RASG_DICDI
ID RASG_DICDI Reviewed; 189 AA.
AC P15064; Q54BT6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ras-like protein rasG;
DE EC=3.6.5.2 {ECO:0000305|PubMed:18948008};
DE Flags: Precursor;
GN Name=rasG; ORFNames=DDB_G0293434;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2644652; DOI=10.1073/pnas.86.3.938;
RA Robbins S.M., Williams J.G., Jermyn K.A., Spiegelman G.B., Weeks G.;
RT "Growing and developing Dictyostelium cells express different ras genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:938-942(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX2;
RX PubMed=1339294; DOI=10.1016/0167-4781(92)90467-e;
RA Robbins S.M., Williams J.G., Spiegelman G.B., Weeks G.;
RT "Cloning and characterization of the Dictyostelium discoideum rasG genomic
RT sequences.";
RL Biochim. Biophys. Acta 1130:85-89(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP INTERACTION WITH RIPA.
RX PubMed=10473630; DOI=10.1091/mbc.10.9.2829;
RA Lee S., Parent C.A., Insall R., Firtel R.A.;
RT "A novel Ras-interacting protein required for chemotaxis and cyclic
RT adenosine monophosphate signal relay in Dictyostelium.";
RL Mol. Biol. Cell 10:2829-2845(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLN-61.
RX PubMed=18948008; DOI=10.1016/j.cub.2008.08.069;
RA Zhang S., Charest P.G., Firtel R.A.;
RT "Spatiotemporal regulation of Ras activity provides directional sensing.";
RL Curr. Biol. 18:1587-1593(2008).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity. {ECO:0000269|PubMed:18948008}.
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; EC=3.6.5.2;
CC Evidence={ECO:0000305|PubMed:18948008};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBUNIT: Interacts with ripA. {ECO:0000269|PubMed:10473630}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; J04160; AAA33244.1; -; mRNA.
DR EMBL; Z11533; CAA77632.1; -; Genomic_DNA.
DR EMBL; AAFI02000210; EAL60719.1; -; Genomic_DNA.
DR PIR; A31456; TVDORA.
DR RefSeq; XP_629133.1; XM_629131.1.
DR AlphaFoldDB; P15064; -.
DR SMR; P15064; -.
DR IntAct; P15064; 1.
DR STRING; 44689.DDB0201663; -.
DR PaxDb; P15064; -.
DR EnsemblProtists; EAL60719; EAL60719; DDB_G0293434.
DR GeneID; 8629223; -.
DR KEGG; ddi:DDB_G0293434; -.
DR dictyBase; DDB_G0293434; rasG.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P15064; -.
DR OMA; CCSGCVV; -.
DR PhylomeDB; P15064; -.
DR Reactome; R-DDI-1169092; Activation of RAS in B cells.
DR Reactome; R-DDI-171007; p38MAPK events.
DR Reactome; R-DDI-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DDI-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DDI-9648002; RAS processing.
DR PRO; PR:P15064; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:dictyBase.
DR GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR GO; GO:0044354; C:macropinosome; IDA:dictyBase.
DR GO; GO:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031982; C:vesicle; IDA:dictyBase.
DR GO; GO:0010856; F:adenylate cyclase activator activity; IGI:dictyBase.
DR GO; GO:0003925; F:G protein activity; IDA:dictyBase.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:dictyBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0030250; F:guanylate cyclase activator activity; IMP:dictyBase.
DR GO; GO:0019900; F:kinase binding; IPI:dictyBase.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:dictyBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IDA:dictyBase.
DR GO; GO:0043130; F:ubiquitin binding; IDA:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:dictyBase.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0019954; P:asexual reproduction; IGI:dictyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0071321; P:cellular response to cGMP; IGI:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0043326; P:chemotaxis to folate; IMP:dictyBase.
DR GO; GO:0046847; P:filopodium assembly; IMP:dictyBase.
DR GO; GO:0044351; P:macropinocytosis; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:dictyBase.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:dictyBase.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; IDA:dictyBase.
DR GO; GO:1901262; P:negative regulation of sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:1903666; P:positive regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; IMP:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:dictyBase.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:dictyBase.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IMP:dictyBase.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:dictyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:dictyBase.
DR GO; GO:0046586; P:regulation of calcium-dependent cell-cell adhesion; IMP:dictyBase.
DR GO; GO:1905169; P:regulation of protein localization to phagocytic vesicle; IMP:dictyBase.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:dictyBase.
DR GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
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; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..186
FT /note="Ras-like protein rasG"
FT /id="PRO_0000082663"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281311"
FT REGION 169..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 186
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 186
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 61
FT /note="Q->L: Constitutively active."
FT /evidence="ECO:0000269|PubMed:18948008"
SQ SEQUENCE 189 AA; 21333 MW; AFB502319C090899 CRC64;
MTEYKLVIVG GGGVGKSALT IQLIQNHFID EYDPTIEDSY RKQVTIDEET CLLDILDTAG
QEEYSAMRDQ YMRTGQGFLC VYSITSRSSF DEIASFREQI LRVKDKDRVP MIVVGNKCDL
ESDRQVTTGE GQDLAKSFGS PFLETSAKIR VNVEEAFYSL VREIRKDLKG DSKPEKGKKK
RPLKACTLL
