Q9QUI0 (RHOA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transforming protein RhoA

Gene names

Name:	Rhoa
Synonyms:	Arha, Arha2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	193 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. 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 By similarity. Required for the apical junction formation of keratinocyte cell-cell adhesion. Ref.9 Ref.10
Enzyme regulation	GTP hydrolysis is stimulated by ARHGAP30 By similarity.
Subunit structure	Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2 and ARHGEF3. Interacts with PLCE1 and AKAP13. Interacts with DIAPH1. Interacts (in the constitutively activated, GTP-bound form) with DGKQ. Interacts with GNB2L1/RACK1; enhances RHOA activation. Interacts with PKP4; the interaction is detected at the midbody. Interacts (GTP-bound form preferentially) with PKN2; the interaction stimulates autophosphorylation and phosphorylation of PKN2 By similarity. Interacts with DIAPH1, NET1, RGNEF and RTKN. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton By similarity. Cleavage furrow By similarity. Cytoplasm › cell cortex By similarity. Midbody By similarity. Note: 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 a activated form and in a myosin- and actin-independent manner By similarity. Localized to cell-cell contacts in calcium-treated keratinocytes. Ref.9
Induction	Up-regulated during keratinocyte differentiation. Ref.9
Post-translational modification	Substrate for botulinum ADP-ribosyltransferase By similarity. Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling By similarity. Ubiquitinated by the BCR(BACURD1) and BCR(BACURD2) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration By similarity.
Sequence similarities	Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Disease	Proto-oncogene
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Phosphoprotein Prenylation Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Rho protein signal transduction Traceable author statement. Source: MGI androgen receptor signaling pathway Inferred from direct assay. Source: MGI cell division Inferred from electronic annotation. Source: UniProtKB-KW cell morphogenesis Inferred from genetic interaction. Source: MGI cell-matrix adhesion Inferred from direct assay. Source: MGI integrin-mediated signaling pathway Traceable author statement. Source: MGI negative regulation of intracellular steroid hormone receptor signaling pathway Inferred from direct assay. Source: MGI negative regulation of neuron apoptosis Inferred from mutant phenotype. Source: MGI positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell cycle cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: MGI skeletal muscle tissue development Inferred from direct assay. Source: MGI stress fiber assembly Inferred from direct assay. Source: MGI
Cellular component	cell cortex Inferred from sequence or structural similarity. Source: UniProtKB cleavage furrow Inferred from sequence or structural similarity. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay. Source: MGI midbody Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI ruffle membrane Inferred from direct assay Ref.6. Source: MGI
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 190	190	Transforming protein RhoA		PRO_0000030413
	Propeptide	191 – 193	3	Removed in mature form By similarity		PRO_0000030414
Regions
	Nucleotide binding	12 – 19	8	GTP By similarity
	Nucleotide binding	59 – 63	5	GTP By similarity
	Nucleotide binding	117 – 120	4	GTP By similarity
	Motif	34 – 42	9	Effector region Potential
	Compositional bias	182 – 187	6	Arg/Lys-rich (basic)
Amino acid modifications
	Modified residue	156	1	Phosphotyrosine By similarity
	Modified residue	188	1	Phosphoserine; by PKG/PRKG1 By similarity
	Modified residue	190	1	Cysteine methyl ester By similarity
	Lipidation	190	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Sequence conflict	68	1	R → C in AAC23710. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9QUI0 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C4C8BDC31FF858BC	FASTA	193	21,782
	10 20 30 40 50 60 MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT 70 80 90 100 110 120 AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD 130 140 150 160 170 180 LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ 190 ARRGKKKSGC LIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transposition of RhoA to the murine Y chromosome." Boettger-Tong H.L., Agulnik A.I., Ty T.I., Bishop C.E. Genomics 49:180-187(1998) [PubMed: 9598304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[2]	Budge P.J., Graham B.S. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c, C57BL/6, CD-1 and FVB/N.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[5]	"Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain." Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N., Fujisawa K., Morii N., Madaule P., Narumiya S. J. Biol. Chem. 271:13556-13560(1996) [PubMed: 8662891] [Abstract] Cited for: INTERACTION WITH RTKN.
[6]	"p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin." Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A., Saito Y., Nakao K., Jockusch B.M., Narumiya S. EMBO J. 16:3044-3056(1997) [PubMed: 9214622] [Abstract] Cited for: INTERACTION WITH DIAPH1.
[7]	"Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7." Alberts A.S., Bouquin N., Johnston L.H., Treisman R. J. Biol. Chem. 273:8616-8622(1998) [PubMed: 9535835] [Abstract] Cited for: INTERACTION WITH NET1.
[8]	"Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules." van Horck F.P.G., Ahmadian M.R., Haeusler L.C., Moolenaar W.H., Kranenburg O. J. Biol. Chem. 276:4948-4956(2001) [PubMed: 11058585] [Abstract] Cited for: INTERACTION WITH RGNEF.
[9]	"Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion." Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J., Dotto G.P. J. Cell Biol. 156:137-148(2002) [PubMed: 11777936] [Abstract] Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
[10]	"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells." Wallace S.W., Magalhaes A., Hall A. Mol. Cell. Biol. 31:81-91(2011) [PubMed: 20974804] [Abstract] Cited for: FUNCTION, INTERACTION WITH PKN2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF014371 mRNA. Translation: AAC23710.1. AF178958 mRNA. Translation: AAD52675.1. AF178959 mRNA. Translation: AAD52676.1. AF178960 mRNA. Translation: AAD52677.1. AF178961 mRNA. Translation: AAD52678.1. AK077606 mRNA. Translation: BAC36896.1. AK083624 mRNA. Translation: BAC38971.1. BC068115 mRNA. Translation: AAH68115.1.
IPI	IPI00315100.
RefSeq	NP_058082.2. NM_016802.4.
UniGene	Mm.471622. Mm.757.
3D structure databases
ProteinModelPortal	Q9QUI0.
SMR	Q9QUI0. Positions 2-181.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29984N.
IntAct	Q9QUI0. 6 interactions.
MINT	MINT-118662.
STRING	Q9QUI0.
PTM databases
PhosphoSite	Q9QUI0.
Proteomic databases
PRIDE	Q9QUI0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000007959; ENSMUSP00000007959; ENSMUSG00000007815.
GeneID	11848.
KEGG	mmu:11848.
Organism-specific databases
CTD	387.
MGI	MGI:1096342. Rhoa.
Phylogenomic databases
eggNOG	roNOG08740.
GeneTree	ENSGT00550000074256.
HOGENOM	HBG745225.
HOVERGEN	HBG009351.
InParanoid	Q9QUI0.
OMA	DSPDSLX.
OrthoDB	EOG4G4GRD.
PhylomeDB	Q9QUI0.
Gene expression databases
ArrayExpress	Q9QUI0.
Bgee	Q9QUI0.
CleanEx	MM_RHOA.
Genevestigator	Q9QUI0.
GermOnline	ENSMUSG00000007815. Mus musculus.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003578. Small_GTPase_Rho. [Graphical view]
KO	K04513.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00174. RHO. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. Small_GTP. 1 hit.
PROSITE	PS51420. RHO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	279815.
SOURCE	Search...

Entry information

Entry name

RHOA_MOUSE

Accession

Primary (citable) accession number: Q9QUI0
Secondary accession number(s): O88336

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program