P61587 (RND3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho-related GTP-binding protein RhoE

Alternative name(s):
Protein MemB
Rho family GTPase 3
Rho-related GTP-binding protein Rho8
Rnd3

Gene names

Name:	RND3
Synonyms:	ARHE, RHO8, RHOE

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	244 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	Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.
Subunit structure	Binds ROCK1 By similarity. Interacts with UBXD5. Ref.8
Subcellular location	Golgi apparatus membrane; Peripheral membrane protein.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Traceable author statement Ref.1. Source: ProtInc cell adhesion Traceable author statement Ref.1. Source: ProtInc small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Traceable author statement Ref.7. Source: ProtInc GTPase activity Traceable author statement Ref.7. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 241

241

Rho-related GTP-binding protein RhoE

PRO_0000198878

Propeptide

242 – 244

3

Removed in mature form By similarity

PRO_0000281230

Regions

Nucleotide binding

30 – 37

8

GTP By similarity

Nucleotide binding

77 – 81

5

GTP By similarity

Nucleotide binding

135 – 138

4

GTP By similarity

Motif

52 – 60

9

Effector region Potential

Amino acid modifications

Modified residue

241

1

Cysteine methyl ester By similarity

Lipidation

241

1

S-farnesyl cysteine Ref.7

Secondary structure

1

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244

Helix Strand Turn

Details...

Beta strand

23 – 31

9

Helix

36 – 45

10

Beta strand

56 – 65

10

Beta strand

70 – 78

9

Helix

82 – 84

3

Turn

85 – 87

3

Helix

88 – 91

4

Beta strand

96 – 103

8

Helix

107 – 115

9

Helix

117 – 124

8

Beta strand

129 – 135

7

Helix

137 – 141

5

Helix

143 – 150

8

Turn

151 – 153

3

Helix

159 – 169

11

Beta strand

172 – 176

5

Turn

179 – 181

3

Helix

183 – 198

16

Sequences

	Sequence		Length	Mass (Da)
	P61587 [UniParc]. Last modified May 24, 2004. Version 1. Checksum: DD2D4021CD42BACC	FASTA	244	27,368
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion." Nobes C.D., Lauritzen I., Mattei M.-G., Paris S., Hall A., Chardin P. J. Cell Biol. 141:187-197(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Spleen.
[2]	"memB, a progression marker of human melanoma cell lines, encodes a member of a rho-related family." van Groningen J.J.M., Van Rijk A.A.F., Bloemers H.P.J., Swart G.W.M. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Kidney.
[7]	"Identification of a novel human Rho protein with unusual properties: GTPase deficiency and in vivo farnesylation." Foster R., Hu K.-Q., Lu Y., Nolan K.M., Thissen J., Settleman J. Mol. Cell. Biol. 16:2689-2699(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-244, CHARACTERIZATION, ISOPRENYLATION AT CYS-241. Tissue: Fetal brain.
[8]	"Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers." Katoh H., Harada A., Mori K., Negishi M. Mol. Cell. Biol. 22:2952-2964(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBXD5.
[9]	"Crystal structure of Rnd3/RhoE: functional implications." Fiegen D., Blumenstein L., Stege P., Vetter I.R., Ahmadian M.R. FEBS Lett. 525:100-104(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-200 IN COMPLEX WITH GTP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X95282 mRNA. Translation: CAA64603.1.
X97758 mRNA. Translation: CAA66352.1.
AF498969 mRNA. Translation: AAM21116.1.
BT006769 mRNA. Translation: AAP35415.1.
CH471058 Genomic DNA. Translation: EAX11524.1.
CH471058 Genomic DNA. Translation: EAX11526.1.
BC012513 mRNA. Translation: AAH12513.1.
S82240 mRNA. Translation: AAB47133.1.

IPI

IPI00001437.

RefSeq

NP_001241667.1. NM_001254738.1.
NP_005159.1. NM_005168.4.

UniGene

Hs.6838.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M7B	X-ray	2.00	A	19-200	[»]
2V55	X-ray	3.70	B/D	1-200	[»]

ProteinModelPortal

P61587.

ModBase

Search...

Protein-protein interaction databases

IntAct

P61587. 2 interactions.

MINT

MINT-3974781.

STRING

9606.ENSP00000263895.

PTM databases

PhosphoSite

P61587.

Polymorphism databases

DMDM

47606459.

Proteomic databases

PaxDb

P61587.

PRIDE

P61587.

Protocols and materials databases

DNASU

390.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263895; ENSP00000263895; ENSG00000115963.
ENST00000375734; ENSP00000364886; ENSG00000115963.

GeneID

390.

KEGG

hsa:390.

UCSC

uc002txe.3. human.

Organism-specific databases

CTD

390.

GeneCards

GC02M151324.

HGNC

HGNC:671. RND3.

MIM

602924. gene.

neXtProt

NX_P61587.

PharmGKB

PA24953.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233974.

HOVERGEN

HBG009351.

InParanoid

P61587.

KO

K07859.

OMA

VELSTHR.

OrthoDB

EOG4W6NWT.

PhylomeDB

P61587.

Gene expression databases

ArrayExpress

P61587.

Bgee

P61587.

CleanEx

HS_RND3.

Genevestigator

P61587.

GermOnline

ENSG00000115963. Homo sapiens.

Family and domain databases

InterPro

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]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51420. RHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P61587.

GenomeRNAi

390.

NextBio

1627.

SOURCE

Search...

Entry information

Entry name

RND3_HUMAN

Accession

Primary (citable) accession number: P61587
Secondary accession number(s): D3DP95, P52199

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.