ID   RAS2_MUCCL              Reviewed;         198 AA.
AC   P22279;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Ras-like protein 2;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE   Flags: Precursor;
GN   Name=RAS2;
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: No transcripts for RAS2 were detected in any
CC       developmental stage.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; M55176; AAA83994.1; -; Genomic_DNA.
DR   PIR; B36365; B36365.
DR   AlphaFoldDB; P22279; -.
DR   SMR; P22279; -.
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..195
FT                   /note="Ras-like protein 2"
FT                   /id="PRO_0000082680"
FT   PROPEP          196..198
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281323"
FT   MOTIF           40..48
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         65..69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         124..127
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         195
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           195
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  22782 MW;  60BF7EDA4B679352 CRC64;
     MSTKGAAFLK EYKIVMVGDG GVGKSAMTIQ FIQSTFVDEY DPTIEDSYRK QCLIDSECAM
     LDILDTAGQE EYSAMRERFM RNGEGFVLIY SITSYHTFEQ VQKLHEQIAR VKDLEHFPMV
     LVGNKCDLEQ DRQVPTSAGR DLAKQYNCQF FEASAKQNVR IQDAFHGLVR EIRRSQQEKC
     KKQKQYDEKQ ASLCCIVM