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Reviewed, UniProtKB/Swiss-Prot P61585 (RHOA_BOVIN)

Last modified November 24, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Transforming protein RhoA
Alternative name(s):
    Gb
    p21
Gene names
Name: RHOA
Synonyms: ARHA, RHO12
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP By similarity.

Cofactor

Magnesium By similarity.

Subunit structure

Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts with PLCE1 and AKAP13. Interacts with RGNEF. Interacts with DIAPH1. Interacts (in the constitutively activated, GTP-bound form) with DGKQ By similarity.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmcytoskeleton.

Post-translational modification

Substrate for botulinum ADP-ribosyltransferase.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Transforming protein RhoA
PRO_0000030407
Propeptide191 – 1933Removed in mature form
PRO_0000030408

Regions

Nucleotide binding12 – 198GTP
Nucleotide binding59 – 635GTP By similarity
Nucleotide binding117 – 1204GTP
Motif34 – 429Effector region Potential
Compositional bias182 – 1876Arg/Lys-rich (basic)

Amino acid modifications

Modified residue411ADP-ribosylasparagine; by botulinum toxin
Modified residue1561Phosphotyrosine By similarity
Modified residue1901Cysteine methyl ester
Lipidation1901S-geranylgeranyl cysteine

Sequences

Sequence LengthMass (Da)Tools
P61585-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: C4DA2DC31FF858BC

FASTA19321,768
        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 LVL 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning of Gb, the substrate for botulinum ADP-ribosyltransferase from bovine adrenal gland and its identification as a rho gene product."
Ogorochi T., Nemoto Y., Nakajima M., Nakamura E., Fujiwara M., Narumiya S.
Biochem. Biophys. Res. Commun. 163:1175-1181(1989) [PubMed: 2506852] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[3]"Substrate for botulinum ADP-ribosyltransferase, Gb, has an amino acid sequence homologous to a putative rho gene product."
Narumiya S., Sekine A., Fujiwara M.
J. Biol. Chem. 263:17255-17257(1988) [PubMed: 3141419] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-25; 42-50; 52-57; 59-97; 99-104; 134-162 AND 169-176.
Tissue: Adrenal gland.
[4]"Guanine nucleotide-dependent ADP-ribosylation of soluble rho catalyzed by Clostridium botulinum C3 ADP-ribosyltransferase. Isolation and characterization of a newly recognized form of rhoA."
Williamson K.C., Smith L.A., Moss J., Vaughan M.
J. Biol. Chem. 265:20807-20812(1990) [PubMed: 2174426] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-70 AND 99-194, ADP-RIBOSYLATION AT ASN-41.
[5]"Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase."
Sekine A., Fujiwara M., Narumiya S.
J. Biol. Chem. 264:8602-8605(1989) [PubMed: 2498316] [Abstract]
Cited for: PROTEIN SEQUENCE OF 37-47, ADP-RIBOSYLATION AT ASN-41.
[6]"The posttranslationally modified C-terminal structure of bovine aortic smooth muscle rhoA p21."
Katayama M., Kawata M., Yoshida Y., Horiuchi H., Yamamoto T., Matsuura Y., Takai Y.
J. Biol. Chem. 266:12639-12645(1991) [PubMed: 1905729] [Abstract]
Cited for: ISOPRENYLATION AT CYS-190.
Tissue: Aortic smooth muscle.
+Additional computationally mapped references.

Cross-references

Sequence databases

M27278 mRNA. Translation: AAA30409.1.
BC102880 mRNA. Translation: AAI02881.1.
IPIIPI00688998.
PIRTVBO12. A33518.
RefSeqNP_788818.1.
UniGeneBt.49678

3D structure databases

SMRP61585. Positions 1-181.
ModBaseSearch...

Protein-protein interaction databases

STRINGP61585.

Proteomic databases

PRIDEP61585.

Genome annotation databases

EnsemblENSBTAT00000005600; ENSBTAP00000005600; ENSBTAG00000004279; Bos taurus. [Genome view]
GeneID338049.
KEGGbta:338049.

Organism-specific databases

CTD338049.

Phylogenomic databases

HOVERGENP61585.
OMAKWIAEVL
OrthoDBEOG969TCZ

Family and domain databases

InterProIPR003578. GTPase_Rho.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRHOA_BOVIN
AccessionPrimary (citable) accession number: P61585
Secondary accession number(s): P06749, Q3ZC72, Q9UEJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 24, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents