DRG1_XENLA
ID DRG1_XENLA Reviewed; 367 AA.
AC P43690;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Developmentally-regulated GTP-binding protein 1;
DE Short=DRG-1;
DE Short=xDRG;
DE AltName: Full=Translation factor GTPase DRG1;
DE Short=TRAFAC GTPase DRG1;
DE EC=3.6.5.-;
GN Name=drg1; Synonyms=drg;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8179998;
RA Kumar S., Iwao M., Yamagishi T., Noda M., Asashima M.;
RT "Expression of GTP-binding protein gene drg during Xenopus laevis
RT development.";
RL Int. J. Dev. Biol. 37:539-546(1993).
RN [2]
RP DEVELOPMENTAL STAGE.
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 [3]
RP FUNCTION, AND MUTAGENESIS OF PRO-73 AND SER-78.
RX PubMed=28855639; DOI=10.1038/s41598-017-10088-5;
RA Schellhaus A.K., Moreno-Andres D., Chugh M., Yokoyama H., Moschopoulou A.,
RA De S., Bono F., Hipp K., Schaeffer E., Antonin W.;
RT "Developmentally Regulated GTP binding protein 1 (DRG1) controls
RT microtubule dynamics.";
RL Sci. Rep. 7:9996-9996(2017).
CC -!- FUNCTION: Catalyzes the conversion of GTP to GDP through hydrolysis of
CC the gamma-phosphate bond in GTP (By similarity). Binds to microtubules
CC and promotes microtubule polymerization and bundling. GTPase activity
CC is not necessary for these microtubule-related functions
CC (PubMed:28855639). {ECO:0000250|UniProtKB:Q9Y295,
CC ECO:0000269|PubMed:28855639}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9Y295};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q9Y295};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y295}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y295}.
CC -!- TISSUE SPECIFICITY: Expressed in many adult amd embryonic tissues. In
CC adults, highest levels in ovaries and testes, followed by skeletal
CC muscle, stomach, brain, kidney and liver. Weak expression in heart and
CC brain. {ECO:0000269|PubMed:8179998}.
CC -!- DEVELOPMENTAL STAGE: At stage 22, expressed in blood islands, somites,
CC eyes, trunk neural crest, mandibular crest segment, hyoid crest segment
CC and branchial crest segment. At stage 32, expressed in otic vesicle,
CC pronephros, forebraiin, midbrain, hindbrain, branchial arch, eyes,
CC lens, spinal cord and notochord. {ECO:0000269|PubMed:15676025,
CC ECO:0000269|PubMed:8179998}.
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; D13865; BAA02978.1; -; mRNA.
DR PIR; I51426; I51426.
DR RefSeq; NP_001084013.1; NM_001090544.1.
DR AlphaFoldDB; P43690; -.
DR SMR; P43690; -.
DR BioGRID; 100578; 1.
DR IntAct; P43690; 1.
DR MaxQB; P43690; -.
DR DNASU; 399253; -.
DR GeneID; 399253; -.
DR KEGG; xla:399253; -.
DR CTD; 399253; -.
DR Xenbase; XB-GENE-980759; drg1.L.
DR OMA; SAKHPGQ; -.
DR OrthoDB; 754662at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 399253; Expressed in ovary and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; IDA:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA: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 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..367
FT /note="Developmentally-regulated GTP-binding protein 1"
FT /id="PRO_0000205426"
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 MUTAGEN 73
FT /note="P->V: Does not affect the microtubule-related
FT activities, including binding and tubulin polymerization."
FT /evidence="ECO:0000269|PubMed:28855639"
FT MUTAGEN 78
FT /note="S->N: Does not affect the microtubule-related
FT activities, including binding and tubulin polymerization."
FT /evidence="ECO:0000269|PubMed:28855639"
SQ SEQUENCE 367 AA; 40415 MW; 27189D72BA3A2386 CRC64;
MSGTLARIAE IEAEMARTQK NKATAYHLGL LKARLAKLRR ELITPKGGGG GGPGEGFDVA
KTGDARIGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGVVRYKG AKIQLLDLPG
IIEGAKDGKG RGRQVIAVAR TCNLILIVLD VLKPLGHKKI IENELEGFGI RLNKQPPNIG
FKKKDKGGIN LTATCAQSEL DNDTVKSILA EYKIHNADIT LRSDATADDL IDVVEGNRVY
IPCIYVLNKI DQISIEELDI IYKVPHCVPI SAHHRWNFDD LLEKIWDYLQ LVRIYTKPKG
QLPDYTSPVV LPCSHTAAED FCTKIHKNLI KEFKYALVWG SSVKHNPQKV GKDHVLEDED
VIQIVKK
