GNL3L_BOVIN
ID GNL3L_BOVIN Reviewed; 575 AA.
AC Q3T0J9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Guanine nucleotide-binding protein-like 3-like protein;
GN Name=GNL3L;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {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.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; BC102363; AAI02364.1; -; mRNA.
DR RefSeq; NP_001029479.1; NM_001034307.2.
DR RefSeq; XP_005228268.1; XM_005228211.3.
DR AlphaFoldDB; Q3T0J9; -.
DR SMR; Q3T0J9; -.
DR STRING; 9913.ENSBTAP00000004772; -.
DR PaxDb; Q3T0J9; -.
DR PRIDE; Q3T0J9; -.
DR Ensembl; ENSBTAT00000004772; ENSBTAP00000004772; ENSBTAG00000031564.
DR GeneID; 507679; -.
DR KEGG; bta:507679; -.
DR CTD; 54552; -.
DR VEuPathDB; HostDB:ENSBTAG00000031564; -.
DR VGNC; VGNC:29474; GNL3L.
DR eggNOG; KOG2484; Eukaryota.
DR GeneTree; ENSGT00940000155877; -.
DR HOGENOM; CLU_011106_5_4_1; -.
DR InParanoid; Q3T0J9; -.
DR OMA; NWIKYFR; -.
DR OrthoDB; 1210675at2759; -.
DR TreeFam; TF313085; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000031564; Expressed in uterine horn and 104 other tissues.
DR ExpressionAtlas; Q3T0J9; baseline.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Coiled coil; GTP-binding; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..575
FT /note="Guanine nucleotide-binding protein-like 3-like
FT protein"
FT /id="PRO_0000284380"
FT DOMAIN 118..303
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 51..79
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Basic 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 252..259
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 296..299
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9NVN8"
SQ SEQUENCE 575 AA; 64837 MW; 6B48BC61DA6E1E95 CRC64;
MMKLRHKNKK PGKGSKGCKK PAKQNGKKAA TKVAYSPQFF HSNDHASREA ELKKKRVGEM
REKQQAAREQ ERHRRRTIES YCQDVLRRQE EFEHKEEVLQ ELNMFPQLDD EATRKAYYKE
FHKVVEYSDV ILEVLDSRDP LGCRCFQMEE TVLRAEGNKK LVLVLNKIDL VPKEVVEKWL
EYLRNELPTV AFKASTQHQV KNLNRCSVPV DQASESLLKS KACFGAENLM RVLGNYCRLG
EVRTHIRVGV VGLPNVGKSS LINSLKRSRA CSVGAVPGVT KFMQEVYLDK FIRLLDAPGI
VPGPNSEVGT ILRNCIHVQK LADPVTPVET ILQRCNLEEI SSYYGVSGFQ TTEHFLTAVA
HRLGKKKKGG IYSQEQAAKA VLADWVSGKI SFYTLPPSTH TLPTHLSAEI VKEMTEVFDI
EDTEQANEDT MECLATGESD ELLGDMDPLE MEIKWLHSPM VKIADAMENK TTVYKIGDLT
GYCTNPNRHQ MGWAKRNVDL HPRNNSMVDV CPVDRRPVLQ RIMETDPLQQ GQALASALKK
KKKIQKRADK LASKLSDSMM SALDLSGNAD DSAGD
