DIRA_CAEEL
ID DIRA_CAEEL Reviewed; 219 AA.
AC Q09930;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=GTP-binding protein drn-1 {ECO:0000305};
DE AltName: Full=Di-Ras/Rig/Noey2 Ras-like protein homolog {ECO:0000303|PubMed:22897658};
DE Flags: Precursor; Fragment;
GN Name=drn-1 {ECO:0000312|WormBase:C54A12.4};
GN ORFNames=C54A12.4 {ECO:0000312|WormBase:C54A12.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH EPAC-1, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLY-40 AND SER-45.
RX PubMed=22897658; DOI=10.1111/j.1365-2443.2012.01627.x;
RA Tada M., Gengyo-Ando K., Kobayashi T., Fukuyama M., Mitani S., Kontani K.,
RA Katada T.;
RT "Neuronally expressed Ras-family GTPase Di-Ras modulates synaptic activity
RT in Caenorhabditis elegans.";
RL Genes Cells 17:778-789(2012).
CC -!- FUNCTION: Displays low GTPase activity and exists predominantly in the
CC GTP-bound form (By similarity). Together with epac-1, may regulate
CC acetylcholine release at the neuromuscular junctions probably
CC downstream of G-protein gsa-1 and adenylate cyclase acy-1
CC (PubMed:22897658). {ECO:0000250|UniProtKB:Q96HU8,
CC ECO:0000269|PubMed:22897658}.
CC -!- SUBUNIT: Interacts with epac-1 (via C-terminus).
CC {ECO:0000269|PubMed:22897658}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in neurons including the
CC nerve ring, ventral and dorsal nerve cord motor neurons and tail
CC ganglia. {ECO:0000269|PubMed:22897658}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile. Resistant to paralysis
CC induced by treatment with acetylcholinesterase inhibitor aldicarb (but
CC not with acetylcholine agonist levamisole). Hypersensitivity to
CC aldicarb treatment is partially reduced in an egl-30(js126), goa-
CC 1(n1134) or gsa-1(ce94) mutant background.
CC {ECO:0000269|PubMed:22897658}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Di-Ras family.
CC {ECO:0000305}.
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DR EMBL; BX284602; CCD68002.2; -; Genomic_DNA.
DR PIR; T15833; T15833.
DR RefSeq; NP_001333544.1; NM_001346628.1.
DR AlphaFoldDB; Q09930; -.
DR SMR; Q09930; -.
DR STRING; 6239.C54A12.4.1; -.
DR PaxDb; Q09930; -.
DR PeptideAtlas; Q09930; -.
DR PRIDE; Q09930; -.
DR EnsemblMetazoa; C54A12.4.1; C54A12.4.1; WBGene00016911.
DR GeneID; 183765; -.
DR KEGG; cel:CELE_C54A12.4; -.
DR UCSC; C54A12.4; c. elegans.
DR CTD; 183765; -.
DR WormBase; C54A12.4; CE51761; WBGene00016911; drn-1.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000176101; -.
DR HOGENOM; CLU_041217_9_10_1; -.
DR InParanoid; Q09930; -.
DR OrthoDB; 1218505at2759; -.
DR PhylomeDB; Q09930; -.
DR PRO; PR:Q09930; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016911; Expressed in larva and 3 other tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN <1..216
FT /note="GTP-binding protein drn-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438305"
FT PROPEP 217..219
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000438306"
FT MOTIF 59..67
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 37..44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 56..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 85..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 146..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 177..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT MOD_RES 216
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 216
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62330"
FT MUTAGEN 40
FT /note="G->V: Probably constitutively active. Does not
FT reduce paralysis induced by aldicarb treatment."
FT /evidence="ECO:0000269|PubMed:22897658"
FT MUTAGEN 45
FT /note="S->N: Probably nucleotide-free or GDP-bound. Reduces
FT paralysis induced by aldicarb treatment."
FT /evidence="ECO:0000269|PubMed:22897658"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 23834 MW; CC593752DC3951DF CRC64;
LLDTDFSIEA TAATTTAGSG SKVAEASTSD YRVAVFGAGG VGKSSITQRF VKGTFNENYV
PTIEDTYRQV ISCNQKNVCT LQITDTTGSH QFPAMQRLSI SKGNAFILIY SVTNKQSFAE
LVPIIEMMKE VKGNAIAETP IMLVGNKKDE ESKREVSSNS GQKVATNMEC GFIETSAKNN
ENITELFQQL LALEKKRQLA LTMDDPDGKN GKKKGCHIM
