P17081 (RHOQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho-related GTP-binding protein RhoQ

Alternative name(s):
Ras-like protein TC10
Ras-like protein family member 7A

Gene names

Name:	RHOQ
Synonyms:	ARHQ, RASL7A, TC10

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	205 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	Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia. Ref.9
Enzyme regulation	Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase.
Subunit structure	Interacts with CDC42EP4 in a GTP-dependent manner. Interacts with ARHGAP33/TCGAP By similarity. Interacts with CDC42EP1, CDC42EP2, CDC42EP3, PARD6A, PARD6G (and probably PARD6B) in a GTP-dependent manner. Part of a quaternary complex containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein (PRKCI or PRKCZ). Interacts with EXO70 in a GTP-dependent manner. Interacts with GOPC. Ref.6 Ref.7 Ref.8 Ref.9
Subcellular location	Cytoplasm. Cell membrane; Lipid-anchor Ref.9.
Post-translational modification	May be post-translationally modified by both palmitoylation and polyisoprenylation.
Sequence similarities	Belongs to the small GTPase superfamily. Rho family.
Sequence caution	The sequence AAA36547.1 differs from that shown. Reason: Erroneous initiation. The sequence AAM21123.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cortical actin cytoskeleton organization Inferred from mutant phenotype PubMed 11821390. Source: BHF-UCL insulin receptor signaling pathway Inferred from mutant phenotype PubMed 11309621. Source: BHF-UCL negative regulation of establishment of protein localization to plasma membrane Inferred from mutant phenotype PubMed 11309621. Source: BHF-UCL positive regulation of filopodium assembly Inferred from direct assay PubMed 10445846. Source: BHF-UCL positive regulation of glucose import Inferred from mutant phenotype PubMed 11309621. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 10445846. Source: BHF-UCL regulation of actin cytoskeleton organization Inferred by curator PubMed 10445846. Source: BHF-UCL regulation of cell shape Inferred from electronic annotation. Source: Compara regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	actin filament Inferred from direct assay PubMed 10445846. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome membrane raft Inferred from electronic annotation. Source: Compara plasma membrane Inferred from direct assay PubMed 10445846. Source: BHF-UCL
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay PubMed 10445846. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 202

202

Rho-related GTP-binding protein RhoQ

PRO_0000198871

Propeptide

203 – 205

3

Removed in mature form By similarity

PRO_0000281222

Regions

Nucleotide binding

16 – 23

8

GTP By similarity

Nucleotide binding

63 – 67

5

GTP By similarity

Nucleotide binding

121 – 124

4

GTP By similarity

Motif

38 – 46

9

Effector region By similarity

Amino acid modifications

Modified residue

202

1

Cysteine methyl ester By similarity

Lipidation

202

1

S-farnesyl cysteine By similarity

Experimental info

Mutagenesis

23

1

T → N: Loss of interaction with GOPC. Ref.8

Mutagenesis

44

1

D → A: Loss of interaction with GOPC. Ref.8

Mutagenesis

67

1

Q → L: Constitutively active. Interacts with PARD6 proteins and GOPC. Ref.7

Secondary structure

1

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205

Helix Strand Turn

Details...

