GNL3L_MOUSE
ID GNL3L_MOUSE Reviewed; 577 AA.
AC Q6PGG6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Guanine nucleotide-binding protein-like 3-like protein;
GN Name=Gnl3l;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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).
RN [3]
RP FUNCTION, INTERACTION WITH TERF1 AND TERT, AND MUTAGENESIS OF ASN-166.
RX PubMed=19487455; DOI=10.1083/jcb.200812121;
RA Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.;
RT "GNL3L stabilizes the TRF1 complex and promotes mitotic transition.";
RL J. Cell Biol. 185:827-839(2009).
RN [4]
RP FUNCTION, INTERACTION WITH MDM2 AND TP53, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-253.
RX PubMed=21132010; DOI=10.1038/onc.2010.550;
RA Meng L., Hsu J.K., Tsai R.Y.;
RT "GNL3L depletion destabilizes MDM2 and induces p53-dependent G2/M arrest.";
RL Oncogene 30:1716-1726(2011).
CC -!- FUNCTION: Stabilizes TERF1 telomeric association by preventing TERF1
CC recruitment by PML. Stabilizes TERF1 protein by preventing its
CC ubiquitination and hence proteasomal degradation. Does so by
CC interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase.
CC Required for cell proliferation. By stabilizing TRF1 protein during
CC mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2
CC protein by preventing its ubiquitination, and hence proteasomal
CC degradation. By acting on MDM2, may affect TP53 activity. Required for
CC normal processing of ribosomal pre-rRNA. Binds GTP (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:19487455,
CC ECO:0000269|PubMed:21132010}.
CC -!- SUBUNIT: Interacts with MDM2; this interaction, which occurs in the
CC nucleoplasm, stabilizes MDM2. Indirectly interacts with TP53, via MDM2-
CC binding. Interacts with TERF1; this interaction probably occurs in the
CC nucleoplasm and is increased during mitosis, when the nucleolus is
CC disassembled. This binding may promote TERF1 homodimerization.
CC Interacts with TERT. {ECO:0000269|PubMed:19487455,
CC ECO:0000269|PubMed:21132010}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21132010}.
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.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AL805937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057033; AAH57033.1; -; mRNA.
DR EMBL; BC079653; AAH79653.1; -; mRNA.
DR CCDS; CCDS41174.1; -.
DR RefSeq; NP_001162071.1; NM_001168600.1.
DR RefSeq; NP_932778.1; NM_198110.2.
DR RefSeq; XP_006528868.1; XM_006528805.3.
DR AlphaFoldDB; Q6PGG6; -.
DR SMR; Q6PGG6; -.
DR BioGRID; 231842; 3.
DR IntAct; Q6PGG6; 1.
DR MINT; Q6PGG6; -.
DR STRING; 10090.ENSMUSP00000108311; -.
DR iPTMnet; Q6PGG6; -.
DR PhosphoSitePlus; Q6PGG6; -.
DR EPD; Q6PGG6; -.
DR MaxQB; Q6PGG6; -.
DR PaxDb; Q6PGG6; -.
DR PeptideAtlas; Q6PGG6; -.
DR PRIDE; Q6PGG6; -.
DR ProteomicsDB; 271007; -.
DR Antibodypedia; 43618; 211 antibodies from 23 providers.
DR DNASU; 237107; -.
DR Ensembl; ENSMUST00000026297; ENSMUSP00000026297; ENSMUSG00000025266.
DR Ensembl; ENSMUST00000112691; ENSMUSP00000108311; ENSMUSG00000025266.
DR GeneID; 237107; -.
DR KEGG; mmu:237107; -.
DR UCSC; uc009uou.2; mouse.
DR CTD; 54552; -.
DR MGI; MGI:2448557; Gnl3l.
DR VEuPathDB; HostDB:ENSMUSG00000025266; -.
DR eggNOG; KOG2484; Eukaryota.
DR GeneTree; ENSGT00940000155877; -.
DR HOGENOM; CLU_011106_5_4_1; -.
DR InParanoid; Q6PGG6; -.
DR OMA; NWIKYFR; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q6PGG6; -.
DR TreeFam; TF313085; -.
DR BioGRID-ORCS; 237107; 24 hits in 76 CRISPR screens.
DR ChiTaRS; Gnl3l; mouse.
DR PRO; PR:Q6PGG6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6PGG6; protein.
DR Bgee; ENSMUSG00000025266; Expressed in undifferentiated genital tubercle and 226 other tissues.
DR ExpressionAtlas; Q6PGG6; baseline and differential.
DR Genevisible; Q6PGG6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:1904816; P:positive regulation of protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
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; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..577
FT /note="Guanine nucleotide-binding protein-like 3-like
FT protein"
FT /id="PRO_0000284382"
FT DOMAIN 118..304
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 9..28
FT /note="Required for nucleolar localization"
FT /evidence="ECO:0000250"
FT COILED 43..103
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166..169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 253..260
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 297..300
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MUTAGEN 166
FT /note="N->I: No effect on TERF1-binding. Loss of ability to
FT stabilize TERF1 protein."
FT /evidence="ECO:0000269|PubMed:19487455"
FT MUTAGEN 253
FT /note="G->V: Mislocalized to the nucleoplasm. No effect on
FT the reduction of MDM2 ubiquitination."
FT /evidence="ECO:0000269|PubMed:21132010"
SQ SEQUENCE 577 AA; 65195 MW; C2F6E1FE5EED9815 CRC64;
MMKIRHKNKK PGKGSKGCKK PARQNGKKVT SRPSSAPQIV HGNDHASREA ELKKKRVEEM
REKQQVAREQ ERQRHRTMES YCQDVLKRQQ EFEQKEEVLQ ELNMFPQLDD EATRKAYYKE
FRKVVEYSDV ILEVLDARDP LGCRCFQMEE TVLRAEGNKK LVLVLNKIDL VPKEIVEKWL
EYLLNELPTV AFKASTQHHQ VKNLTRCKVP VDQASESLLK SRACFGAENL MRVLGNYCRL
GEVRGHIRVG VVGLPNVGKS SLINSLKRSR ACSVGAVPGV TKFMQEVYLD KFIRLLDAPG
IVPGPNSEVG TILRNCIHVQ KLADPVTPVE TILQRCNLEE ISSYYGVSGF QTTEHFLTAV
AHRLGKKKKG GVYSQEQAAK AVLADWVSGK ISFYTLPPPT HTLPTHLSAE IVKEMTEVFD
IEDTEHANED TMECLAVGES DELLGDMDPQ EMEVRWLHSP LVKIADAIEN RSTVYKIGNL
TGYCTKPNRN QMGWPKRNVD HHCPQNNRVV EVSSVDRRPM LQRILETDPL QQGQALASAL
KNKKKLQKRS DKIATKLSDS MMSMLDLSGN SDDCAGD
