RASB_DICDI
ID RASB_DICDI Reviewed; 197 AA.
AC P32252; Q54CB9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ras-like protein rasB;
DE EC=3.6.5.2 {ECO:0000305|PubMed:18948008};
DE Flags: Precursor;
GN Name=rasB; ORFNames=DDB_G0292998;
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=8455930;
RA Daniel J.M., Spiegelman G.B., Weeks G.;
RT "Characterization of a third ras gene, rasB, that is expressed throughout
RT the growth and development of Dictyostelium discoideum.";
RL Oncogene 8:1041-1047(1993).
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).
RN [3]
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 [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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; M96622; AAA33246.1; -; mRNA.
DR EMBL; AAFI02000199; EAL60851.1; -; Genomic_DNA.
DR RefSeq; XP_629300.1; XM_629298.1.
DR AlphaFoldDB; P32252; -.
DR SMR; P32252; -.
DR STRING; 44689.DDB0201661; -.
DR PaxDb; P32252; -.
DR PRIDE; P32252; -.
DR EnsemblProtists; EAL60851; EAL60851; DDB_G0292998.
DR GeneID; 8629023; -.
DR KEGG; ddi:DDB_G0292998; -.
DR dictyBase; DDB_G0292998; rasB.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P32252; -.
DR OMA; QSRAQQW; -.
DR PhylomeDB; P32252; -.
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:P32252; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005938; C:cell cortex; 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:0016363; C:nuclear matrix; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; 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; ISS:dictyBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0032466; P:negative regulation of cytokinesis; IMP:dictyBase.
DR GO; GO:0045806; P:negative regulation of endocytosis; IMP:dictyBase.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IMP:dictyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IMP:dictyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IEP:dictyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:dictyBase.
DR GO; GO:0043520; P:regulation of myosin II filament assembly; IDA:dictyBase.
DR GO; GO:1905169; P:regulation of protein localization to phagocytic vesicle; 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..194
FT /note="Ras-like protein rasB"
FT /id="PRO_0000082660"
FT PROPEP 195..197
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281308"
FT MOTIF 35..43
FT /note="Effector region"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 194
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 194
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 197 AA; 22268 MW; A3D8D3C6846BD9F4 CRC64;
MSVSNEYKLV VMGGGGVGKS ALTIQFIQNH FIEEYDPTIE DSYRRQCQVD EDTCLLDILD
TAGQDDYSAM RDQYMRTGQG FLCVYDVTSR TSFEEINVVR EQIIRVKDND KVPIVLVGNK
CDLENLREVT EGEGSELAKS FSVPFLETSA KKRLNVDECF FEVVREIKKS LKEPGRSKKD
KKGGILKKFK GGDCLIL
