RHO3_ASHGO
ID RHO3_ASHGO Reviewed; 224 AA.
AC Q9HF51;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=GTP-binding protein RHO3;
DE Flags: Precursor;
GN Name=RHO3; OrderedLocusNames=ADL252W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11156982; DOI=10.1093/genetics/157.2.601;
RA Wendland J., Philippsen P.;
RT "Cell polarity and hyphal morphogenesis are controlled by multiple rho-
RT protein modules in the filamentous ascomycete Ashbya gossypii.";
RL Genetics 157:601-610(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Involved in the regulation of actin polarization. Rho
CC proteins are required for distinct steps during polarized hyphal growth
CC of A.gossypii. {ECO:0000269|PubMed:11156982}.
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}.
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DR EMBL; AF210629; AAG41252.1; -; Genomic_DNA.
DR EMBL; AE016817; AAS51668.1; -; Genomic_DNA.
DR RefSeq; NP_983844.1; NM_209197.1.
DR AlphaFoldDB; Q9HF51; -.
DR SMR; Q9HF51; -.
DR STRING; 33169.AAS51668; -.
DR EnsemblFungi; AAS51668; AAS51668; AGOS_ADL252W.
DR GeneID; 4619979; -.
DR KEGG; ago:AGOS_ADL252W; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q9HF51; -.
DR OMA; MPLCGGS; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005933; C:cellular bud; IEA:EnsemblFungi.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; 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:0019901; F:protein kinase binding; IBA:GO_Central.
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:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IEA:EnsemblFungi.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IEA:EnsemblFungi.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:EnsemblFungi.
DR GO; GO:0045921; P:positive regulation of exocytosis; IEA:EnsemblFungi.
DR GO; GO:0090338; P:positive regulation of formin-nucleated actin cable assembly; IEA:EnsemblFungi.
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:0010590; P:regulation of septum digestion after cytokinesis; IEA:EnsemblFungi.
DR GO; GO:0007264; P:small GTPase mediated 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; 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..221
FT /note="GTP-binding protein RHO3"
FT /id="PRO_0000198933"
FT PROPEP 222..224
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT /id="PRO_0000281263"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..52
FT /note="Effector region"
FT BINDING 22..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 69..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20171"
FT BINDING 127..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT MOD_RES 221
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT LIPID 221
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62745"
SQ SEQUENCE 224 AA; 24490 MW; 723B7FB92C077E8B CRC64;
MPLCGSSSSS KHPIERKIVI LGDGACGKTS LLNVFTRGYF PKVYEPTVFE NYIHDIFVDN
QHITLSLWDT AGQEEFDRLR SLSYSDTHTI MLCFSVDSRD SLENVKNKWV SEIADHCEGV
KLVLVALKCD LRSSDEYGNE SAITPGSIQN QKYNGGGGNG LIPYDEGLAM AKQIGALRYL
ECSAKMNRGV NEAFTEAARC ALTATPKGAR DSAPEAESSS CTIM
