RAS_CRYNJ
ID RAS_CRYNJ Reviewed; 216 AA.
AC P0CQ42; O74650; Q560H3; Q5KPH2; Q9HFU0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Ras-like protein;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
GN Name=RAS1; Synonyms=RAS; OrderedLocusNames=CNA02810;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10455236;
RX DOI=10.1002/(sici)1097-0061(199908)15:11<1133::aid-yea438>3.0.co;2-n;
RA Tanaka K., Nambu H., Katoh Y., Kai M., Hidaka Y.;
RT "Molecular cloning of homologs of RAS and RHO1 genes from Cryptococcus
RT neoformans.";
RL Yeast 15:1133-1139(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=12553941; DOI=10.1016/s1087-1845(02)00518-2;
RA Waugh M.S., Vallim M.A., Heitman J., Alspaugh J.A.;
RT "Ras1 controls pheromone expression and response during mating in
RT Cryptococcus neoformans.";
RL Fungal Genet. Biol. 38:110-121(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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:P01112};
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; AB017640; BAA33397.1; -; mRNA.
DR EMBL; AF294647; AAG25584.1; -; Genomic_DNA.
DR EMBL; AE017341; AAW40866.1; -; Genomic_DNA.
DR RefSeq; XP_566685.1; XM_566685.1.
DR AlphaFoldDB; P0CQ42; -.
DR SMR; P0CQ42; -.
DR STRING; 5207.AAW40866; -.
DR PaxDb; P0CQ42; -.
DR EnsemblFungi; AAW40866; AAW40866; CNA02810.
DR GeneID; 3253597; -.
DR KEGG; cne:CNA02810; -.
DR VEuPathDB; FungiDB:CNA02810; -.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_0_1; -.
DR InParanoid; P0CQ42; -.
DR OMA; CCSGCVV; -.
DR OrthoDB; 1259506at2759; -.
DR Proteomes; UP000002149; 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 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; Palmitate; Prenylation; Reference proteome.
FT CHAIN 1..213
FT /note="Ras-like protein"
FT /id="PRO_0000082674"
FT PROPEP 214..216
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281329"
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 213
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 209
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 210
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 75
FT /note="E -> D (in Ref. 2; AAG25584)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="S -> P (in Ref. 2; AAG25584)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..181
FT /note="Missing (in Ref. 2; AAG25584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24252 MW; A7B7DF8FF8B87F71 CRC64;
MSKAQFLREY KLVVVGGGGV GKSALTIQFI QSHFVDEYDP TIEDSYRKQC IIDEEVALLD
VLDTAGQEEY GAMREQYMRT GEGFLLVYSI TSRSSFEEVS TFHQQILRVK DKDYFPVVVV
ANKCDLEYER QVQPHEGRDL AKRFNAQCIE TSAKQRVNVD EAFIAVVRAI RRYQKESGPP
QAVNAPAKSQ MSAVGGRAAE KDDHVDKGCC RGCVVL
