RASD_DICDI
ID RASD_DICDI Reviewed; 187 AA.
AC P03967; Q54C81;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ras-like protein rasD;
DE EC=3.6.5.2 {ECO:0000305|PubMed:18948008};
DE AltName: Full=Transforming protein p23 homolog;
DE Flags: Precursor;
GN Name=rasD; Synonyms=ras, rasA; ORFNames=DDB_G0292996;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=6091907; DOI=10.1016/0092-8674(84)90199-5;
RA Reymond C.D., Gomer R.H., Mehdy M.C., Firtel R.A.;
RT "Developmental regulation of a Dictyostelium gene encoding a protein
RT homologous to mammalian ras protein.";
RL Cell 39:141-148(1984).
RN [2]
RP SEQUENCE REVISION TO 137-143.
RC STRAIN=AX3;
RX PubMed=1703508; DOI=10.1101/gad.5.1.9;
RA Esch R.K., Firtel R.A.;
RT "cAMP and cell sorting control the spatial expression of a developmentally
RT essential cell-type-specific ras gene in Dictyostelium.";
RL Genes Dev. 5:9-21(1991).
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 FUNCTION, AND CATALYTIC ACTIVITY.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed at a low level in vegetative cells; not
CC expressed between the onset of development and aggregation, and is then
CC re-expressed in the multicellular aggregate stages.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; Z11804; CAA77848.1; -; Genomic_DNA.
DR EMBL; AAFI02000199; EAL60850.1; -; Genomic_DNA.
DR PIR; A01371; TVDORS.
DR RefSeq; XP_629338.1; XM_629336.1.
DR AlphaFoldDB; P03967; -.
DR SMR; P03967; -.
DR STRING; 44689.DDB0216195; -.
DR PaxDb; P03967; -.
DR ABCD; P03967; 1 sequenced antibody.
DR EnsemblProtists; EAL60850; EAL60850; DDB_G0292996.
DR GeneID; 8629062; -.
DR KEGG; ddi:DDB_G0292996; -.
DR dictyBase; DDB_G0292996; rasD.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P03967; -.
DR OMA; QCVIDDI; -.
DR PhylomeDB; P03967; -.
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:P03967; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005829; C:cytosol; TAS:dictyBase.
DR GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
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:0004860; F:protein kinase inhibitor activity; IMP:dictyBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IMP:dictyBase.
DR GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0000165; P:MAPK cascade; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:dictyBase.
DR GO; GO:0042331; P:phototaxis; IMP:dictyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0043052; P:thermotaxis; IMP: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..184
FT /note="Ras-like protein rasD"
FT /id="PRO_0000082662"
FT PROPEP 185..187
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281310"
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 184
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 184
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 187 AA; 21202 MW; 7F526253B8316678 CRC64;
MTEYKLVIVG GGGVGKSALT IQLIQNHFID EYDPTIEDSY RKQVSIDDET CLLDILDTAG
QEEYSAMRDQ YMRTGQGFLC VYSITSRSSY DEIASFREQI LRVKDKDRVP LILVGNKADL
DHERQVSVNE GQELAKGFNC PFMESSAKSR INVEEAFYSL VREIRKELKG DQSSGKAQKK
KKQCLIL
