RASS_DICDI
ID RASS_DICDI Reviewed; 194 AA.
AC P32254; Q54QW0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ras-like protein rasS;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P32253};
DE Flags: Precursor;
GN Name=rasS; ORFNames=DDB_G0283537;
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=8290260;
RA Daniel J.M., Bush J., Cardelli J., Spiegelman G.B., Weeks G.;
RT "Isolation of two novel ras genes in Dictyostelium discoideum; evidence for
RT a complex, developmentally regulated ras gene subfamily.";
RL Oncogene 9:501-508(1994).
RN [2]
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).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity. {ECO:0000250|UniProtKB:P32253}.
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:0000250|UniProtKB:P32253};
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; Z14134; CAA78508.1; -; mRNA.
DR EMBL; AAFI02000055; EAL65646.1; -; Genomic_DNA.
DR PIR; S31410; S31410.
DR RefSeq; XP_639024.1; XM_633932.1.
DR AlphaFoldDB; P32254; -.
DR SMR; P32254; -.
DR IntAct; P32254; 1.
DR STRING; 44689.DDB0191147; -.
DR PaxDb; P32254; -.
DR EnsemblProtists; EAL65646; EAL65646; DDB_G0283537.
DR GeneID; 8624152; -.
DR KEGG; ddi:DDB_G0283537; -.
DR dictyBase; DDB_G0283537; rasS.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P32254; -.
DR OMA; CVYSITY; -.
DR PhylomeDB; P32254; -.
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:P32254; -.
DR Proteomes; UP000002195; Chromosome 4.
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; ISS:dictyBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0044351; P:macropinocytosis; IMP:dictyBase.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:dictyBase.
DR GO; GO:2000146; P:negative regulation of cell motility; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:dictyBase.
DR GO; GO:1905303; P:positive regulation of macropinocytosis; IMP:dictyBase.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:dictyBase.
DR GO; GO:0019953; P:sexual reproduction; IEP: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 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..191
FT /note="Ras-like protein rasS"
FT /id="PRO_0000082664"
FT PROPEP 192..194
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281312"
FT REGION 168..194
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 191
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 191
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 194 AA; 22266 MW; AF4C1BD37B938B59 CRC64;
MFNFKLVLVG PGGVGKSCLT IQFIAQKFVD EYDPTLEDSY RKQTTVDGEE CLLDIYDTAG
QEDFSAVRDQ YMRTGEGFLC VYSITYLQSF KEIHRLHNHL LKVKDLDSVP FVLVGNKCDL
NEYREVSTAE GEELAKKLNC KFLETSAKER INVSESFYEL VREVKKARQS NQHSNSQEQN
TDQPIKKKKS CNLL