Beta strand

6 – 16

11

Helix

22 – 31

10

Beta strand

46 – 54

9

Beta strand

56 – 62

7

Beta strand

67 – 70

4

Turn

71 – 73

3

Helix

74 – 77

4

Beta strand

82 – 89

8

Helix

93 – 101

9

Helix

103 – 110

8

Beta strand

116 – 121

6

Helix

129 – 135

7

Turn

136 – 139

4

Helix

145 – 155

11

Beta strand

160 – 162

3

Turn

165 – 167

3

Helix

171 – 183

13

Sequences

	Sequence		Length	Mass (Da)
	P17081 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: 82695B4F8FBF0B75	FASTA	205	22,659
	10 20 30 40 50 60 MAHGPGALML KCVVVGDGAV GKTCLLMSYA NDAFPEEYVP TVFDHYAVSV TVGGKQYLLG 70 80 90 100 110 120 LYDTAGQEDY DRLRPLSYPM TDVFLICFSV VNPASFQNVK EEWVPELKEY APNVPFLLIG 130 140 150 160 170 180 TQIDLRDDPK TLARLNDMKE KPICVEQGQK LAKEIGACCY VECSALTQKG LKTVFDEAII 190 200 AILTPKKHTV KKRIGSRCIN CCLIT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line." Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P. Mol. Cell. Biol. 10:1793-1798(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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.
[3]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[5]	"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: Lung and Skin.
[6]	"The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins." Joberty G., Perlungher R.R., Macara I.G. Mol. Cell. Biol. 19:6585-6597(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDC42EP1; CDC42EP2 AND CDC42EP3. Tissue: Embryo.
[7]	"The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42." Joberty G., Petersen C., Gao L., Macara I.G. Nat. Cell Biol. 2:531-539(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARD6A AND PARD6G, MUTAGENESIS OF GLN-67.
[8]	"PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10." Neudauer C.L., Joberty G., Macara I.G. Biochem. Biophys. Res. Commun. 280:541-547(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GOPC, MUTAGENESIS OF THR-23 AND ASP-44.
[9]	"Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10." Cheng J., Wang H., Guggino W.B. J. Biol. Chem. 280:3731-3739(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GOPC, SUBCELLULAR LOCATION, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M31470 mRNA. Translation: AAA36547.1. Different initiation.
AF498976 mRNA. Translation: AAM21123.1. Different initiation.
AC018682 Genomic DNA. Translation: AAY14834.1.
CH471053 Genomic DNA. Translation: EAX00251.1.
BC056154 mRNA. Translation: AAH56154.3.
BC065291 mRNA. Translation: AAH65291.2.
BC070485 mRNA. Translation: AAH70485.2.
BC093805 mRNA. Translation: AAH93805.2.
BC101806 mRNA. Translation: AAI01807.1.

IPI

IPI00012511.

PIR

TVHUC4. D34788.

RefSeq

NP_036381.2. NM_012249.3.

UniGene

Hs.709193.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ATX	X-ray	2.65	A/B	1-185	[»]

ProteinModelPortal

P17081.

ModBase

Search...

Protein-protein interaction databases

IntAct

P17081. 4 interactions.

STRING

9606.ENSP00000238738.

PTM databases

PhosphoSite

P17081.

Polymorphism databases

DMDM

62906861.

Proteomic databases

PaxDb

P17081.

PRIDE

P17081.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000238738; ENSP00000238738; ENSG00000119729.

GeneID

23433.

KEGG

hsa:23433.

UCSC

uc002rva.3. human.

Organism-specific databases

CTD

23433.

GeneCards

GC02P046768.

HGNC

HGNC:17736. RHOQ.

MIM

605857. gene.

neXtProt

NX_P17081.

PharmGKB

PA134904280.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOVERGEN

HBG009351.

InParanoid

P17081.

KO

K07194.

OMA

LAPRCIN.

OrthoDB

EOG434W6W.

Enzyme and pathway databases

Pathway_Interaction_DB

insulin_pathway. Insulin Pathway.
insulin_glucose_pathway. Insulin-mediated glucose transport.

Reactome

REACT_111102. Signal Transduction.

SignaLink

P17081.

Gene expression databases

ArrayExpress

P17081.

Bgee

P17081.

CleanEx

HS_RHOQ.

Genevestigator

P17081.

GermOnline

ENSG00000119729. Homo sapiens.

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

ChiTaRS

RHOQ. human.

EvolutionaryTrace

P17081.

GenomeRNAi

23433.

NextBio

45687.

SOURCE

Search...

Entry information

Entry name

RHOQ_HUMAN

Accession

Primary (citable) accession number: P17081
Secondary accession number(s): D6W5A6 , Q0VGN1, Q52LS8, Q53SJ1, Q6NS39, Q6P146, Q7Z480

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	April 26, 2005
Last modified:	May 29, 2013
This is version 137 of the entry and version 2 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.