RHOQ_HUMAN
ID RHOQ_HUMAN Reviewed; 205 AA.
AC P17081; D6W5A6; Q0VGN1; Q52LS8; Q53SJ1; Q6NS39; Q6P146; Q7Z480;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Rho-related GTP-binding protein RhoQ;
DE AltName: Full=Ras-like protein TC10;
DE AltName: Full=Ras-like protein family member 7A;
DE Flags: Precursor;
GN Name=RHOQ; Synonyms=ARHQ, RASL7A, TC10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2108320; DOI=10.1128/mcb.10.4.1793-1798.1990;
RA Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.;
RT "Characterization of four novel ras-like genes expressed in a human
RT teratocarcinoma cell line.";
RL Mol. Cell. Biol. 10:1793-1798(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH CDC42EP1; CDC42EP2 AND CDC42EP3.
RC TISSUE=Embryo;
RX PubMed=10490598; DOI=10.1128/mcb.19.10.6585;
RA Joberty G., Perlungher R.R., Macara I.G.;
RT "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins.";
RL Mol. Cell. Biol. 19:6585-6597(1999).
RN [7]
RP INTERACTION WITH PARD6A AND PARD6G, AND MUTAGENESIS OF GLN-67.
RX PubMed=10934474; DOI=10.1038/35019573;
RA Joberty G., Petersen C., Gao L., Macara I.G.;
RT "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to
RT Cdc42.";
RL Nat. Cell Biol. 2:531-539(2000).
RN [8]
RP INTERACTION WITH GOPC, AND MUTAGENESIS OF THR-23 AND ASP-44.
RX PubMed=11162552; DOI=10.1006/bbrc.2000.4160;
RA Neudauer C.L., Joberty G., Macara I.G.;
RT "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family
RT GTPase TC10.";
RL Biochem. Biophys. Res. Commun. 280:541-547(2001).
RN [9]
RP INTERACTION WITH GOPC, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15546864; DOI=10.1074/jbc.m410026200;
RA Cheng J., Wang H., Guggino W.B.;
RT "Regulation of cystic fibrosis transmembrane regulator trafficking and
RT protein expression by a Rho family small GTPase TC10.";
RL J. Biol. Chem. 280:3731-3739(2005).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC an active GTP-bound and an inactive GDP-bound state. In active state
CC binds to a variety of effector proteins to regulate cellular responses.
CC Involved in epithelial cell polarization processes. May play a role in
CC CFTR trafficking to the plasma membrane. Causes the formation of thin,
CC actin-rich surface projections called filopodia.
CC {ECO:0000269|PubMed:15546864}.
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase.
CC -!- SUBUNIT: Interacts with CDC42EP4 in a GTP-dependent manner. Interacts
CC with ARHGAP33/TCGAP (By similarity). Interacts with CDC42EP1, CDC42EP2,
CC CDC42EP3, PARD6A, PARD6G (and probably PARD6B) in a GTP-dependent
CC manner. Part of a quaternary complex containing PARD3, some PARD6
CC protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein (PRKCI
CC or PRKCZ). Interacts with EXO70 in a GTP-dependent manner. Interacts
CC with GOPC. {ECO:0000250, ECO:0000269|PubMed:10490598,
CC ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:11162552,
CC ECO:0000269|PubMed:15546864}.
CC -!- INTERACTION:
CC P17081; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-689202, EBI-11524452;
CC P17081; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-689202, EBI-10269566;
CC P17081; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-689202, EBI-741158;
CC P17081; Q9BYG5: PARD6B; NbExp=3; IntAct=EBI-689202, EBI-295391;
CC P17081; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-689202, EBI-740727;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15546864}. Cell
CC membrane {ECO:0000269|PubMed:15546864}; Lipid-anchor
CC {ECO:0000269|PubMed:15546864}.
CC -!- PTM: May be post-translationally modified by both palmitoylation and
CC polyisoprenylation.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36547.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAM21123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M31470; AAA36547.1; ALT_INIT; mRNA.
DR EMBL; AF498976; AAM21123.1; ALT_INIT; mRNA.
DR EMBL; AC018682; AAY14834.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00251.1; -; Genomic_DNA.
DR EMBL; BC056154; AAH56154.3; -; mRNA.
DR EMBL; BC065291; AAH65291.2; -; mRNA.
