RSR1_CANAX
ID RSR1_CANAX Reviewed; 248 AA.
AC P52498;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ras-related protein RSR1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P13856};
DE Flags: Precursor;
GN Name=RSR1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 11651 / B792 / 171D;
RX PubMed=9308185; DOI=10.1099/00221287-143-9-3033;
RA Yaar L., Mevarech M., Koltin Y.;
RT "A Candida albicans RAS-related gene (CaRSR1) is involved in budding, cell
RT morphogenesis and hypha development.";
RL Microbiology 143:3033-3044(1997).
CC -!- FUNCTION: Ras-related protein which binds GDP/GTP and possesses
CC intrinsic GTPase activity (By similarity). Involved in both yeast and
CC hypha development. In the yeast phase, it is required for normal
CC (polar) bud site selection and is involved in cell morphogenesis; in
CC the yeast-mycelial transition it is involved in germ tube emergence;
CC and in the development of the hyphae it is involved in cell elongation
CC (PubMed:9308185). {ECO:0000250|UniProtKB:P13856,
CC ECO:0000269|PubMed:9308185}.
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:P13856};
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). {ECO:0000250|UniProtKB:P13856}.
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; U46158; AAB81286.1; -; Genomic_DNA.
DR AlphaFoldDB; P52498; -.
DR SMR; P52498; -.
DR VEuPathDB; FungiDB:CAWG_01560; -.
DR VEuPathDB; FungiDB:CR_02140W_A; -.
DR PHI-base; PHI:62; -.
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:2000114; P:regulation of establishment of cell polarity; IMP:CACAO.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04177; RSR1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041841; Rsr1.
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.
FT CHAIN 1..245
FT /note="Ras-related protein RSR1"
FT /id="PRO_0000082690"
FT PROPEP 246..248
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281341"
FT REGION 182..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 183..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 245
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 245
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 248 AA; 27658 MW; CD30C4112F7767DE CRC64;
MRDYKVVVLG AGGVGKSSIT VQFVQGVYVE SYDPTIEDSY RKQIEVDGRA CDLEILDTAG
VAQFTAMREL YIKSGKGFLL VYSVTDENSL KELLALREQV LRIKDSDNVP MVLVGNKCDL
EDDRVLSIED GVKVSQDWGL VPFYETSAMY KTNVDEAFID VVRQIMRKEA AISAEKKQQK
ELQKQQQQQQ QEQDAEGQQQ QQKSGKSKSS ATQKDATADG QTDVNARLKQ SINDHPKSSS
GSKFCTII
