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RHOA_PONAB
ID   RHOA_PONAB              Reviewed;         193 AA.
AC   Q5REY6;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Transforming protein RhoA;
DE            EC=3.6.5.2;
DE   Flags: Precursor;
GN   Name=RHOA;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Regulates KCNA2 potassium channel activity
CC       by reducing its location at the cell surface in response to CHRM1
CC       activation; promotes KCNA2 endocytosis. Acts as an allosteric activator
CC       of guanine nucleotide exchange factor ECT2 by binding in its activated
CC       GTP-bound form to the PH domain of ECT2 which stimulates the release of
CC       PH inhibition and promotes the binding of substrate RHOA to the ECT2
CC       catalytic center. May be an activator of PLCE1. In neurons, involved in
CC       the inhibition of the initial spine growth. Upon activation by CaMKII,
CC       modulates dendritic spine structural plasticity by relaying CaMKII
CC       transient activation to synapse-specific, long-term signaling. Acts as
CC       a regulator of platelet alpha-granule release during activation and
CC       aggregation of platelets (By similarity).
CC       {ECO:0000250|UniProtKB:P61586, ECO:0000250|UniProtKB:P61589,
CC       ECO:0000250|UniProtKB:Q9QUI0}.
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. Interacts
CC       (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal domain) (By
CC       similarity). Interacts (GTP-bound form) with ECT2; the interaction
CC       results in allosteric activation of ECT2 (By similarity). Interacts
CC       with RAP1GDS1; the interaction is direct and in a 1:1 stoichiometry (By
CC       similarity). {ECO:0000250|UniProtKB:P61586,
CC       ECO:0000250|UniProtKB:Q9QUI0}.
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:0000250|UniProtKB:Q9QUI0}. 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:Q9QUI0}.
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: Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (By
CC       similarity). Phosphorylation by SLK at Ser-188 in response to AGTR2
CC       activation (By similarity). {ECO:0000250|UniProtKB:P61586,
CC       ECO:0000250|UniProtKB:P61589}.
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; CR857377; CAH89671.1; -; mRNA.
DR   RefSeq; NP_001124755.1; NM_001131283.1.
DR   AlphaFoldDB; Q5REY6; -.
DR   BMRB; Q5REY6; -.
DR   SMR; Q5REY6; -.
DR   Ensembl; ENSPPYT00000053963; ENSPPYP00000039086; ENSPPYG00000013873.
DR   GeneID; 100171605; -.
DR   KEGG; pon:100171605; -.
DR   CTD; 387; -.
DR   GeneTree; ENSGT00950000182945; -.
DR   InParanoid; Q5REY6; -.
DR   OrthoDB; 1166960at2759; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0043296; C:apical junction complex; ISS:UniProtKB.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IEA:Ensembl.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0017022; F:myosin binding; IEA:Ensembl.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0002363; P:alpha-beta T cell lineage commitment; IEA:Ensembl.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
DR   GO; GO:0043297; P:apical junction assembly; ISS:UniProtKB.
DR   GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0043366; P:beta selection; IEA:Ensembl.
DR   GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
DR   GO; GO:0036089; P:cleavage furrow formation; ISS:UniProtKB.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR   GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0097498; P:endothelial tube lumen extension; IEA:Ensembl.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR   GO; GO:0021861; P:forebrain radial glial cell differentiation; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:1903673; P:mitotic cleavage furrow formation; ISS:UniProtKB.
DR   GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR   GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl.
DR   GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0045792; P:negative regulation of cell size; IEA:Ensembl.
DR   GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IEA:Ensembl.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR   GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR   GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IEA:Ensembl.
DR   GO; GO:0060193; P:positive regulation of lipase activity; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR   GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB.
DR   GO; GO:1904695; P:positive regulation of vascular associated smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl.
DR   GO; GO:0010975; P:regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0033688; P:regulation of osteoblast proliferation; IEA:Ensembl.
DR   GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
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; IEA:Ensembl.
DR   GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR   GO; GO:0061383; P:trabecula morphogenesis; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cell membrane; Cell projection; Cytoplasm;
KW   Cytoskeleton; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Prenylation; Proto-oncogene;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..190
FT                   /note="Transforming protein RhoA"
FT                   /id="PRO_0000292954"
FT   PROPEP          191..193
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P61585"
FT                   /id="PRO_0000290013"
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"
FT                   /evidence="ECO:0000250|UniProtKB:P61589"
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   CONFLICT        190
FT                   /note="C -> R (in Ref. 1; CAH89671)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   193 AA;  21768 MW;  C4DA2DC31FF858BC CRC64;
     MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT
     AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
     LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ
     ARRGKKKSGC LVL
 
 
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