| IED ID | IndEnz0005000101 |
| Enzyme Type ID | lipase000101 |
| Protein Name |
Rho-related GTP-binding protein RhoC Rho cDNA clone 9 h9 |
| Gene Name | RHOC ARH9 ARHC |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYIADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRQDEHTRRELAKMKQEPVRSEEGRDMANRISAFGYLECSAKTKEGVREVFEMATRAGLQVRKNKRRRGCPIL |
| Enzyme Length | 193 |
| Uniprot Accession Number | P08134 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells. {ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:20974804}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 12..19; /note=GTP; /evidence=ECO:0000250; NP_BIND 59..63; /note=GTP; /evidence=ECO:0000250; NP_BIND 117..120; /note=GTP; /evidence=ECO:0000250 |
| Features | Beta strand (6); Chain (1); Glycosylation (2); Helix (9); Lipidation (1); Modified residue (2); Motif (1); Natural variant (1); Nucleotide binding (3); Propeptide (1); Turn (3) |
| Keywords | 3D-structure;ADP-ribosylation;Cell membrane;GTP-binding;Glycoprotein;Lipoprotein;Membrane;Methylation;Nucleotide-binding;Prenylation;Reference proteome |
| Interact With | Q9Y4F9; Q96MK2 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow {ECO:0000269|PubMed:16236794}. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. |
| Modified Residue | MOD_RES 41; /note=ADP-ribosylasparagine; by botulinum toxin; /evidence=ECO:0000250; MOD_RES 190; /note=Cysteine methyl ester; /evidence=ECO:0000250|UniProtKB:P62745 |
| Post Translational Modification | PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly. {ECO:0000269|PubMed:24141704}.; PTM: (Microbial infection) Glucosylated at Thr-37 by C.difficile toxins TcdA and TcdB in the colonic epithelium (PubMed:24905543). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption (PubMed:24905543). {ECO:0000269|PubMed:24905543}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1Z2C; 2GCN; 2GCO; 2GCP; |
| Mapped Pubmed ID | 10619026; 10652353; 10753910; 10873388; 11018042; 11207612; 11283606; 11294240; 11331307; 11839578; 11942626; 12090470; 12101119; 12185584; 12220504; 12221096; 12730235; 12783890; 12802051; 12808121; 12939257; 12970882; 14514689; 14555841; 14614010; 15006353; 15107133; 15210733; 15507212; 15642170; 15668138; 15670823; 15699075; 15969750; 16112081; 16189514; 16202622; 16212495; 16219803; 16431929; 16439214; 16511001; 16776779; 16777452; 16896804; 16899593; 17018591; 17077126; 17151359; 17265125; 17353931; 17497936; 17549441; 17696235; 17765681; 17896152; 17897917; 17932950; 18006505; 18058225; 18211678; 18218625; 18478927; 18794150; 18980974; 19016761; 19094228; 19107362; 19152186; 19157876; 19222696; 19367725; 19421144; 19462897; 19477269; 19499974; 19642867; 19701800; 19713215; 19723632; 19861405; 19887681; 19911011; 19953094; 20014943; 20056178; 20101212; 20232393; 20403997; 20503409; 21079653; 21087931; 21159255; 21208644; 21242305; 21351730; 21454492; 21537845; 21566117; 21575520; 21576392; 21674277; 21732343; 21757538; 21862636; 22057916; 22094460; 22190034; 22217540; 22275430; 22293682; 22304920; 22673745; 22790947; 22896661; 22911725; 22911862; 22935975; 22992742; 23036489; 23145020; 23200924; 23222643; 23255595; 23302395; 23319595; 23382905; 23444367; 23474984; 23716662; 23764197; 23993968; 24096540; 24128008; 24312560; 24376640; 24414340; 24447566; 24457551; 24533098; 24914801; 24986540; 25123151; 25236186; 25416956; 25425145; 25516960; 25622907; 25624724; 25649143; 25659578; 25677806; 25933027; 26020100; 26260613; 26615410; 26673619; 26741994; 26898345; 27108649; 27147504; 27355867; 27481945; 27487132; 27494896; 27748883; 27748937; 28069441; 28146423; 28508825; 28536953; 28818073; 28949796; 28960175; 28984384; 29500478; 2966156; 30779947; 31062507; 31324164; 31340863; 31488179; 31519588; 31871319; 32314833; 32693062; 32719397; 33082325; 33825439; 33865221; 3839510; 7721814; 8543060; 8617235; 8662509; 8662891; 8702756; 8807639; 8939998; 9211904; 9308960; 9354661; 9792683; 9870942; 9870943; 9988689; |
| Motif | MOTIF 34..42; /note=Effector region; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 22,006 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.6.5.2; |