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Rho-related GTP-binding protein RhoQ (Ras-like protein TC10) (Ras-like protein family member 7A)

 RHOQ_HUMAN              Reviewed;         205 AA.
P17081; D6W5A6; Q0VGN1; Q52LS8; Q53SJ1; Q6NS39; Q6P146; Q7Z480;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
05-DEC-2018, entry version 184.
RecName: Full=Rho-related GTP-binding protein RhoQ;
AltName: Full=Ras-like protein TC10;
AltName: Full=Ras-like protein family member 7A;
Flags: Precursor;
Name=RHOQ; Synonyms=ARHQ, RASL7A, TC10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2108320; DOI=10.1128/MCB.10.4.1793;
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].
PubMed=12508121; DOI=10.1038/nature01348;
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 GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[6]
INTERACTION WITH CDC42EP1; CDC42EP2 AND CDC42EP3.
TISSUE=Embryo;
PubMed=10490598; DOI=10.1128/MCB.19.10.6585;
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).
[7]
INTERACTION WITH PARD6A AND PARD6G, AND MUTAGENESIS OF GLN-67.
PubMed=10934474; DOI=10.1038/35019573;
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).
[8]
INTERACTION WITH GOPC, AND MUTAGENESIS OF THR-23 AND ASP-44.
PubMed=11162552; DOI=10.1006/bbrc.2000.4160;
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).
[9]
INTERACTION WITH GOPC, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=15546864; DOI=10.1074/jbc.M410026200;
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).
-!- 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. {ECO:0000269|PubMed:15546864}.
-!- ACTIVITY 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 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. {ECO:0000250,
ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:10934474,
ECO:0000269|PubMed:11162552, ECO:0000269|PubMed:15546864}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15546864}.
Cell membrane {ECO:0000269|PubMed:15546864}; Lipid-anchor
{ECO:0000269|PubMed:15546864}.
-!- PTM: May be post-translationally modified by both palmitoylation
and polyisoprenylation.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA36547.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAM21123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M31470; AAA36547.1; ALT_INIT; mRNA.
EMBL; AF498976; AAM21123.1; ALT_INIT; mRNA.
EMBL; AC018682; AAY14834.1; -; Genomic_DNA.
EMBL; CH471053; EAX00251.1; -; Genomic_DNA.
EMBL; BC056154; AAH56154.3; -; mRNA.
EMBL; BC065291; AAH65291.2; -; mRNA.
EMBL; BC070485; AAH70485.2; -; mRNA.
EMBL; BC093805; AAH93805.2; -; mRNA.
EMBL; BC101806; AAI01807.1; -; mRNA.
CCDS; CCDS33191.1; -.
PIR; D34788; TVHUC4.
RefSeq; NP_036381.2; NM_012249.3.
UniGene; Hs.709193; -.
PDB; 2ATX; X-ray; 2.65 A; A/B=1-185.
PDBsum; 2ATX; -.
ProteinModelPortal; P17081; -.
SMR; P17081; -.
BioGrid; 117001; 13.
IntAct; P17081; 7.
STRING; 9606.ENSP00000238738; -.
iPTMnet; P17081; -.
PhosphoSitePlus; P17081; -.
SwissPalm; P17081; -.
BioMuta; RHOQ; -.
DMDM; 62906861; -.
EPD; P17081; -.
PaxDb; P17081; -.
PeptideAtlas; P17081; -.
PRIDE; P17081; -.
ProteomicsDB; 53452; -.
Ensembl; ENST00000238738; ENSP00000238738; ENSG00000119729.
GeneID; 23433; -.
KEGG; hsa:23433; -.
UCSC; uc061ivt.1; human.
CTD; 23433; -.
DisGeNET; 23433; -.
EuPathDB; HostDB:ENSG00000119729.10; -.
GeneCards; RHOQ; -.
HGNC; HGNC:17736; RHOQ.
HPA; HPA044938; -.
MIM; 605857; gene.
neXtProt; NX_P17081; -.
OpenTargets; ENSG00000119729; -.
PharmGKB; PA134904280; -.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00940000155970; -.
HOVERGEN; HBG009351; -.
InParanoid; P17081; -.
KO; K07194; -.
OMA; IMANGTG; -.
