Detail Information for IndEnz0005000101
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;