RHOA_RAT
ID RHOA_RAT Reviewed; 193 AA.
AC P61589;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Transforming protein RhoA {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61586};
DE Flags: Precursor;
GN Name=Rhoa {ECO:0000312|RGD:619921}; Synonyms=Arha, Arha2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SHR, and Wistar Kyoto;
RA Andresen B.T., Jackson E.K., Romero G.G.;
RT "Sequence of Wistar-Kyoto (WKY) and spontaneously hypertensive rat (SHR)
RT RhoA cDNA.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH KCNA2.
RX PubMed=9635436; DOI=10.1016/s0092-8674(00)81212-x;
RA Cachero T.G., Morielli A.D., Peralta E.G.;
RT "The small GTP-binding protein RhoA regulates a delayed rectifier potassium
RT channel.";
RL Cell 93:1077-1085(1998).
RN [4]
RP PHOSPHORYLATION AT SER-188.
RX PubMed=18420945; DOI=10.1161/circresaha.107.164764;
RA Guilluy C., Rolli-Derkinderen M., Loufrani L., Bourge A., Henrion D.,
RA Sabourin L., Loirand G., Pacaud P.;
RT "Ste20-related kinase SLK phosphorylates Ser188 of RhoA to induce
RT vasodilation in response to angiotensin II Type 2 receptor activation.";
RL Circ. Res. 102:1265-1274(2008).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21423166; DOI=10.1038/nature09823;
RA Murakoshi H., Wang H., Yasuda R.;
RT "Local, persistent activation of Rho GTPases during plasticity of single
RT dendritic spines.";
RL Nature 472:100-104(2011).
CC -!- FUNCTION: Small GTPase which cycles between an active GTP-bound and an
CC inactive GDP-bound state. Mainly associated with cytoskeleton
CC organization, in active state binds to a variety of effector proteins
CC to regulate cellular responses such as cytoskeletal dynamics, cell
CC migration and cell cycle. Regulates a signal transduction pathway
CC linking plasma membrane receptors to the assembly of focal adhesions
CC and actin stress fibers. Involved in a microtubule-dependent signal
CC that is required for the myosin contractile ring formation during cell
CC cycle cytokinesis. Plays an essential role in cleavage furrow
CC formation. Required for the apical junction formation of keratinocyte
CC cell-cell adhesion. Essential for the SPATA13-mediated regulation of
CC cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-
CC DIAPH1 signaling pathway plays an important role in ERBB2-dependent
CC stabilization of microtubules at the cell cortex. It controls the
CC localization of APC and CLASP2 to the cell membrane, via the regulation
CC of GSK3B activity. In turn, membrane-bound APC allows the localization
CC of the MACF1 to the cell membrane, which is required for microtubule
CC capture and stabilization (By similarity). Regulates KCNA2 potassium
CC channel activity by reducing its location at the cell surface in
CC response to CHRM1 activation; promotes KCNA2 endocytosis
CC (PubMed:9635436). Acts as an allosteric activator of guanine nucleotide
CC exchange factor ECT2 by binding in its activated GTP-bound form to the
CC PH domain of ECT2 which stimulates the release of PH inhibition and
CC promotes the binding of substrate RHOA to the ECT2 catalytic center (By
CC similarity). May be an activator of PLCE1 (By similarity). In neurons,
CC involved in the inhibition of the initial spine growth. Upon activation
CC by CaMKII, modulates dendritic spine structural plasticity by relaying
CC CaMKII transient activation to synapse-specific, long-term signaling
CC (PubMed:21423166). Acts as a regulator of platelet alpha-granule
CC release during activation and aggregation of platelets (By similarity).
CC {ECO:0000250|UniProtKB:P61586, ECO:0000250|UniProtKB:Q9QUI0,
CC ECO:0000269|PubMed:21423166, ECO:0000269|PubMed:9635436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P61586};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P61586};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. Activated by GEFs such as ARHGEF2, ARHGEF3,
CC ARHGEF28 and BCR. Inhibited by GAPs such as ARHGAP30. Inhibited by GDP
CC dissociation inhibitors such as ARHGDIA.
CC {ECO:0000250|UniProtKB:P61586}.
