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P61588 (RND3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho-related GTP-binding protein RhoE
Alternative name(s):
Rho family GTPase 3
Rnd3
Gene names
Name:Rnd3
Synonyms:Arhe, Rhoe
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.

Subunit structure

Interacts with UBXD5 By similarity. Binds ROCK1. Ref.3

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein Ref.3.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processsmall GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 241241Rho-related GTP-binding protein RhoE
PRO_0000198879
Propeptide242 – 2443Removed in mature form By similarity
PRO_0000281231

Regions

Nucleotide binding30 – 378GTP By similarity
Nucleotide binding77 – 815GTP By similarity
Nucleotide binding135 – 1384GTP By similarity
Motif52 – 609Effector region Potential

Amino acid modifications

Modified residue2411Cysteine methyl ester By similarity
Lipidation2411S-farnesyl cysteine

Secondary structure

1 ................................ 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61588 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: DD2D4021CD42BACC

FASTA24427,368
        10         20         30         40         50         60 
MKERRASQKL SSKSIMDPNQ NVKCKIVVVG DSQCGKTALL HVFAKDCFPE NYVPTVFENY 

        70         80         90        100        110        120 
TASFEIDTQR IELSLWDTSG SPYYDNVRPL SYPDSDAVLI CFDISRPETL DSVLKKWKGE 

       130        140        150        160        170        180 
IQEFCPNTKM LLVGCKSDLR TDVSTLVELS NHRQTPVSYD QGANMAKQIG AATYIECSAL 

       190        200        210        220        230        240 
QSENSVRDIF HVATLACVNK TNKNVKRNKS QRATKRISHM PSRPELSAVA TDLRKDKAKS 


CTVM

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[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].
[3]"RhoE binds to ROCK I and inhibits downstream signaling."
Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J.
Mol. Cell. Biol. 23:4219-4229(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ROCK1, SUBCELLULAR LOCATION.
[4]"Crystal structure of the core domain of RhoE/Rnd3: a constitutively activated small G protein."
Garavini H., Riento K., Phelan J.P., McAlister M.S., Ridley A.J., Keep N.H.
Biochemistry 41:6303-6310(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 14-200.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK011442 mRNA. Translation: BAB27622.1.
AK035195 mRNA. Translation: BAC28975.1.
BC009002 mRNA. Translation: AAH09002.1.
IPIIPI00157487.
RefSeqNP_083086.1. NM_028810.2.
UniGeneMm.46497.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWNX-ray2.10A/C16-200[»]
ProteinModelPortalP61588.
ModBaseSearch...

PTM databases

PhosphoSiteP61588.

Proteomic databases

PRIDEP61588.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017288; ENSMUSP00000017288; ENSMUSG00000017144.
GeneID74194.
KEGGmmu:74194.
UCSCuc008jqf.1. mouse.

Organism-specific databases

CTD390.
MGIMGI:1921444. Rnd3.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00700000104387.
HOGENOMHOG000233974.
HOVERGENHBG009351.
InParanoidP61588.
KOK07859.
OMAVELSTHR.
OrthoDBEOG4W6NWT.

Gene expression databases

ArrayExpressP61588.
BgeeP61588.
CleanExMM_RND3.
GenevestigatorP61588.
GermOnlineENSMUSG00000017144. Mus musculus.

Family and domain databases

InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61588.
NextBio1627.
SOURCESearch...

Entry information

Entry nameRND3_MOUSE
AccessionPrimary (citable) accession number: P61588
Secondary accession number(s): P52199, Q6ZWS2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: May 29, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents