q21086; -.
DR Reactome; R-CEL-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q21086; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003821; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
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 InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR Pfam; PF08701; GN3L_Grn1; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 3: Inferred from homology;
KW Coiled coil; GTP-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..556
FT /note="Guanine nucleotide-binding protein-like 3 homolog"
FT /id="PRO_0000122450"
FT DOMAIN 138..317
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 58..95
FT /evidence="ECO:0000255"
FT COMPBIAS 463..477
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184..187
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 266..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 310..313
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 556 AA; 62339 MW; 95AC9FCFECAAB465 CRC64;
MAKYCLKKTS KRVSCAKRYK IEKKVRDHNR KVKKEAKKNG TTNKKEKTIS VPNSCPFKEE
ILVQAEQERE KIKVRQEAAK EAAKIHRIEK RKNNLPANFE SMVAKASKQG TEFDKKVASA
AEHEKFNTLD DKTIKAYASE VRKTVEIADV IIQVLDARDP LGSRSKSVED QVLKGGKRLV
LLLNKIDLVP RENVQKWLEY LRGQFPTIAF KASTQEQKSN IGRFNSAILN NTETSKCVGA
DIVMKILANY CRNKDIKTSI RVGVVGFPNV GKSSVINSLK RRKACNVGNL PGITKEIQEV
ELDKNIRLID SPGVILVSQK DLDPIEVALK NAIRVDNLLD PIAPVHAILR RCSKETIMLH
YNLADFNSVD QFLAQLARRI GKLRRGARPD VNAAAKRVLN DWNTGKLRYY THPPEQGTAK
EDIVVPAEVV SQFSKEFDID AIAEEQNQIV EGLPMESDII APHNSDEEED DDDEMETDVN
EKKQTVTSGR KVKGPTKDDD KPVLPESLAL EGNVQLNKLI KTAIKKQKKK SKKTANRADK
LSDSLGNMLG GDAMEM
