RHO1_ASHGO
ID RHO1_ASHGO Reviewed; 207 AA.
AC Q9HF54;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=GTP-binding protein RHO1;
DE Flags: Precursor;
GN Name=RHO1; OrderedLocusNames=ABR183W;
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; AF210628; AAG41249.1; -; Genomic_DNA.
DR EMBL; AE016815; AAS50955.1; -; Genomic_DNA.
DR RefSeq; NP_983131.1; NM_208484.1.
DR AlphaFoldDB; Q9HF54; -.
DR SMR; Q9HF54; -.
DR STRING; 33169.AAS50955; -.
DR EnsemblFungi; AAS50955; AAS50955; AGOS_ABR183W.
DR GeneID; 4619241; -.
DR KEGG; ago:AGOS_ABR183W; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q9HF54; -.
DR OMA; APEVNHY; -.
DR Proteomes; UP000000591; Chromosome II.
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: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: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..204
FT /note="GTP-binding protein RHO1"
FT /id="PRO_0000198932"
FT PROPEP 205..207
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281262"
FT REGION 187..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 193..207
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 204
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 23046 MW; 0A71F6A434C33B3A CRC64;
MSQQMHNPSI RRKLVIVGDG ACGKTCLLIV FAKGKFPQVY VPTVFDNYVA DVEVDGRRVE
LALWDTAGQE DYDRLRPLSY PDSNVVLICY SIDLPDSLEN VMEKWISEVL YFCQGVPIIL
VGCKADLRND PQVIEQLRQQ GQQPVSQAQA QEVADQIGAV EYIECSAKTG FGVREVFEAA
TRASLMGKQG KSKAKSDKKK KKKCVVL
