| IED ID | IndEnz0005000087 |
| Enzyme Type ID | lipase000087 |
| Protein Name |
Transforming protein RhoA EC 3.6.5.2 Rho cDNA clone 12 h12 |
| Gene Name | RHOA ARH12 ARHA RHO12 |
| 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 | MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGCLVL |
| Enzyme Length | 193 |
| Uniprot Accession Number | P61586 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase. Activated by GEFs such as ARHGEF2, ARHGEF3, ARHGEF28 and BCR (PubMed:23940119, PubMed:12221096). Inhibited by GAPs such as ARHGAP30 (PubMed:21565175). Inhibited by GDP dissociation inhibitors such as ARHGDIA (PubMed:20400958). {ECO:0000269|PubMed:12221096, ECO:0000269|PubMed:20400958, ECO:0000269|PubMed:21565175, ECO:0000269|PubMed:23940119}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000269|PubMed:21565175, ECO:0000269|PubMed:23940119};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000305|PubMed:21565175, ECO:0000305|PubMed:23940119}; |
| DNA Binding | |
| EC Number | 3.6.5.2 |
| Enzyme Function | FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers (PubMed:8910519, PubMed:9121475, PubMed:31570889). Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis (PubMed:16236794, PubMed:12900402). Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion (PubMed:20974804, PubMed:23940119). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (PubMed:19934221). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (PubMed:20937854). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436, PubMed:19403695). Acts as an allosteric activator of guanine nucleotide exchange factor ECT2 by binding in its activated GTP-bound form to the PH domain of ECT2 which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the ECT2 catalytic center (PubMed:31888991). May be an activator of PLCE1 (PubMed:16103226). In neurons, involved in the inhibition of the initial spine growth. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (By similarity). {ECO:0000250|UniProtKB:P61589, ECO:0000250|UniProtKB:Q9QUI0, ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:19403695, ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:23940119, ECO:0000269|PubMed:31570889, ECO:0000269|PubMed:31888991, ECO:0000269|PubMed:8910519, ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9635436}.; FUNCTION: (Microbial infection) Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague. {ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12538863}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 12..19; /note="GTP"; /evidence="ECO:0000269|PubMed:10748207, ECO:0000269|PubMed:12777804"; NP_BIND 59..63; /note="GTP"; /evidence="ECO:0000250"; NP_BIND 117..120; /note="GTP"; /evidence="ECO:0000269|PubMed:10748207, ECO:0000269|PubMed:12777804" |
| Features | Beta strand (9); Chain (1); Glycosylation (3); Helix (10); Lipidation (1); Modified residue (6); Motif (1); Mutagenesis (7); Natural variant (2); Nucleotide binding (3); Propeptide (1); Sequence conflict (1); Site (1); Turn (3) |
| Keywords | 3D-structure;ADP-ribosylation;Cell cycle;Cell division;Cell membrane;Cell projection;Cytoplasm;Cytoskeleton;Direct protein sequencing;Disease variant;Ectodermal dysplasia;GTP-binding;Glycoprotein;Host-virus interaction;Hydrolase;Lipoprotein;Magnesium;Membrane;Methylation;Nucleotide-binding;Phosphoprotein;Prenylation;Proto-oncogene;Reference proteome;Ubl conjugation |
| Interact With | Q15109; Q7Z6G8-3; P05067; Q07960; P52565; O15085; Q9NZN5; Q8IW93; Q92974; P46527; Q9Y4D1; O60610; Q9UKT9; P19338; Q9Y4F9; Q9Y4F9-2; Q96MK2; Q13464; Q9BST9; Q15796; Q9HCE7-2; Q15654; O08808; Q6PDM6; Q9Z0S9; Q8C6B2; A0A0F6B1Q8; Q9FD10 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex {ECO:0000269|PubMed:9635436}. Midbody. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9QUI0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9QUI0}. Note=Localized to cell-cell contacts in calcium-treated keratinocytes (By similarity). Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Localizes to the equatorial cell cortex (at the site of the presumptive furrow) in early anaphase in an activated form and in a myosin- and actin-independent manner. {ECO:0000250|UniProtKB:Q9QUI0}. |
