DRG2_MOUSE
ID DRG2_MOUSE Reviewed; 364 AA.
AC Q9QXB9; Q5SX94;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Developmentally-regulated GTP-binding protein 2;
DE Short=DRG-2;
DE AltName: Full=Translation factor GTPase DRG2;
DE Short=TRAFAC GTPase DRG2;
DE EC=3.6.5.-;
GN Name=Drg2;
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 [MRNA].
RX PubMed=10760581; DOI=10.1016/s0167-4781(00)00025-7;
RA Li B., Trueeb B.;
RT "DRG represents a family of two closely related GTP-binding proteins.";
RL Biochim. Biophys. Acta 1491:196-204(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP INTERACTION WITH RWDD1, AND UBIQUITINATION.
RX PubMed=15676025; DOI=10.1111/j.1365-2443.2005.00825.x;
RA Ishikawa K., Azuma S., Ikawa S., Semba K., Inoue J.;
RT "Identification of DRG family regulatory proteins (DFRPs): specific
RT regulation of DRG1 and DRG2.";
RL Genes Cells 10:139-150(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the conversion of GTP to GDP through hydrolysis of
CC the gamma-phosphate bond in GTP. When hydroxylated at C-3 of 'Lys-21'
CC by JMJD7, may bind to RNA and play a role in translation.
CC {ECO:0000250|UniProtKB:P55039}.
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:P55039};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P55039};
CC -!- SUBUNIT: Interacts with RWDD1; this interaction confers protection to
CC polyubiquitination and proteolytic degradation (PubMed:15676025).
CC Interacts with JMJD7; this interaction is direct (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P55039,
CC ECO:0000269|PubMed:15676025}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55039}. Cytoplasm
CC {ECO:0000250|UniProtKB:P55039}.
CC -!- TISSUE SPECIFICITY: Fairly high levels in liver, heart, kidney, and
CC brain. Very low levels in lung, spleen, testis and skeletal muscle.
CC -!- PTM: Polyubiquitinated. {ECO:0000305|PubMed:15676025}.
CC -!- PTM: Hydroxylated (with S stereochemistry) at C-3 of Lys-21 by JMJD7.
CC {ECO:0000250|UniProtKB:P55039}.
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; AJ243590; CAB65258.1; -; mRNA.
DR EMBL; AL596090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082564; AAH82564.1; -; mRNA.
DR CCDS; CCDS24791.1; -.
DR RefSeq; NP_067329.1; NM_021354.1.
DR AlphaFoldDB; Q9QXB9; -.
DR SMR; Q9QXB9; -.
DR BioGRID; 199311; 13.
DR IntAct; Q9QXB9; 2.
DR MINT; Q9QXB9; -.
DR STRING; 10090.ENSMUSP00000018568; -.
DR iPTMnet; Q9QXB9; -.
DR PhosphoSitePlus; Q9QXB9; -.
DR SwissPalm; Q9QXB9; -.
DR EPD; Q9QXB9; -.
DR MaxQB; Q9QXB9; -.
DR PaxDb; Q9QXB9; -.
DR PeptideAtlas; Q9QXB9; -.
DR PRIDE; Q9QXB9; -.
DR ProteomicsDB; 279486; -.
DR Antibodypedia; 1408; 135 antibodies from 21 providers.
DR DNASU; 13495; -.
DR Ensembl; ENSMUST00000018568; ENSMUSP00000018568; ENSMUSG00000020537.
DR GeneID; 13495; -.
DR KEGG; mmu:13495; -.
DR UCSC; uc007jfy.1; mouse.
DR CTD; 1819; -.
DR MGI; MGI:1342307; Drg2.
DR VEuPathDB; HostDB:ENSMUSG00000020537; -.
DR eggNOG; KOG1486; Eukaryota.
DR GeneTree; ENSGT00940000153340; -.
DR HOGENOM; CLU_044997_0_0_1; -.
DR InParanoid; Q9QXB9; -.
DR OMA; VCDQVHR; -.
DR OrthoDB; 754662at2759; -.
DR PhylomeDB; Q9QXB9; -.
DR TreeFam; TF105706; -.
DR BioGRID-ORCS; 13495; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Drg2; mouse.
DR PRO; PR:Q9QXB9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QXB9; protein.
DR Bgee; ENSMUSG00000020537; Expressed in ear vesicle and 250 other tissues.
DR Genevisible; Q9QXB9; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Hydroxylation; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..364
FT /note="Developmentally-regulated GTP-binding protein 2"
FT /id="PRO_0000205428"
FT DOMAIN 63..288
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT DOMAIN 288..363
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 69..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 94..98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 246..249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 269..271
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT MOD_RES 21
FT /note="(3S)-3-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P55039"
SQ SEQUENCE 364 AA; 40718 MW; 932353C8FF257BE8 CRC64;
MGILEKISEI EKEIARTQKN KATEYHLGLL KAKLAKYRAQ LLEPSKSASS KGEGFDVMKS
GDARVALIGF PSVGKSTFLS LMTSTASEAA SYEFTTLTCI PGVIEYKGAN IQLLDLPGII
EGAAQGRGRG RQVIAVARTA DVVVMMLDAT KGDVQRSLLE KELESVGIRL NKHKPNIYFK
PKKGGGISFN STVTLTQCSE KLVQLILHEY KIFNAEVLFR EDCSPDDFID VIVGNRVYMP
CLYVYNKIDQ ISMEEVDRLA RKPNSVVISC GMKLNLDYLL EMLWEYLALT CIYTKKRGQR
PDFTDAIILR KGASVEHVCH RIHRSLASQF KYALVWGTST KYSPQRVGLT HTMEHEDVIQ
IVKK
