RHOA_MOUSE
ID RHOA_MOUSE Reviewed; 193 AA.
AC Q9QUI0; O88336;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Transforming protein RhoA;
DE EC=3.6.5.2 {ECO:0000269|PubMed:24352656};
DE Flags: Precursor;
GN Name=Rhoa; Synonyms=Arha, Arha2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=9598304; DOI=10.1006/geno.1998.5219;
RA Boettger-Tong H.L., Agulnik A.I., Ty T.I., Bishop C.E.;
RT "Transposition of RhoA to the murine Y chromosome.";
RL Genomics 49:180-187(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, CD-1, and FVB/N;
RA Budge P.J., Graham B.S.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP INTERACTION WITH RTKN.
RX PubMed=8662891; DOI=10.1074/jbc.271.23.13556;
RA Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N.,
RA Fujisawa K., Morii N., Madaule P., Narumiya S.;
RT "Rhotekin, a new putative target for Rho bearing homology to a
RT serine/threonine kinase, PKN, and rhophilin in the rho-binding domain.";
RL J. Biol. Chem. 271:13556-13560(1996).
RN [6]
RP INTERACTION WITH DIAPH1.
RX PubMed=9214622; DOI=10.1093/emboj/16.11.3044;
RA Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A.,
RA Saito Y., Nakao K., Jockusch B.M., Narumiya S.;
RT "p140mDia, a mammalian homolog of Drosophila diaphanous, is a target
RT protein for Rho small GTPase and is a ligand for profilin.";
RL EMBO J. 16:3044-3056(1997).
RN [7]
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 [8]
RP INTERACTION WITH NET1.
RX PubMed=9535835; DOI=10.1074/jbc.273.15.8616;
RA Alberts A.S., Bouquin N., Johnston L.H., Treisman R.;
RT "Analysis of RhoA-binding proteins reveals an interaction domain conserved
RT in heterotrimeric G protein beta subunits and the yeast response regulator
RT protein Skn7.";
RL J. Biol. Chem. 273:8616-8622(1998).
RN [9]
RP INTERACTION WITH ARHGEF28.
RX PubMed=11058585; DOI=10.1074/jbc.m003839200;
RA van Horck F.P.G., Ahmadian M.R., Haeusler L.C., Moolenaar W.H.,
RA Kranenburg O.;
RT "Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide
RT exchange factor that interacts with microtubules.";
RL J. Biol. Chem. 276:4948-4956(2001).
RN [10]
RP FUNCTION, AND SEROTONYLATION AT GLN-63.
RX PubMed=14697203; DOI=10.1016/s0092-8674(03)01014-6;
RA Walther D.J., Peter J.U., Winter S., Hoeltje M., Paulmann N., Grohmann M.,
RA Vowinckel J., Alamo-Bethencourt V., Wilhelm C.S., Ahnert-Hilger G.,
RA Bader M.;
RT "Serotonylation of small GTPases is a signal transduction pathway that
RT triggers platelet alpha-granule release.";
RL Cell 115:851-862(2003).
RN [11]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11777936; DOI=10.1083/jcb.200105140;
RA Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J.,
RA Dotto G.P.;
RT "Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in
RT keratinocyte cell-cell adhesion.";
RL J. Cell Biol. 156:137-148(2002).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=21543326; DOI=10.1074/jbc.m111.245209;
RA Wu C., Agrawal S., Vasanji A., Drazba J., Sarkaria S., Xie J., Welch C.M.,
RA Liu M., Anand-Apte B., Horowitz A.;
RT "Rab13-dependent trafficking of RhoA is required for directional migration
RT and angiogenesis.";
RL J. Biol. Chem. 286:23511-23520(2011).
RN [14]
RP FUNCTION, AND INTERACTION WITH PKN2.
RX PubMed=20974804; DOI=10.1128/mcb.01001-10;
RA Wallace S.W., Magalhaes A., Hall A.;
RT "The Rho target PRK2 regulates apical junction formation in human bronchial
RT epithelial cells.";
RL Mol. Cell. Biol. 31:81-91(2011).
RN [15]
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24352656; DOI=10.1074/jbc.m113.534636;
RA Raynaud F., Moutin E., Schmidt S., Dahl J., Bertaso F., Boeckers T.M.,
RA Homburger V., Fagni L.;
RT "Rho-GTPase-activating protein interacting with Cdc-42-interacting protein
RT 4 homolog 2 (Rich2): a new Ras-related C3 botulinum toxin substrate 1
RT (Rac1) GTPase-activating protein that controls dendritic spine
RT morphogenesis.";
RL J. Biol. Chem. 289:2600-2609(2014).
RN [16]
RP UBIQUITINATION.
RX PubMed=29088697; DOI=10.1038/nature24470;
RA Escamilla C.O., Filonova I., Walker A.K., Xuan Z.X., Holehonnur R.,
RA Espinosa F., Liu S., Thyme S.B., Lopez-Garcia I.A., Mendoza D.B., Usui N.,
RA Ellegood J., Eisch A.J., Konopka G., Lerch J.P., Schier A.F., Speed H.E.,
RA Powell C.M.;
RT "Kctd13 deletion reduces synaptic transmission via increased RhoA.";
RL Nature 551:227-231(2017).
