DRG1_BOVIN
ID DRG1_BOVIN Reviewed; 367 AA.
AC Q3MHP5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Developmentally-regulated GTP-binding protein 1;
DE Short=DRG-1;
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 3;
DE Short=NEDD-3;
DE AltName: Full=Translation factor GTPase DRG1;
DE Short=TRAFAC GTPase DRG1;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q9Y295};
GN Name=DRG1;
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=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of GTP to GDP through hydrolysis of
CC the gamma-phosphate bond in GTP. Appears to have an intrinsic GTPase
CC activity that is stimulated by ZC3H15/DFRP1 binding likely by
CC increasing the affinity for the potassium ions. When hydroxylated at C-
CC 3 of 'Lys-22' by JMJD7, may bind to RNA and play a role in translation.
CC Binds to microtubules and promotes microtubule polymerization and
CC bundling that are required for mitotic spindle assembly during prophase
CC to anaphase transition. GTPase activity is not necessary for these
CC microtubule-related functions. {ECO:0000250|UniProtKB:Q9Y295}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:Q9Y295};
CC -!- ACTIVITY REGULATION: The GTPase activity is enhanced by potassium ions
CC as well as by DFRP1 binding. {ECO:0000250|UniProtKB:Q9Y295}.
CC -!- SUBUNIT: Interacts (via its C-terminal) with TAL1. Interacts with
CC DFRP1/ZC3H15; this interaction prevents DRG1 poly-ubiquitination and
CC degradation by proteasome. DRG1-ZC3H15/DFRP1 complex co-sediments with
CC polysomes. Interacts with STK16. Interacts with JMJD7. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9Y295}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y295}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y295}. Note=The DRG1-ZC3H15/DFRP1 complex
CC associates with polysomes. {ECO:0000250|UniProtKB:Q9Y295}.
CC -!- DOMAIN: The ThrRS, GTPase, SpoT (TGS) domain is not necessary for GTP
CC binding nor for the GTPase activity. It appears to play a regulatory
CC role favoring GTP hydrolysis mediated by DFRP1/ZC3H15.
CC {ECO:0000250|UniProtKB:Q9Y295}.
CC -!- PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli.
CC {ECO:0000250|UniProtKB:Q9Y295}.
CC -!- PTM: Hydroxylated (with S stereochemistry) at C-3 of Lys-22 by JMJD7.
CC {ECO:0000250|UniProtKB:Q9Y295}.
CC -!- PTM: Phosphorylated at Thr-100 by STK16.
CC {ECO:0000250|UniProtKB:Q9Y295}.
CC -!- PTM: Polyubiquitinated; this modification induces proteolytic
CC degradation and is impaired by interaction with ZC3H15.
CC {ECO:0000250|UniProtKB:Q9Y295}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|PROSITE-ProRule:PRU01047}.
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DR EMBL; BC105158; AAI05159.1; -; mRNA.
DR RefSeq; NP_001029863.1; NM_001034691.1.
DR AlphaFoldDB; Q3MHP5; -.
DR BMRB; Q3MHP5; -.
DR SMR; Q3MHP5; -.
DR STRING; 9913.ENSBTAP00000011834; -.
DR PaxDb; Q3MHP5; -.
DR PeptideAtlas; Q3MHP5; -.
DR PRIDE; Q3MHP5; -.
DR Ensembl; ENSBTAT00000011834; ENSBTAP00000011834; ENSBTAG00000008990.
DR GeneID; 540161; -.
DR KEGG; bta:540161; -.
DR CTD; 4733; -.
DR VEuPathDB; HostDB:ENSBTAG00000008990; -.
DR VGNC; VGNC:53899; DRG1.
DR eggNOG; KOG1487; Eukaryota.
DR GeneTree; ENSGT00940000153340; -.
DR HOGENOM; CLU_044997_0_0_1; -.
DR InParanoid; Q3MHP5; -.
DR OMA; SAKHPGQ; -.
DR OrthoDB; 754662at2759; -.
DR TreeFam; TF105677; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000008990; Expressed in spermatocyte and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR CDD; cd01896; DRG; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR045001; DRG.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR031662; GTP-binding_2.
DR InterPro; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR PANTHER; PTHR43127; PTHR43127; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF16897; MMR_HSR1_Xtn; 1.
DR Pfam; PF02824; TGS; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; GTP-binding; Hydrolase; Hydroxylation; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y295"
FT CHAIN 2..367
FT /note="Developmentally-regulated GTP-binding protein 1"
FT /id="PRO_0000261587"
FT DOMAIN 65..290
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT DOMAIN 290..366
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 2..16
FT /note="Required for interaction with STK16"
FT /evidence="ECO:0000250|UniProtKB:Q9Y295"
FT BINDING 71..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 96..100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 248..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 271..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y295"
FT MOD_RES 22
FT /note="(3S)-3-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y295"
FT MOD_RES 100
FT /note="Phosphothreonine; by STK16"
FT /evidence="ECO:0000250|UniProtKB:Q9Y295"
SQ SEQUENCE 367 AA; 40542 MW; 4A177EA7C8E23005 CRC64;
MSSTLAKIAE IEAEMARTQK NKATAHHLGL LKARLAKLRR ELITPKGGGG GGPGEGFDVA
KTGDARIGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGVIRYKG AKIQLLDLPG
IIEGAKDGKG RGRQVIAVAR TCNLILIVLD VLKPLGHKKI IENELEGFGI RLNSKPPNIG
FKKKDKGGIN LTATCPQSEL DAETVKSILA EYKIHNADVT LRSDATADDL IDVVEGNRVY
IPCIYVLNKI DQISIEELDI IYKVPHCVPI SAHHRWNFDD LLEKIWDYLK LVRIYTKPKG
QLPDYTSPVV LPYSRTTVED FCMKIHKNLI KEFKYALVWG LSVKHNPQKV GKDHTLEDED
VIQIVKK