CC -!- SUBUNIT: Interacts with ARHGEF28 (By similarity). Interacts (via GTP-
CC bound form) with RIPOR1 (via N-terminus); this interaction links RHOA
CC to STK24 and STK26 kinases. Interacts with RIPOR2 (via active GTP- or
CC inactive GDP-bound forms) isoform 1 and isoform 2; these interactions
CC are direct, block the loading of GTP to RHOA and decrease upon
CC chemokine CCL19 stimulation in primary T lymphocytes. Binds PRKCL1,
CC ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN.
CC Interacts with PLCE1 and AKAP13. Interacts with DIAPH1. Interacts (in
CC the constitutively activated, GTP-bound form) with DGKQ. Interacts with
CC RACK1; enhances RHOA activation. Interacts with PKP4; the interaction
CC is detected at the midbody. Interacts (GTP-bound form preferentially)
CC with PKN2; the interaction stimulates autophosphorylation and
CC phosphorylation of PKN2. Interacts with ARHGDIA; this interaction
CC inactivates and stabilizes RHOA. Interacts with ARHGDIB (By
CC similarity). Interacts (GTP-bound form) with KCNA2 (via cytoplasmic N-
CC terminal domain) (PubMed:9635436). Interacts (GTP-bound form) with
CC ECT2; the interaction results in allosteric activation of ECT2 (By
CC similarity). Interacts with RAP1GDS1; the interaction is direct and in
CC a 1:1 stoichiometry (By similarity). {ECO:0000250|UniProtKB:P61586,
CC ECO:0000250|UniProtKB:Q9QUI0, ECO:0000269|PubMed:9635436}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61586};
CC Lipid-anchor {ECO:0000250|UniProtKB:P61586}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P61586}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P61586}. Cleavage furrow
CC {ECO:0000250|UniProtKB:P61586}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:P61586}. Midbody {ECO:0000250|UniProtKB:P61586}.
CC Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9QUI0}. Cell
CC projection, dendrite {ECO:0000305|PubMed:21423166}. Nucleus
CC {ECO:0000250|UniProtKB:P61586}. Note=Localized to cell-cell contacts in
CC calcium-treated keratinocytes (By similarity). Translocates to the
CC equatorial region before furrow formation in a ECT2-dependent manner.
CC Localizes to the equatorial cell cortex (at the site of the presumptive
CC furrow) in early anaphase in an activated form and in a myosin- and
CC actin-independent manner. {ECO:0000250|UniProtKB:P61586,
CC ECO:0000250|UniProtKB:Q9QUI0}.
CC -!- PTM: Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (By
CC similarity). Phosphorylation by SLK at Ser-188 in response to AGTR2
CC activation (PubMed:18420945). {ECO:0000250|UniProtKB:P61586,
CC ECO:0000269|PubMed:18420945}.
CC -!- PTM: Ubiquitinated by the BCR(KCTD13) and BCR(TNFAIP1) E3 ubiquitin
CC ligase complexes, leading to its degradation by the proteasome, thereby
CC regulating the actin cytoskeleton and synaptic transmission in neurons.
CC {ECO:0000250|UniProtKB:Q9QUI0}.
CC -!- PTM: Serotonylation of Gln-63 by TGM2 during activation and aggregation
CC of platelets leads to constitutive activation of GTPase activity.
CC {ECO:0000250|UniProtKB:Q9QUI0}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AY026068; AAK11717.1; -; mRNA.
DR EMBL; AY026069; AAK11718.1; -; mRNA.
DR EMBL; BC061732; AAH61732.1; -; mRNA.
DR RefSeq; NP_476473.1; NM_057132.3.
DR RefSeq; XP_006243761.1; XM_006243699.1.
DR RefSeq; XP_006243762.1; XM_006243700.1.
DR RefSeq; XP_006243763.1; XM_006243701.1.
DR PDB; 3TVD; X-ray; 2.99 A; A/B=1-193.
DR PDBsum; 3TVD; -.
DR AlphaFoldDB; P61589; -.
DR BMRB; P61589; -.
DR SMR; P61589; -.
DR BioGRID; 250720; 3.
DR IntAct; P61589; 7.
DR MINT; P61589; -.
DR STRING; 10116.ENSRNOP00000066672; -.
DR iPTMnet; P61589; -.
DR PhosphoSitePlus; P61589; -.
DR SwissPalm; P61589; -.
DR World-2DPAGE; 0004:P61589; -.
DR jPOST; P61589; -.
DR PaxDb; P61589; -.
DR PRIDE; P61589; -.
