RAS1_NEUCR
ID RAS1_NEUCR Reviewed; 213 AA.
AC P22126; Q7RVX3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein ras-1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
GN Name=ras-1; Synonyms=ras; ORFNames=NCU08823;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=74-ORS-6a / FGSC 4200;
RX PubMed=2146163; DOI=10.1016/0014-5793(90)81061-r;
RA Altschuler D.L., Muro A., Schijman A., Almonacid F.B., Torres H.N.;
RT "Neurospora crassa cDNA clones coding for a new member of the ras protein
RT family.";
RL FEBS Lett. 273:103-106(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ito S., Sugisaki M., Inoue H.;
RT "Analyses of structure and function of NC-ras gene of Neurospora crassa.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-70.
RC TISSUE=Mycelium;
RA Lee C.-W., Lee E.J.;
RT "Structural analysis of ras genes from filamentous fungi.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity.
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 -!- 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; X53533; CAA37612.1; -; mRNA.
DR EMBL; AB016991; BAA32498.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA32627.2; -; Genomic_DNA.
DR EMBL; U33746; AAA74986.1; -; Genomic_DNA.
DR PIR; S12892; S12892.
DR PIR; T47196; T47196.
DR RefSeq; XP_961863.2; XM_956770.3.
DR AlphaFoldDB; P22126; -.
DR SMR; P22126; -.
DR STRING; 5141.EFNCRP00000008765; -.
DR EnsemblFungi; EAA32627; EAA32627; NCU08823.
DR GeneID; 3878011; -.
DR KEGG; ncr:NCU08823; -.
DR VEuPathDB; FungiDB:NCU08823; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P22126; -.
DR OMA; CCSGCVV; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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; Prenylation; Reference proteome.
FT CHAIN 1..210
FT /note="Protein ras-1"
FT /id="PRO_0000082704"
FT PROPEP 211..213
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281358"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 210
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 210
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 213 AA; 24026 MW; 4DFD3B3C6DDC0D9B CRC64;
MANKFTREYK LVVVGGGGVG KSCLTIQLIQ GHFLDEYDPT IEDSYRKQCT IDNEVALLDI
LDTAGQEEYS AMREQYMRTG EGFLLVFAIN SRESFEEIRI YQQQILRVKD RDSFPMIIVG
NKYDLRGERV VSEQEGQALA AEFGTKYIET SAKTQHNVEN AFYDLVREIR KEDKKLGEKV
GGTSFANNNG AVKQMDVGDE DVQAGCCAKC IMM