| Modified Residue | MOD_RES 34; /note=(Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate; /evidence=ECO:0000269|PubMed:19362538; MOD_RES 37; /note=(Microbial infection) O-AMP-threonine; by Vibrio VopS; /evidence=ECO:0000269|PubMed:19039103; MOD_RES 41; /note=(Microbial infection) ADP-ribosylasparagine; by botulinum toxin; /evidence=ECO:0000305|PubMed:1328215; MOD_RES 63; /note=5-glutamyl serotonin; /evidence=ECO:0000250|UniProtKB:Q9QUI0; MOD_RES 188; /note=Phosphoserine; by PKG/PRKG1; /evidence=ECO:0000269|PubMed:11162591; MOD_RES 190; /note=Cysteine methyl ester; /evidence=ECO:0000250|UniProtKB:P62745 |
| Post Translational Modification | PTM: (Microbial infection) Substrate for botulinum ADP-ribosyltransferase. {ECO:0000269|PubMed:1328215}.; PTM: (Microbial infection) Cleaved by yopT protease when the cell is infected by some Yersinia pathogens. This removes the lipid attachment, and leads to its displacement from plasma membrane and to subsequent cytoskeleton cleavage. {ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12538863}.; PTM: (Microbial infection) AMPylation at Tyr-34 and Thr-37 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo. {ECO:0000269|PubMed:19039103, ECO:0000269|PubMed:19362538}.; 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:7777059, PubMed:7775453, PubMed:24905543). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption and cell death, resulting in the loss of colonic epithelial barrier function (PubMed:7777059, PubMed:7775453). {ECO:0000269|PubMed:24905543, ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059}.; PTM: (Microbial infection) Glycosylated (O-GlcNAcylated) at Thr-37 by C.novyi toxin TcdA (PubMed:8810274). O-GlcNAcylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption (PubMed:8810274). {ECO:0000269|PubMed:8810274}.; PTM: Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (PubMed:11162591). Phosphorylation by SLK at Ser-188 in response to AGTR2 activation (By similarity). {ECO:0000250|UniProtKB:P61589, ECO:0000269|PubMed:11162591}.; PTM: Ubiquitinated by the BCR(KCTD13) and BCR(TNFAIP1) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and synaptic transmission in neurons. {ECO:0000269|PubMed:19782033}.; PTM: Serotonylation of Gln-63 by TGM2 during activation and aggregation of platelets leads to constitutive activation of GTPase activity. {ECO:0000250|UniProtKB:Q9QUI0}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (48) |
| Cross Reference PDB | 1A2B; 1CC0; 1CXZ; 1DPF; 1FTN; 1KMQ; 1LB1; 1OW3; 1S1C; 1TX4; 1X86; 1XCG; 2RGN; 3KZ1; 3LW8; 3LWN; 3LXR; 3MSX; 3T06; 4D0N; 4XH9; 4XOI; 4XSG; 4XSH; 5A0F; 5BWM; 5C2K; 5C4M; 5EZ6; 5FR1; 5FR2; 5HPY; 5IRC; 5JCP; 5JHG; 5JHH; 5M6X; 5M70; 5ZHX; 6BC0; 6BCA; 6BCB; 6KX2; 6KX3; 6R3V; 6V6M; 6V6U; 6V6V; |
| Mapped Pubmed ID | 10037681; 10232922; 10489445; 10490598; 10523665; 10523675; 10526156; 10579713; 10591629; 10619026; 10652353; 10699171; 10753910; 10769020; 10873388; 10877843; 10913441; 11018042; 11058585; 11085924; 11179879; 11207612; 11283606; 11294240; 11331307; 11335720; 11373293; 11396949; 11431473; 11432776; 11447115; 11606631; 11672528; 11680691; 11689693; 11704860; 11741970; 11779461; 11788600; 11804589; 11804590; 11818523; 11822867; 11830597; 11839765; 11884391; 11889037; 11907271; 11912491; 11933159; 11942626; 12016230; 12071848; 12071859; 12093360; 12101119; 12115629; 12119292; 12134165; 12154081; 12169092; 12185584; 12195014; 12220504; 12221077; 12244193; 12397214; 12401808; 12429848; 12445208; 12524425; 12531887; 12534282; 12579323; 12584113; 12593858; 12650940; 12692008; 12692556; 12719789; 12730235; 12732141; 12783890; 12802051; 12805219; 12808121; 12847276; 12857875; 12877655; 12879077; 12939257; 12953056; 12972426; 12972601; 1383236; 14506264; 14512443; 14514689; 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| Motif | MOTIF 34..42; /note=Effector region; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 21,768 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:19669; RHEA:19670 |
| Cross Reference Brenda | 3.6.5.2; |