RAS1_MUCCL
ID RAS1_MUCCL Reviewed; 203 AA.
AC P22278;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ras-like protein 1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
GN Name=RAS1;
OS Mucor circinelloides f. lusitanicus (Mucor racemosus var. lusitanicus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=29924;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 1216b / BCRC 32522 / CBS 277.49 / NRRL 3631;
RX PubMed=1701021; DOI=10.1128/mcb.10.12.6654-6663.1990;
RA Casale W.L., McConnell D.G., Wang S.-Y., Lee Y.-J., Linz J.E.;
RT "Expression of a gene family in the dimorphic fungus Mucor racemosus which
RT exhibits striking similarity to human ras genes.";
RL Mol. Cell. Biol. 10:6654-6663(1990).
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; Lipid-anchor.
CC -!- DEVELOPMENTAL STAGE: In all developmental stages analyzed. Its signal
CC was more intense in sporulating mycelium.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; M55175; AAA83378.1; -; Genomic_DNA.
DR PIR; A36365; A36365.
DR AlphaFoldDB; P22278; -.
DR SMR; P22278; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation.
FT CHAIN 1..200
FT /note="Ras-like protein 1"
FT /id="PRO_0000082679"
FT PROPEP 201..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281322"
FT MOTIF 39..47
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 200
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 200
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 203 AA; 23236 MW; 52098F53F3966A54 CRC64;
MSKASSFVRE YKLVMVGGGG VGKSALTIQF IQSHFVDEYD PTIEDSYRKQ CVIDSETALL
DVLDTAGQEE YSAMREQYMR NGEGFLLVYS ITSRLSFEEI TTFYQQICRV KDRDYFPMVL
VGNKCDLEGD RQVSSQEGRD LAKNFGCQFI ETSAKQRINV DEAFFEVVRD IRRYNKEQET
RGHDQFGIQD APDVASDKCC ILM