Q92730 (RND1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho-related GTP-binding protein Rho6

Alternative name(s):
Rho family GTPase 1
Rnd1

Gene names

Name:	RND1
Synonyms:	RHO6

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	232 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	Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments. Ref.7
Subunit structure	Binds GRB7 and PLXNB1. Interacts with UBXD5. Interacts with PLXNA2. Ref.8 Ref.9 Ref.10
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm › cytoskeleton Ref.9.
Tissue specificity	Mostly expressed in brain and liver.
Sequence similarities	Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Inferred from direct assay Ref.7Ref.1. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome negative regulation of cell adhesion Inferred from direct assay Ref.1. Source: UniProtKB neuron remodeling Inferred from direct assay Ref.7. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	adherens junction Inferred from direct assay Ref.1. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Non-traceable author statement Ref.7Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB7	Q14451	4	EBI-448618,EBI-970191

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 229

229

Rho-related GTP-binding protein Rho6

PRO_0000198874

Propeptide

230 – 232

3

Removed in mature form By similarity

PRO_0000281226

Regions

Nucleotide binding

20 – 27

8

GTP

Nucleotide binding

38 – 45

8

GTP

Nucleotide binding

67 – 71

5

GTP

Nucleotide binding

125 – 128

4

GTP

Motif

42 – 50

9

Effector region Potential

Amino acid modifications

Modified residue

229

1

Cysteine methyl ester By similarity

Lipidation

229

1

S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant

44

1

P → R.
Corresponds to variant rs2270577 [ dbSNP | Ensembl ].

VAR_020188

Experimental info

Mutagenesis

27

1

T → N: Impairs interaction with UBXD5. Ref.9

Mutagenesis

45

1

T → A: Abolishes interaction with UBXD5. Ref.9

Secondary structure

1

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232

Helix Strand Turn

Details...

Beta strand

14 – 19

6

Helix

26 – 35

10

Beta strand

46 – 55

10

Beta strand

60 – 68

9

Helix

72 – 74

3

Turn

75 – 77

3

Helix

78 – 81

4

Beta strand

86 – 93

8

Helix

98 – 104

7

Helix

106 – 114

9

Beta strand

118 – 125

8

Helix

127 – 131

5

Helix

133 – 141

9

Helix

149 – 159

11

Beta strand

162 – 166

5

Turn

169 – 171

3

Helix

173 – 188

16

Sequences

	Sequence		Length	Mass (Da)
	Q92730 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 9FD56ACB878FBCCA	FASTA	232	26,056
	10 20 30 40 50 60 MKERRAPQPV VARCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY TACLETEEQR 70 80 90 100 110 120 VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETV DSALKKWRTE ILDYCPSTRV 130 140 150 160 170 180 LLIGCKTDLR TDLSTLMELS HQKQAPISYE QGCAIAKQLG AEIYLEGSAF TSEKSIHSIF 190 200 210 220 230 RTASMLCLNK PSPLPQKSPV RSLSKRLLHL PSRSELISST FKKEKAKSCS IM

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: Brain.
[2]	"Human Rnd1 in carcinogenesis." Tanaka S., Sugimachi K. Submitted (MAR-2000) 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: Brain.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[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 (JUL-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: Brain.
[7]	"Rnd1, a novel rho family GTPase, induces the formation of neuritic processes in PC12 cells." Aoki J., Katoh H., Mori K., Negishi M. Biochem. Biophys. Res. Commun. 278:604-608(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family." Vayssiere B., Zalcman G., Mahe Y., Mirey G., Ligensa T., Weidner K.M., Chardin P., Camonis J. FEBS Lett. 467:91-96(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB7.
[9]	"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, MUTAGENESIS OF THR-27 AND THR-45, SUBCELLULAR LOCATION.
[10]	"Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells." Oinuma I., Katoh H., Harada A., Negishi M. J. Biol. Chem. 278:25671-25677(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLXNB1.
[11]	"Structure and function of the intracellular region of the plexin-B1 transmembrane receptor." Tong Y., Hota P.K., Penachioni J.Y., Hamaneh M.B., Kim S., Alviani R.S., Shen L., He H., Tempel W., Tamagnone L., Park H.W., Buck M. J. Biol. Chem. 284:35962-35972(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 5-200 IN COMPLEX WITH GDP AND PLXNB1.
[12]	"Crystal structure of plexin A2 RBD in complex with RND1." Structural genomics consortium (SGC) Submitted (JAN-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 5-200 IN COMPLEX WITH PLXNA2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y07923 mRNA. Translation: CAA69228.1.
AB040147 mRNA. Translation: BAB17851.1.
AF498967 mRNA. Translation: AAM21114.1.
AK292762 mRNA. Translation: BAF85451.1.
CH471111 Genomic DNA. Translation: EAW58019.1.
BC026356 mRNA. Translation: AAH26356.1.

IPI

IPI00023211.

RefSeq

NP_055285.1. NM_014470.3.

UniGene

Hs.124940.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CLS	X-ray	2.31	A/B	5-200	[»]
2REX	X-ray	2.30	B/D	5-200	[»]
3Q3J	X-ray	1.97	B	5-200	[»]

ProteinModelPortal

Q92730.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92730. 5 interactions.

MINT

MINT-265539.

STRING

9606.ENSP00000308461.

PTM databases

PhosphoSite

Q92730.

Polymorphism databases

DMDM

2500182.

Proteomic databases

PaxDb

Q92730.

PRIDE

Q92730.

Protocols and materials databases

DNASU

27289.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309739; ENSP00000308461; ENSG00000172602.

GeneID

27289.

KEGG

hsa:27289.

UCSC

uc001rsn.3. human.

Organism-specific databases

CTD

27289.

GeneCards

GC12M049250.

HGNC

HGNC:18314. RND1.

MIM

609038. gene.

neXtProt

NX_Q92730.

PharmGKB

PA134972408.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233974.

HOVERGEN

HBG009351.

InParanoid

Q92730.

KO

K07531.

OMA

VCLNKPS.

OrthoDB

EOG4MW86X.

PhylomeDB

Q92730.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

Q92730.

Bgee

Q92730.

CleanEx

HS_RND1.

Genevestigator

Q92730.

GermOnline

ENSG00000172602. 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

Q92730.

GenomeRNAi

27289.

NextBio

50236.

SOURCE

Search...

Entry information

Entry name

RND1_HUMAN

Accession

Primary (citable) accession number: Q92730
Secondary accession number(s): A8K9P7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 131 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.