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RASC_DICDI
ID   RASC_DICDI              Reviewed;         189 AA.
AC   P32253; Q54TX8;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Ras-like protein rasC;
DE            EC=3.6.5.2 {ECO:0000305|PubMed:18948008};
DE   Flags: Precursor;
GN   Name=rasC; ORFNames=DDB_G0281385;
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].
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).
RN   [3]
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: Maximally expressed during early aggregation.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; Z18926; CAA79359.1; -; Genomic_DNA.
DR   EMBL; AAFI02000041; EAL66674.1; -; Genomic_DNA.
DR   PIR; S31985; S31985.
DR   RefSeq; XP_640683.1; XM_635591.1.
DR   AlphaFoldDB; P32253; -.
DR   SMR; P32253; -.
DR   STRING; 44689.DDB0214827; -.
DR   PaxDb; P32253; -.
DR   EnsemblProtists; EAL66674; EAL66674; DDB_G0281385.
DR   GeneID; 8623068; -.
DR   KEGG; ddi:DDB_G0281385; -.
DR   dictyBase; DDB_G0281385; rasC.
DR   eggNOG; KOG0395; Eukaryota.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; P32253; -.
DR   OMA; AQWVILD; -.
DR   PhylomeDB; P32253; -.
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:P32253; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0031252; C:cell leading edge; IC:dictyBase.
DR   GO; GO:0005811; C:lipid droplet; HDA:dictyBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:1904841; F:TORC2 complex binding; IDA:dictyBase.
DR   GO; GO:0030036; P:actin cytoskeleton organization; 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:0048870; P:cell motility; 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:0007163; P:establishment or maintenance of cell polarity; IMP:dictyBase.
DR   GO; GO:0120320; P:lateral pseudopodium retraction; IMP:dictyBase.
DR   GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR   GO; GO:0110094; P:polyphosphate-mediated signaling; 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; IGI:dictyBase.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:dictyBase.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:dictyBase.
DR   GO; GO:0061122; P:positive regulation of positive chemotaxis to cAMP; IMP:dictyBase.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:dictyBase.
DR   GO; GO:1904515; P:positive regulation of TORC2 signaling; IDA:dictyBase.
DR   GO; GO:0051291; P:protein heterooligomerization; IDA:dictyBase.
DR   GO; GO:0043491; P:protein kinase B signaling; IMP:dictyBase.
DR   GO; GO:0007265; P:Ras protein signal transduction; IDA:dictyBase.
DR   GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR   GO; GO:0001558; P:regulation of cell growth; IMP:dictyBase.
DR   GO; GO:0051602; P:response to electrical stimulus; IMP:dictyBase.
DR   GO; GO:0007165; P:signal transduction; 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..186
FT                   /note="Ras-like protein rasC"
FT                   /id="PRO_0000082661"
FT   PROPEP          187..189
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281309"
FT   MOTIF           33..41
FT                   /note="Effector region"
FT   BINDING         11..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         58..62
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..120
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"
SQ   SEQUENCE   189 AA;  21496 MW;  AA963BCAED409775 CRC64;
     MSKLLKLVIV GDGGVGKSAL TIQLTQNQFI AEYDPTIENS YRKQVNIDEE VYMLDILDTA
     GQEEYSAMRD QYIRSGRGFL IVYSIISRAS FEAVTTFREQ ILRVKDLSTY PIVIIGNKAD
     LPDKDRKVPP MEGKELAKSF GAPFLETSAK SRVNVEEAFF TLVREIKRWN QNPQNEEMLP
     PKKRGCIIL
 
 
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