##gff-version 3 P61586 UniProtKB Chain 1 190 . . . ID=PRO_0000030411;Note=Transforming protein RhoA P61586 UniProtKB Propeptide 191 193 . . . ID=PRO_0000030412;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61585 P61586 UniProtKB Region 61 78 . . . Note=Switch II region%3B involved in RAP1GDS1 isoform 2 binding;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:30190425,ECO:0007744|PDB:5ZHX;Dbxref=PMID:30190425 P61586 UniProtKB Motif 34 42 . . . Note=Effector region;Ontology_term=ECO:0000255;evidence=ECO:0000255 P61586 UniProtKB Binding site 12 19 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10748207,ECO:0000269|PubMed:12777804;Dbxref=PMID:10748207,PMID:12777804 P61586 UniProtKB Binding site 30 37 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820 P61586 UniProtKB Binding site 59 63 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820 P61586 UniProtKB Binding site 117 120 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10748207,ECO:0000269|PubMed:12777804;Dbxref=PMID:10748207,PMID:12777804 P61586 UniProtKB Binding site 160 162 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62820 P61586 UniProtKB Site 189 190 . . . Note=(Microbial infection) Cleavage%3B by yopT;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12062101,ECO:0000269|PubMed:12538863;Dbxref=PMID:12062101,PMID:12538863 P61586 UniProtKB Modified residue 34 34 . . . Note=(Microbial infection) O-AMP-tyrosine%3B by Haemophilus IbpA%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19362538;Dbxref=PMID:19362538 P61586 UniProtKB Modified residue 37 37 . . . Note=(Microbial infection) O-AMP-threonine%3B by Vibrio VopS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19039103;Dbxref=PMID:19039103 P61586 UniProtKB Modified residue 41 41 . . . Note=(Microbial infection) ADP-ribosylasparagine%3B by botulinum toxin;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:1328215;Dbxref=PMID:1328215 P61586 UniProtKB Modified residue 63 63 . . . Note=5-glutamyl serotonin;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QUI0 P61586 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine%3B by PKG/PRKG1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11162591;Dbxref=PMID:11162591 P61586 UniProtKB Modified residue 190 190 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61585 P61586 UniProtKB Lipidation 185 185 . . . Note=(Microbial infection) N6-stearoyl lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30061757;Dbxref=PMID:30061757 P61586 UniProtKB Lipidation 186 186 . . . Note=(Microbial infection) N6-stearoyl lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30061757;Dbxref=PMID:30061757 P61586 UniProtKB Lipidation 187 187 . . . Note=(Microbial infection) N6-stearoyl lysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30061757;Dbxref=PMID:30061757 P61586 UniProtKB Lipidation 190 190 . . . Note=S-geranylgeranyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P61585 P61586 UniProtKB Glycosylation 34 34 . . . Note=(Microbial infection) O-linked (GlcNAc) tyrosine%3B by Photorhabdus PAU_02230%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24141704;Dbxref=PMID:24141704 P61586 UniProtKB Glycosylation 37 37 . . . Note=(Microbial infection) O-alpha-linked (GlcNAc) threonine%3B by C.novyi toxin TcdA%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8810274;Dbxref=PMID:8810274 P61586 UniProtKB Glycosylation 37 37 . . . Note=(Microbial infection) O-linked (Glc) threonine%3B by C.difficile toxins TcdA and TcdB%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24905543,ECO:0000269|PubMed:7775453,ECO:0000269|PubMed:7777059;Dbxref=PMID:24905543,PMID:7775453,PMID:7777059 P61586 UniProtKB Cross-link 135 135 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23871831;Dbxref=PMID:23871831 P61586 UniProtKB Natural variant 47 47 . . . ID=VAR_083545;Note=In EDFAOB%3B somatic mosaic variant%3B decreased Rho protein signal transduction%3B decreased substrate adhesion-dependent cell spreading%3B decreased number of stress fibers assembly%3B decreased cytoplasmic microtubule organization. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31570889;Dbxref=PMID:31570889 P61586 UniProtKB Natural variant 71 71 . . . ID=VAR_083546;Note=In EDFAOB%3B somatic mosaic variant%3B decreased Rho protein signal transduction%3B decreased substrate adhesion-dependent cell spreading%3B decreased stress fibers assembly%3B decreased cytoplasmic microtubule organization. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31570889;Dbxref=PMID:31570889 P61586 UniProtKB Mutagenesis 14 14 . . . Note=Increased Rho protein signal transduction. Constitutively active. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19948726,ECO:0000269|PubMed:31570889;Dbxref=PMID:19948726,PMID:31570889 P61586 UniProtKB Mutagenesis 19 19 . . . Note=Decreased Rho protein signal transduction. Decreased substrate adhesion-dependent cell spreading. Decreased stress fibers assembly. Decreased cytoplasmic microtubule organization. T->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31570889;Dbxref=PMID:31570889 P61586 UniProtKB Mutagenesis 34 34 . . . Note=Abolishes interaction with DGKQ. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10066731,ECO:0000269|PubMed:19362538;Dbxref=PMID:10066731,PMID:19362538 P61586 UniProtKB Mutagenesis 34 34 . . . Note=Abolishes AMPylation by Haemophilus IbpA. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10066731,ECO:0000269|PubMed:19362538;Dbxref=PMID:10066731,PMID:19362538 P61586 UniProtKB Mutagenesis 37 37 . . . Note=Abolished monoglucosylation by C.difficile toxin TcdA. Abolished O-GlcNAcylation by C.novyi toxin TcdA. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7775453,ECO:0000269|PubMed:8810274;Dbxref=PMID:7775453,PMID:8810274 P61586 UniProtKB Mutagenesis 63 63 . . . Note=Causes constitutive activation. Q->L P61586 UniProtKB Mutagenesis 135 135 . . . Note=Reduced FBXL19-mediated ubiquitination and subsequent degradation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23871831;Dbxref=PMID:23871831 P61586 UniProtKB Mutagenesis 185 187 . . . Note=In 3KR mutant%3B abolished stearoylation in response to S.flexneri infection. KKK->RRR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30061757;Dbxref=PMID:30061757 P61586 UniProtKB Mutagenesis 193 193 . . . Note=Converts geranyl-geranylation to farnesylation%3B does not prevent the cleavage by yopT. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12538863;Dbxref=PMID:12538863 P61586 UniProtKB Sequence conflict 23 23 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P61586 UniProtKB Beta strand 4 13 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Helix 14 16 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8BNT P61586 UniProtKB Helix 18 23 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Beta strand 42 48 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Beta strand 51 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Helix 64 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Turn 67 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Helix 70 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Beta strand 78 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Helix 89 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Helix 99 106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5FR2 P61586 UniProtKB Beta strand 112 117 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Helix 119 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Helix 125 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Turn 133 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Helix 141 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Beta strand 154 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Turn 161 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Helix 167 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V6U P61586 UniProtKB Turn 182 184 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZHX P61586 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5ZHX P61586 UniProtKB Beta strand 190 193 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5FR1