RAPC_DICDI
ID RAPC_DICDI Reviewed; 278 AA.
AC Q55BW0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ras-related protein rapC;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P10114};
DE Flags: Precursor;
GN Name=rapC; ORFNames=DDB_G0270340;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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 -!- 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:P10114};
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; AAFI02000005; EAL72520.1; -; Genomic_DNA.
DR RefSeq; XP_646721.1; XM_641629.1.
DR AlphaFoldDB; Q55BW0; -.
DR SMR; Q55BW0; -.
DR STRING; 44689.DDB0229440; -.
DR PaxDb; Q55BW0; -.
DR EnsemblProtists; EAL72520; EAL72520; DDB_G0270340.
DR GeneID; 8617693; -.
DR KEGG; ddi:DDB_G0270340; -.
DR dictyBase; DDB_G0270340; rapC.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_0_1; -.
DR InParanoid; Q55BW0; -.
DR OMA; GDEQCCS; -.
DR PhylomeDB; Q55BW0; -.
DR Reactome; R-DDI-170968; Frs2-mediated activation.
DR Reactome; R-DDI-354192; Integrin signaling.
DR Reactome; R-DDI-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-DDI-392517; Rap1 signalling.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q55BW0; -.
DR Proteomes; UP000002195; Chromosome 1.
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:0010812; P:negative regulation of cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:dictyBase.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:dictyBase.
DR GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 3: Inferred from homology;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..275
FT /note="Ras-related protein rapC"
FT /id="PRO_0000368236"
FT PROPEP 276..278
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000369262"
FT REGION 176..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..40
FT /note="Effector region"
FT COMPBIAS 180..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..17
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 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 275
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 275
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 278 AA; 30710 MW; C4F9D4FEE3BF7E6D CRC64;
MQTYKVVVLG ASGTGKTSLT VRFVNGDFVE TYDPTIEDLY RKVIETNKGE HIMLEIMDTS
GTERYLAMRD LYIRNAQAFV LVYSITSRVS LLELENIKNY ICQVKDRPIS QIPMVVLGNK
CDLEDTRVVF PEEVEALTKK WGIEDFLETS AKIDMNIQSA YDCLTLQLMS KQSFLNGSSN
GKDKKDKKEK KTHKKDSGSN NSSINSSSSS LSVSGGSNLS ISSSCSSSSF SNLSNSTSST
SVNNLNQSQT NAPIRTKSKR SLKSAKVDKN PKGKCLIM
