RHO1_CANAL
ID RHO1_CANAL Reviewed; 198 AA.
AC O42825; A0A1D8PSB7; Q5A200;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=GTP-binding protein RHO1;
DE Flags: Precursor;
GN Name=RHO1; OrderedLocusNames=CAALFM_CR02860WA;
GN ORFNames=CaO19.10362, CaO19.2843;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9401032; DOI=10.1128/jb.179.24.7734-7741.1997;
RA Kondoh O., Tachibana Y., Ohya Y., Arisawa M., Watanabe T.;
RT "Cloning of the RHO1 gene from Candida albicans and its regulation of beta-
RT 1,3-glucan synthesis.";
RL J. Bacteriol. 179:7734-7741(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D86430; BAA24262.1; -; Genomic_DNA.
DR EMBL; CP017630; AOW31026.1; -; Genomic_DNA.
DR RefSeq; XP_715774.1; XM_710681.1.
DR AlphaFoldDB; O42825; -.
DR SMR; O42825; -.
DR BioGRID; 1225651; 3.
DR STRING; 237561.O42825; -.
DR PRIDE; O42825; -.
DR GeneID; 3642564; -.
DR KEGG; cal:CAALFM_CR02860WA; -.
DR CGD; CAL0000192659; RHO1.
DR VEuPathDB; FungiDB:CR_02860W_A; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; O42825; -.
DR OMA; RWIPEIK; -.
DR OrthoDB; 1166960at2759; -.
DR PHI-base; PHI:270; -.
DR PRO; PR:O42825; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0001411; C:hyphal tip; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0005525; F:GTP binding; IDA:CGD.
DR GO; GO:0003924; F:GTPase activity; ISS:CGD.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IMP:CGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:1900240; P:negative regulation of phenotypic switching; IMP:CGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:CGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:CGD.
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; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 3: Inferred from homology;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..195
FT /note="GTP-binding protein RHO1"
FT /id="PRO_0000198935"
FT PROPEP 196..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281265"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
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 121..124
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-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 198 AA; 21999 MW; 1E3738D13EAA1057 CRC64;
MVNGPAELRR KLVIVGDGAC GKTCLLIVFS KGTFPEVYVP TVFENYVADV EVDGRKVELA
LWDTAGQEDY DRLRPLSYPD SNVILICFSV DSPDSLDNVL EKWISEVLHF CQGVPIILVG
CKSDLRDDPH TIEALRQQQQ QPVSTSEGQQ VAQRIGAADY LECSAKTGRG VREVFEAATR
ASLRVKEKKE KKKKCVVL
