RASZ_DICDI
ID RASZ_DICDI Reviewed; 214 AA.
AC Q55CA9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ras-like protein rasZ;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P32253};
DE Flags: Precursor;
GN Name=rasZ; ORFNames=DDB_G0270140;
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 -!- 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; AAFI02000005; EAL72420.1; -; Genomic_DNA.
DR RefSeq; XP_646572.1; XM_641480.1.
DR AlphaFoldDB; Q55CA9; -.
DR SMR; Q55CA9; -.
DR STRING; 44689.DDB0229435; -.
DR PaxDb; Q55CA9; -.
DR EnsemblProtists; EAL72420; EAL72420; DDB_G0270140.
DR GeneID; 8617541; -.
DR KEGG; ddi:DDB_G0270140; -.
DR dictyBase; DDB_G0270140; rasZ.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q55CA9; -.
DR OMA; IVNFHTQ; -.
DR PhylomeDB; Q55CA9; -.
DR PRO; PR:Q55CA9; -.
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:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; HEP: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 3: Inferred from homology;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..211
FT /note="Ras-like protein rasZ"
FT /id="PRO_0000365571"
FT PROPEP 212..214
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000365572"
FT MOTIF 38..46
FT /note="Effector region"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 211
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 214 AA; 24751 MW; 3C42DCEBFC912174 CRC64;
MASYKNNNLV RLCIMGDGGV GKTAVTIQFI SNHFVYYYDP TIEDSYRKQC VIDDQVYMLD
ILDTAGQDEL TAMRDQWIRS CEGFVLVYSI TSRSSFDQVQ FFREQIIRVL DRDDVPIMMI
GNKSDLDDER QVTYQEGKDL ARCLGMSFME VSAKSRANIE EVFNETVRSV KRREESLLKK
DKSKDGKDIK KKNSIIKKLN QKVNNTKTSI CKMM
