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UniProtKB/Swiss-Prot entry P17081


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RHOQ_HUMAN
Primary accession number P17081
Secondary accession numbers Q0VGN1 Q52LS8 Q53SJ1 Q6NS39 Q6P146 Q7Z480
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on April 26, 2005 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name Rho-related GTP-binding protein RhoQ [Precursor]
Synonyms Ras-related GTP-binding protein TC10
Ras-like protein family member 7A
Gene name
Name: RHOQ
Synonyms: ARHQ, RASL7A, TC10
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2108320 [NCBI, ExPASy, EBI, Israel, Japan]
Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.;
"Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line.";
Mol. Cell. Biol. 10:1793-1798(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01348; PubMed=12508121 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH CDC42EP1; CDC42EP2 AND CDC42EP3.
TISSUE=Embryo;
PubMed=10490598 [NCBI, ExPASy, EBI, Israel, Japan]
Joberty G., Perlungher R.R., Macara I.G.;
"The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins.";
Mol. Cell. Biol. 19:6585-6597(1999).
[6]
INTERACTION WITH PARD6A AND PARD6G, AND MUTAGENESIS OF GLN-67.
DOI=10.1038/35019573; PubMed=10934474 [NCBI, ExPASy, EBI, Israel, Japan]
Joberty G., Petersen C., Gao L., Macara I.G.;
"The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42.";
Nat. Cell Biol. 2:531-539(2000).
[7]
INTERACTION WITH GOPC, AND MUTAGENESIS OF THR-23 AND ASP-44.
DOI=10.1006/bbrc.2000.4160; PubMed=11162552 [NCBI, ExPASy, EBI, Israel, Japan]
Neudauer C.L., Joberty G., Macara I.G.;
"PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10.";
Biochem. Biophys. Res. Commun. 280:541-547(2001).
[8]
INTERACTION WITH GOPC, SUBCELLULAR LOCATION, AND FUNCTION.
DOI=10.1074/jbc.M410026200; PubMed=15546864 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng J., Wang H., Guggino W.B.;
"Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10.";
J. Biol. Chem. 280:3731-3739(2005).
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.
  • 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: Interacts with CDC42EP4 in a GTP-dependent manner. Interacts with TCGAP/SNX26 (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.
  • INTERACTION:
    Q5VT25:CDC42BPA; NbExp=1; IntAct=EBI-689202, EBI-689171;
    Q6DT37:CDC42BPG; NbExp=1; IntAct=EBI-689202, EBI-689124;
  • SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Lipid-anchor.
  • PTM: May be post-translationally modified by both palmitoylation and polyisoprenylation.
  • SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M31470; AAA36547.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF498976; AAM21123.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC018682; AAY14834.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC056154; AAH56154.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065291; AAH65291.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070485; AAH70485.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093805; AAH93805.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101806; AAI01807.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00012511; -.
PIR D34788; TVHUC4.
RefSeq NP_036381.2; -.
UniGene Hs.709193
3D structure databases
PDB
2ATX; X-ray; 2.65 A; A/B=1-185.[ExPASy / RCSB / EBI]
PDBsum 2ATX; -.
ModBase P17081.
Protein-protein interaction databases
IntAct P17081; 2.
PTM databases
PhosphoSite P17081; -.
Enzyme and pathway databases
Pathway_Interaction_DB insulin_pathway; Insulin Pathway.
insulin_glucose_pathway; Insulin-mediated glucose transport.
Reactome REACT_11044; Signaling by Rho GTPases.
Organism-specific databases
GeneCards GC02P046682; -.
H-InvDB HIX0002030; -.
HIX0057104; -.
HGNC HGNC:17736; RHOQ.
GenAtlas RHOQ.
MIM 605857; gene. [NCBI / EBI]
PharmGKB PA134904280; -.
Gene expression databases
ArrayExpress P17081; -.
Bgee P17081; -.
CleanEx HS_RHOQ; -.
GermOnline ENSG00000119729; Homo sapiens.
Ontologies
GO
GO:0005884; Cellular component: actin filament (inferred from direct assay from UniProtKB).
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from UniProtKB).
GO:0032427; Molecular function: GBD domain binding (inferred from physical interaction from UniProtKB).
GO:0005525; Molecular function: GTP binding (inferred by curator from UniProtKB).
GO:0003924; Molecular function: GTPase activity (inferred from direct assay from UniProtKB).
GO:0005522; Molecular function: profilin binding (inferred from physical interaction from UniProtKB).
GO:0030866; Biological process: cortical actin cytoskeleton organization (inferred from mutant phenotype from UniProtKB).
GO:0006184; Biological process: GTP catabolic process (inferred from direct assay from UniProtKB).
GO:0008286; Biological process: insulin receptor signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0051491; Biological process: positive regulation of filopodium assembly (inferred from direct assay from UniProtKB).
GO:0046326; Biological process: positive regulation of glucose import (inferred from mutant phenotype from UniProtKB).
GO:0010552; Biological process: positive regulation of specific transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
GO:0032956; Biological process: regulation of actin cytoskeleton organization (inferred by curator from UniProtKB).
GO:0070201; Biological process: regulation of establishment of protein localization (inferred from mutant phenotype from UniProtKB).
GO:0007264; Biological process: small GTPase mediated signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003578; GTPase_Rho.
IPR013753; Ras.
IPR001806; Ras_GTPase.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.
Pfam PF00071; Ras; 1.
Pfam graphical view of domain structure.
PRINTS PR00449; RASTRNSFRMNG.
SMART SM00174; RHO; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00231; small_GTP; 1.
PROSITE PS51420; RHO; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P17081; -.
Genome annotation databases
Ensembl ENSG00000119729; Homo sapiens. [Contig view]
GeneID 23433; -.
KEGG hsa:23433; -.
Phylogenomic databases
HOVERGEN P17081; -.
OMA P17081; NDVKEKP.
Other
NextBio 45687; -.
SOURCE RHOQ; Homo sapiens.
ProtoNet P17081.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   202  202     Rho-related GTP-binding protein RhoQ. PRO_0000198871
PROPEP   203   205  3     Removed in mature form (By similarity). PRO_0000281222
NP_BIND   16    23  8     GTP (By similarity). 
NP_BIND   63    67  5     GTP (By similarity). 
NP_BIND   121   124  4     GTP (By similarity). 
MOTIF   38    46  9     Effector region (By similarity). 
MOD_RES   202   202        Cysteine methyl ester (By similarity). 
LIPID   202   202        S-farnesyl cysteine (By similarity). 
MUTAGEN   23    23        T->N: Loss of interaction with GOPC. 
MUTAGEN   44    44        D->A: Loss of interaction with GOPC. 
MUTAGEN   67    67        Q->L: Constitutively active. Interacts with PARD6 proteins and GOPC. 
STRAND   6    16  11      
HELIX   22    31  10      
STRAND   46    54  9      
STRAND   56    62  7      
STRAND   67    70  4      
TURN   71    73  3      
HELIX   74    77  4      
STRAND   82    89  8      
HELIX   93   101  9      
HELIX   103   110  8      
STRAND   116   121  6      
HELIX   129   135  7      
TURN   136   139  4      
HELIX   145   155  11      
STRAND   160   162  3      
TURN   165   167  3      
HELIX   171   183  13      
Sequence information
Length: 205 AA [This is the length of the unprocessed precursor] Molecular weight: 22659 Da [This is the MW of the unprocessed precursor] CRC64: 82695B4F8FBF0B75 [This is a checksum on the sequence]
        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 

P17081 in FASTA format

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