CC -!- FUNCTION: Small GTPase which cycles between an active GTP-bound and an
CC inactive GDP-bound state (PubMed:14697203). Mainly associated with
CC cytoskeleton organization, in active state binds to a variety of
CC effector proteins to regulate cellular responses such as cytoskeletal
CC dynamics, cell migration and cell cycle. Regulates a signal
CC transduction pathway linking plasma membrane receptors to the assembly
CC of focal adhesions and actin stress fibers. Involved in a microtubule-
CC dependent signal that is required for the myosin contractile ring
CC formation during cell cycle cytokinesis (By similarity). Plays an
CC essential role in cleavage furrow formation. Required for the apical
CC junction formation of keratinocyte cell-cell adhesion (PubMed:11777936,
CC PubMed:20974804). Essential for the SPATA13-mediated regulation of cell
CC migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1
CC 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. Acts as an
CC allosteric activator of guanine nucleotide exchange factor ECT2 by
CC binding in its activated GTP-bound form to the PH domain of ECT2 which
CC stimulates the release of PH inhibition and promotes the binding of
CC substrate RHOA to the ECT2 catalytic center (By similarity). May be an
CC activator of PLCE1 (PubMed:9635436). In neurons, involved in the
CC 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 (By
CC similarity). Acts as a regulator of platelet alpha-granule release
CC during activation and aggregation of platelets (PubMed:14697203).
CC {ECO:0000250|UniProtKB:P61586, ECO:0000250|UniProtKB:P61589,
CC ECO:0000269|PubMed:11777936, ECO:0000269|PubMed:14697203,
CC ECO:0000269|PubMed:20974804, 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:0000269|PubMed:24352656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:24352656};
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 (PubMed:11058585). 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 (By similarity). Interacts with ARHGEF2, ARHGEF3, NET1
CC and RTKN (PubMed:9535835, PubMed:8662891). Interacts with PLCE1 and
CC AKAP13 (By similarity). Interacts with DIAPH1 (PubMed:9214622).
CC Interacts (in the constitutively activated, GTP-bound form) with DGKQ.
CC Interacts with RACK1; enhances RHOA activation. Interacts with PKP4;
CC the interaction is detected at the midbody (By similarity). Interacts
CC (GTP-bound form preferentially) with PKN2; the interaction stimulates
CC autophosphorylation and phosphorylation of PKN2 (PubMed:20974804).
CC Interacts with ARHGDIA; this interaction inactivates and stabilizes
CC RHOA. Interacts with ARHGDIB (By similarity). Interacts (GTP-bound
CC form) with KCNA2 (via cytoplasmic N-terminal domain) (PubMed:9635436).
CC Interacts (GTP-bound form) with ECT2; the interaction results in
CC allosteric activation of ECT2 (By similarity). Interacts with RAP1GDS1;
CC the interaction is direct and in a 1:1 stoichiometry (By similarity).
CC {ECO:0000250|UniProtKB:P61586, ECO:0000269|PubMed:11058585,
CC ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8662891,
CC ECO:0000269|PubMed:9214622, ECO:0000269|PubMed:9535835,
CC ECO:0000269|PubMed:9635436}.
CC -!- INTERACTION:
CC Q9QUI0; Q8C6B2: Rtkn; NbExp=3; IntAct=EBI-643583, EBI-1162441;
CC Q9QUI0; Q9BST9: RTKN; Xeno; NbExp=2; IntAct=EBI-643583, EBI-446694;
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:0000269|PubMed:11777936,
CC ECO:0000269|PubMed:21543326}. Cell projection, dendrite
CC {ECO:0000269|PubMed:24352656}. Nucleus {ECO:0000250|UniProtKB:P61586}.
CC Note=Localized to cell-cell contacts in calcium-treated keratinocytes
CC (PubMed:11777936). Translocates to the equatorial region before furrow
CC formation in a ECT2-dependent manner. Localizes to the equatorial cell
CC cortex (at the site of the presumptive furrow) in early anaphase in an
CC activated form and in a myosin- and actin-independent manner (By
CC similarity). {ECO:0000250|UniProtKB:P61586,
CC ECO:0000269|PubMed:11777936}.
CC -!- INDUCTION: Up-regulated during keratinocyte differentiation.
CC {ECO:0000269|PubMed:11777936}.
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:0000305|PubMed:29088697}.
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:0000269|PubMed:14697203}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AF014371; AAC23710.1; -; mRNA.
DR EMBL; AF178958; AAD52675.1; -; mRNA.
DR EMBL; AF178959; AAD52676.1; -; mRNA.
DR EMBL; AF178960; AAD52677.1; -; mRNA.
DR EMBL; AF178961; AAD52678.1; -; mRNA.
