P61589 (RHOA_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transforming protein RhoA

Gene names

Name:	Rhoa
Synonyms:	Arha, Arha2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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. Required for the apical junction formation of keratinocyte cell-cell adhesion. 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.
Enzyme regulation	GTP hydrolysis is stimulated by ARHGAP30 By similarity.
Subunit structure	Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts with PLCE1 and AKAP13. Interacts with ARHGEF28. 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.
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. Localized to cell-cell contacts in calcium-treated keratinocytes By similarity.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Traceable author statement PubMed 12782387. Source: RGD androgen receptor signaling pathway Inferred from electronic annotation. Source: Compara apical junction assembly Inferred from sequence or structural similarity. Source: UniProtKB cell-matrix adhesion Inferred from electronic annotation. Source: Compara cellular response to progesterone stimulus Non-traceable author statement PubMed 21440892. Source: BHF-UCL cleavage furrow formation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 17615156. Source: RGD negative regulation of intracellular steroid hormone receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of neuron differentiation Inferred from mutant phenotype PubMed 14517206. Source: RGD neuron projection morphogenesis Inferred from expression pattern PubMed 17109064. Source: RGD ossification involved in bone maturation Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of actin filament polymerization Inferred from mutant phenotype PubMed 17369454. Source: RGD positive regulation of cell adhesion Inferred from expression pattern PubMed 17488779. Source: RGD positive regulation of cell cycle cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell growth Inferred from mutant phenotype PubMed 17537920. Source: RGD positive regulation of cell migration Inferred from expression pattern PubMed 17488779. Source: RGD positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype PubMed 17425560. Source: RGD positive regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 17425560. Source: RGD positive regulation of neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of podosome assembly Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle contraction Inferred from mutant phenotype PubMed 17379756. Source: RGD positive regulation of stress fiber assembly Inferred from electronic annotation. Source: Compara positive regulation of translation Inferred from expression pattern PubMed 17562852. Source: RGD positive regulation of vasoconstriction Inferred from expression pattern PubMed 17468135. Source: RGD regulation of calcium ion transport Inferred from mutant phenotype PubMed 17558400. Source: RGD regulation of dendrite development Inferred from mutant phenotype PubMed 17670984. Source: RGD regulation of osteoblast proliferation Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from expression pattern PubMed 17515837. Source: RGD response to drug Inferred from direct assay PubMed 17492663. Source: RGD response to ethanol Inferred from expression pattern PubMed 17109064PubMed 17442046. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern PubMed 18391481. Source: RGD response to glucose stimulus Inferred from expression pattern PubMed 18356410. Source: RGD response to hypoxia Inferred from expression pattern PubMed 16205723. Source: RGD response to mechanical stimulus Inferred from expression pattern PubMed 17456553. Source: RGD skeletal muscle tissue development Inferred from electronic annotation. Source: Compara small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro spindle assembly involved in mitosis Inferred from electronic annotation. Source: Compara stress fiber assembly Inferred from electronic annotation. Source: Compara stress-activated protein kinase signaling cascade Inferred from mutant phenotype PubMed 17369826. Source: RGD trabecula morphogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	apical junction complex Inferred from sequence or structural similarity. Source: UniProtKB axon Inferred from direct assay PubMed 18554585. Source: RGD cell cortex Inferred from sequence or structural similarity. Source: UniProtKB cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay PubMed 21440892. Source: BHF-UCL lamellipodium Inferred from electronic annotation. Source: Compara membrane Inferred from direct assay PubMed 21440892. Source: BHF-UCL midbody Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara ruffle membrane Inferred from electronic annotation. Source: Compara
Molecular_function	GTP binding Traceable author statement PubMed 12782387. Source: RGD GTPase activity Inferred from direct assay PubMed 21440892. Source: BHF-UCL
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_0000030415

Propeptide

191 – 193

3

Removed in mature form By similarity

PRO_0000030416

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

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

193

Helix Strand Turn

Details...

Beta strand

4 – 13

10

Helix

18 – 27

10

Beta strand

43 – 48

6

Beta strand

51 – 58

8

Helix

65 – 69

5

Helix

70 – 72

3

Beta strand

78 – 85

8

Helix

89 – 97

9

Helix

99 – 106

8

Beta strand

112 – 117

6

Helix

119 – 121

3

Helix

125 – 133

9

Helix

141 – 151

11

Beta strand

154 – 158

5

Turn

161 – 164

4

Helix

167 – 179

13

Sequences

	Sequence		Length	Mass (Da)
	P61589 [UniParc]. Last modified May 24, 2004. 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]	"Sequence of Wistar-Kyoto (WKY) and spontaneously hypertensive rat (SHR) RhoA cDNA." Andresen B.T., Jackson E.K., Romero G.G. Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: SHR and Wistar Kyoto.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY026068 mRNA. Translation: AAK11717.1.
AY026069 mRNA. Translation: AAK11718.1.
BC061732 mRNA. Translation: AAH61732.1.

IPI

IPI00201699.

RefSeq

NP_476473.1. NM_057132.3.

UniGene

Rn.107401.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TVD	X-ray	2.99	A/B	1-193	[»]

ProteinModelPortal

P61589.

SMR

P61589. Positions 2-181.

ModBase

Search...

Protein-protein interaction databases

IntAct

P61589. 1 interaction.

MINT

MINT-4542785.

PTM databases

PhosphoSite

P61589.

2D gel databases

World-2DPAGE

0004:P61589.

Proteomic databases

PaxDb

P61589.

PRIDE

P61589.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000071664; ENSRNOP00000066672; ENSRNOG00000050519.

GeneID

117273.

KEGG

rno:117273.

Organism-specific databases

CTD

387.

RGD

619921. Rhoa.

Phylogenomic databases

eggNOG

COG1100.

GeneTree

ENSGT00700000104143.

HOGENOM

HOG000233974.

HOVERGEN

HBG009351.

InParanoid

P61589.

KO

K04513.

OrthoDB

EOG4G4GRD.

Gene expression databases

ArrayExpress

P61589.

Genevestigator

P61589.

GermOnline

ENSRNOG00000012630. Rattus norvegicus.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00174. RHO. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51420. RHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

620199.

Entry information

Entry name

RHOA_RAT

Accession

Primary (citable) accession number: P61589

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	May 29, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program