DR Ensembl; ENSRNOT00000094929; ENSRNOP00000091658; ENSRNOG00000050519.
DR GeneID; 117273; -.
DR KEGG; rno:117273; -.
DR CTD; 387; -.
DR RGD; 619921; Rhoa.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00950000182945; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; P61589; -.
DR OMA; RWIPEIK; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; P61589; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-RNO-198203; PI3K/AKT activation.
DR Reactome; R-RNO-209563; Axonal growth stimulation.
DR Reactome; R-RNO-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-RNO-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-RNO-4086400; PCP/CE pathway.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-RNO-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-RNO-5625900; RHO GTPases activate CIT.
DR Reactome; R-RNO-5625970; RHO GTPases activate KTN1.
DR Reactome; R-RNO-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
DR Reactome; R-RNO-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR PRO; PR:P61589; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000050519; Expressed in lung and 19 other tissues.
DR Genevisible; P61589; RN.
DR GO; GO:0043296; C:apical junction complex; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IDA:RGD.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IDA:BHF-UCL.
DR GO; GO:0017022; F:myosin binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IPI:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0002363; P:alpha-beta T cell lineage commitment; ISO:RGD.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0043297; P:apical junction assembly; ISS:UniProtKB.
DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; ISO:RGD.
DR GO; GO:0043366; P:beta selection; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0071393; P:cellular response to progesterone stimulus; NAS:BHF-UCL.
DR GO; GO:0021795; P:cerebral cortex cell migration; ISO:RGD.
DR GO; GO:0036089; P:cleavage furrow formation; ISS:UniProtKB.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
DR GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
DR GO; GO:0097498; P:endothelial tube lumen extension; ISO:RGD.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0021861; P:forebrain radial glial cell differentiation; ISO:RGD.
DR GO; GO:0046039; P:GTP metabolic process; IDA:BHF-UCL.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:1903673; P:mitotic cleavage furrow formation; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:RGD.
DR GO; GO:0050919; P:negative chemotaxis; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0045792; P:negative regulation of cell size; ISO:RGD.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:RGD.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:RGD.
DR GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IGI:ParkinsonsUK-UCL.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; ISO:RGD.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:RGD.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IMP:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IMP:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEP:RGD.
DR GO; GO:0042476; P:odontogenesis; ISO:RGD.
DR GO; GO:0043931; P:ossification involved in bone maturation; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:RGD.
DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEP:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IEP:RGD.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:RGD.
DR GO; GO:0060193; P:positive regulation of lipase activity; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0071803; P:positive regulation of podosome assembly; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IEP:RGD.
DR GO; GO:1904695; P:positive regulation of vascular associated smooth muscle contraction; ISO:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEP:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IEP:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:RGD.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; ISO:RGD.
DR GO; GO:1905244; P:regulation of modification of synaptic structure; IMP:SynGO.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISO:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; ISO:RGD.
DR GO; GO:0033688; P:regulation of osteoblast proliferation; ISO:RGD.
DR GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:SynGO.
DR GO; GO:0035385; P:Roundabout signaling pathway; ISS:UniProtKB.
DR GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IMP:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:0061383; P:trabecula morphogenesis; ISO:RGD.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; Prenylation;
KW Proto-oncogene; Reference proteome; Ubl conjugation.
FT CHAIN 1..190
FT /note="Transforming protein RhoA"
FT /id="PRO_0000030415"
FT PROPEP 191..193
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT /id="PRO_0000030416"
FT REGION 61..78
FT /note="Switch II region; involved in RAP1GDS1 binding"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 160..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 63
FT /note="5-glutamyl serotonin"
FT /evidence="ECO:0000250|UniProtKB:Q9QUI0"
FT MOD_RES 188
FT /note="Phosphoserine; by PKG/PRKG1 and SLK"
FT /evidence="ECO:0000269|PubMed:18420945"
FT MOD_RES 190
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT LIPID 190
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:3TVD"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:3TVD"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:3TVD"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:3TVD"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:3TVD"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3TVD"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:3TVD"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:3TVD"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:3TVD"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:3TVD"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3TVD"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:3TVD"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:3TVD"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3TVD"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:3TVD"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:3TVD"
SQ SEQUENCE 193 AA; 21782 MW; C4C8BDC31FF858BC CRC64;
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ
ARRGKKKSGC LIL
