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RHO4_ASHGO
ID   RHO4_ASHGO              Reviewed;         259 AA.
AC   Q9P8V0;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=GTP-binding protein RHO4;
DE   Flags: Precursor;
GN   Name=RHO4; OrderedLocusNames=ACR257C;
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].
RX   PubMed=10721732; DOI=10.1016/s0378-1119(99)00509-0;
RA   Wendland J., Ayad-Durieux Y., Knechtle P., Rebischung C., Philippsen P.;
RT   "PCR-based gene targeting in the filamentous fungus Ashbya gossypii.";
RL   Gene 242:381-391(2000).
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   -!- 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; AF195008; AAF44725.1; -; Genomic_DNA.
DR   EMBL; AE016816; AAS51483.1; -; Genomic_DNA.
DR   RefSeq; NP_983659.1; NM_209012.1.
DR   AlphaFoldDB; Q9P8V0; -.
DR   SMR; Q9P8V0; -.
DR   STRING; 33169.AAS51483; -.
DR   EnsemblFungi; AAS51483; AAS51483; AGOS_ACR257C.
DR   GeneID; 4619794; -.
DR   KEGG; ago:AGOS_ACR257C; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   HOGENOM; CLU_041217_21_1_1; -.
DR   InParanoid; Q9P8V0; -.
DR   OMA; GAFAHIQ; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0000131; C:incipient cellular bud site; 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:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   GO; GO:0030011; P:maintenance of cell polarity; 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: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..256
FT                   /note="GTP-binding protein RHO4"
FT                   /id="PRO_0000198934"
FT   PROPEP          257..259
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281264"
FT   MOTIF           81..89
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..111
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         165..168
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         256
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           256
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   259 AA;  28871 MW;  790A9EE11E67C8F9 CRC64;
     MSAGPLQAAP KKNYGALIGA GPAVGGAAFN RTLSEVASYE RSRRDHATPD YRIKIVVVGD
     GATGKTSLLM SYTQGQFPED YVPTIFENYV TNIEGPRGKV IELALWDTAG QEEYSRLRPL
     SYGDVDIVMV CYAADNRTSL TNAEELWFPE VRHFCPHAPM MLVGLKSDLY SLDALDRLVD
     PTDAELVARK MGAFVHLQCS AKTRQCLEDV FNTAIHTALY DELRAPPQRG VKGMFKKKQQ
     RDPQAQSYKR VRKHRCVVL
 
 
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