PhylomeDB; P17081; -.
TreeFam; TF101109; -.
Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-5627083; RHO GTPases regulate CFTR trafficking.
SignaLink; P17081; -.
SIGNOR; P17081; -.
ChiTaRS; RHOQ; human.
EvolutionaryTrace; P17081; -.
GeneWiki; RHOQ; -.
GenomeRNAi; 23433; -.
PRO; PR:P17081; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000119729; Expressed in 237 organ(s), highest expression level in heart.
CleanEx; HS_RHOQ; -.
ExpressionAtlas; P17081; baseline and differential.
Genevisible; P17081; HS.
GO; GO:0005884; C:actin filament; IDA:BHF-UCL.
GO; GO:0005938; C:cell cortex; IBA:GO_Central.
GO; GO:0042995; C:cell projection; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0032427; F:GBD domain binding; IPI:BHF-UCL.
GO; GO:0005525; F:GTP binding; IBA:GO_Central.
GO; GO:0003924; F:GTPase activity; IDA:BHF-UCL.
GO; GO:0005522; F:profilin binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:BHF-UCL.
GO; GO:0006897; P:endocytosis; IBA:GO_Central.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
GO; GO:0046039; P:GTP metabolic process; IDA:BHF-UCL.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:BHF-UCL.
GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL.
GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IC:BHF-UCL.
GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytoplasm;
GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
Prenylation; Reference proteome.
CHAIN 1 202 Rho-related GTP-binding protein RhoQ.
/FTId=PRO_0000198871.
PROPEP 203 205 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281222.
NP_BIND 16 23 GTP. {ECO:0000250}.
NP_BIND 63 67 GTP. {ECO:0000250}.
NP_BIND 121 124 GTP. {ECO:0000250}.
MOTIF 38 46 Effector region. {ECO:0000250}.
MOD_RES 202 202 Cysteine methyl ester. {ECO:0000250}.
LIPID 202 202 S-farnesyl cysteine. {ECO:0000250}.
MUTAGEN 23 23 T->N: Loss of interaction with GOPC.
{ECO:0000269|PubMed:11162552}.
MUTAGEN 44 44 D->A: Loss of interaction with GOPC.
{ECO:0000269|PubMed:11162552}.
MUTAGEN 67 67 Q->L: Constitutively active. Interacts
with PARD6 proteins and GOPC.
{ECO:0000269|PubMed:10934474}.
STRAND 6 16 {ECO:0000244|PDB:2ATX}.
HELIX 22 31 {ECO:0000244|PDB:2ATX}.
STRAND 46 54 {ECO:0000244|PDB:2ATX}.
STRAND 56 62 {ECO:0000244|PDB:2ATX}.
STRAND 67 70 {ECO:0000244|PDB:2ATX}.
TURN 71 73 {ECO:0000244|PDB:2ATX}.
HELIX 74 77 {ECO:0000244|PDB:2ATX}.
STRAND 82 89 {ECO:0000244|PDB:2ATX}.
HELIX 93 101 {ECO:0000244|PDB:2ATX}.
HELIX 103 110 {ECO:0000244|PDB:2ATX}.
STRAND 116 121 {ECO:0000244|PDB:2ATX}.
HELIX 129 135 {ECO:0000244|PDB:2ATX}.
TURN 136 139 {ECO:0000244|PDB:2ATX}.
HELIX 145 155 {ECO:0000244|PDB:2ATX}.
STRAND 160 162 {ECO:0000244|PDB:2ATX}.
TURN 165 167 {ECO:0000244|PDB:2ATX}.
HELIX 171 183 {ECO:0000244|PDB:2ATX}.
SEQUENCE 205 AA; 22659 MW; 82695B4F8FBF0B75 CRC64;
MAHGPGALML KCVVVGDGAV GKTCLLMSYA NDAFPEEYVP TVFDHYAVSV TVGGKQYLLG
LYDTAGQEDY DRLRPLSYPM TDVFLICFSV VNPASFQNVK EEWVPELKEY APNVPFLLIG
TQIDLRDDPK TLARLNDMKE KPICVEQGQK LAKEIGACCY VECSALTQKG LKTVFDEAII
AILTPKKHTV KKRIGSRCIN CCLIT


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