DR EMBL; AK077606; BAC36896.1; -; mRNA.
DR EMBL; AK083624; BAC38971.1; -; mRNA.
DR EMBL; BC068115; AAH68115.1; -; mRNA.
DR CCDS; CCDS23521.1; -.
DR RefSeq; NP_001300890.1; NM_001313961.1.
DR RefSeq; NP_001300891.1; NM_001313962.1.
DR RefSeq; NP_058082.2; NM_016802.5.
DR PDB; 4F38; X-ray; 2.80 A; A=1-191.
DR PDBsum; 4F38; -.
DR AlphaFoldDB; Q9QUI0; -.
DR SMR; Q9QUI0; -.
DR BioGRID; 198192; 58.
DR DIP; DIP-29984N; -.
DR IntAct; Q9QUI0; 34.
DR MINT; Q9QUI0; -.
DR STRING; 10090.ENSMUSP00000007959; -.
DR ChEMBL; CHEMBL4523479; -.
DR iPTMnet; Q9QUI0; -.
DR PhosphoSitePlus; Q9QUI0; -.
DR SwissPalm; Q9QUI0; -.
DR EPD; Q9QUI0; -.
DR jPOST; Q9QUI0; -.
DR MaxQB; Q9QUI0; -.
DR PaxDb; Q9QUI0; -.
DR PRIDE; Q9QUI0; -.
DR ProteomicsDB; 255214; -.
DR Antibodypedia; 30508; 712 antibodies from 39 providers.
DR DNASU; 11848; -.
DR Ensembl; ENSMUST00000007959; ENSMUSP00000007959; ENSMUSG00000007815.
DR GeneID; 11848; -.
DR KEGG; mmu:11848; -.
DR UCSC; uc009rpe.2; mouse.
DR CTD; 387; -.
DR MGI; MGI:1096342; Rhoa.
DR VEuPathDB; HostDB:ENSMUSG00000007815; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00950000182945; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q9QUI0; -.
DR OMA; RWIPEIK; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; Q9QUI0; -.
DR TreeFam; TF300837; -.
DR BRENDA; 3.6.5.2; 3474.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-MMU-198203; PI3K/AKT activation.
DR Reactome; R-MMU-209563; Axonal growth stimulation.
DR Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-MMU-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5625900; RHO GTPases activate CIT.
DR Reactome; R-MMU-5625970; RHO GTPases activate KTN1.
DR Reactome; R-MMU-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
DR Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 11848; 17 hits in 71 CRISPR screens.
DR ChiTaRS; Rhoa; mouse.
DR PRO; PR:Q9QUI0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9QUI0; protein.
DR Bgee; ENSMUSG00000007815; Expressed in seminal vesicle and 250 other tissues.
DR ExpressionAtlas; Q9QUI0; baseline and differential.
DR Genevisible; Q9QUI0; MM.
DR GO; GO:0043296; C:apical junction complex; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; IDA:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0017022; F:myosin binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
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; IMP:CACAO.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:MGI.
DR GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0043297; P:apical junction assembly; IDA:UniProtKB.
DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; ISO:MGI.
DR GO; GO:0043366; P:beta selection; IMP:CACAO.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IDA:MGI.
DR GO; GO:0034329; P:cell junction assembly; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI.
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; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:MGI.
DR GO; GO:0043542; P:endothelial cell migration; ISO:MGI.
DR GO; GO:0097498; P:endothelial tube lumen extension; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0046039; P:GTP metabolic process; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:MGI.
DR GO; GO:0001822; P:kidney development; IGI:MGI.
DR GO; GO:1903673; P:mitotic cleavage furrow formation; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0050919; P:negative chemotaxis; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0045792; P:negative regulation of cell size; ISO:MGI.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:ARUK-UCL.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IDA:MGI.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IMP:CACAO.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:CACAO.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0042476; P:odontogenesis; IEP:UniProtKB.
DR GO; GO:0043931; P:ossification involved in bone maturation; IMP:BHF-UCL.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IMP:CACAO.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
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:MGI.
DR GO; GO:0060193; P:positive regulation of lipase activity; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IGI:MGI.
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; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:MGI.
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; IMP:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:CACAO.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:CACAO.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:1905244; P:regulation of modification of synaptic structure; ISO:MGI.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IDA:MGI.
DR GO; GO:0033688; P:regulation of osteoblast proliferation; IMP:BHF-UCL.
DR GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0043149; P:stress fiber assembly; IDA:MGI.
DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; ISO:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0061383; P:trabecula morphogenesis; IMP:BHF-UCL.
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_0000030413"
FT PROPEP 191..193
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT /id="PRO_0000030414"
FT REGION 61..78
FT /note="Switch II region; involved in RAP1GDS1 isoform 3
FT 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:0000305|PubMed:14697203"
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 68
FT /note="R -> C (in Ref. 1; AAC23710)"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4F38"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:4F38"
FT TURN 94..98
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:4F38"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4F38"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4F38"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:4F38"
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