DR EMBL; BC070485; AAH70485.2; -; mRNA.
DR EMBL; BC093805; AAH93805.2; -; mRNA.
DR EMBL; BC101806; AAI01807.1; -; mRNA.
DR CCDS; CCDS33191.1; -.
DR PIR; D34788; TVHUC4.
DR RefSeq; NP_036381.2; NM_012249.3.
DR PDB; 2ATX; X-ray; 2.65 A; A/B=1-185.
DR PDBsum; 2ATX; -.
DR AlphaFoldDB; P17081; -.
DR SMR; P17081; -.
DR BioGRID; 117001; 436.
DR IntAct; P17081; 11.
DR STRING; 9606.ENSP00000238738; -.
DR ChEMBL; CHEMBL4295721; -.
DR iPTMnet; P17081; -.
DR PhosphoSitePlus; P17081; -.
DR SwissPalm; P17081; -.
DR BioMuta; RHOQ; -.
DR DMDM; 62906861; -.
DR jPOST; P17081; -.
DR MassIVE; P17081; -.
DR PaxDb; P17081; -.
DR PeptideAtlas; P17081; -.
DR PRIDE; P17081; -.
DR ProteomicsDB; 53452; -.
DR Antibodypedia; 29975; 150 antibodies from 30 providers.
DR DNASU; 23433; -.
DR Ensembl; ENST00000238738.9; ENSP00000238738.4; ENSG00000119729.12.
DR GeneID; 23433; -.
DR KEGG; hsa:23433; -.
DR MANE-Select; ENST00000238738.9; ENSP00000238738.4; NM_012249.4; NP_036381.2.
DR UCSC; uc061ivt.1; human.
DR CTD; 23433; -.
DR DisGeNET; 23433; -.
DR GeneCards; RHOQ; -.
DR HGNC; HGNC:17736; RHOQ.
DR HPA; ENSG00000119729; Low tissue specificity.
DR MIM; 605857; gene.
DR neXtProt; NX_P17081; -.
DR OpenTargets; ENSG00000119729; -.
DR PharmGKB; PA134904280; -.
DR VEuPathDB; HostDB:ENSG00000119729; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000155970; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P17081; -.
DR OMA; EKPICME; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P17081; -.
DR TreeFam; TF101109; -.
DR PathwayCommons; P17081; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-5627083; RHO GTPases regulate CFTR trafficking.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR SignaLink; P17081; -.
DR SIGNOR; P17081; -.
DR BioGRID-ORCS; 23433; 538 hits in 1040 CRISPR screens.
DR ChiTaRS; RHOQ; human.
DR EvolutionaryTrace; P17081; -.
DR GeneWiki; RHOQ; -.
DR GenomeRNAi; 23433; -.
DR Pharos; P17081; Tbio.
DR PRO; PR:P17081; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P17081; protein.
DR Bgee; ENSG00000119729; Expressed in left ventricle myocardium and 190 other tissues.
DR ExpressionAtlas; P17081; baseline and differential.
DR Genevisible; P17081; HS.
DR GO; GO:0005884; C:actin filament; IDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0032427; F:GBD domain binding; IPI:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:BHF-UCL.
DR GO; GO:0005522; F:profilin binding; IPI:BHF-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:BHF-UCL.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0046039; P:GTP metabolic process; IDA:BHF-UCL.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IC:BHF-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..202
FT /note="Rho-related GTP-binding protein RhoQ"
FT /id="PRO_0000198871"
FT PROPEP 203..205
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281222"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 202
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 202
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 23
FT /note="T->N: Loss of interaction with GOPC."
FT /evidence="ECO:0000269|PubMed:11162552"
FT MUTAGEN 44
FT /note="D->A: Loss of interaction with GOPC."
FT /evidence="ECO:0000269|PubMed:11162552"
FT MUTAGEN 67
FT /note="Q->L: Constitutively active. Interacts with PARD6
FT proteins and GOPC."
FT /evidence="ECO:0000269|PubMed:10934474"
FT STRAND 6..16
FT /evidence="ECO:0007829|PDB:2ATX"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:2ATX"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:2ATX"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:2ATX"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2ATX"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2ATX"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2ATX"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2ATX"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:2ATX"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:2ATX"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2ATX"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:2ATX"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:2ATX"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:2ATX"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2ATX"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2ATX"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:2ATX"
SQ 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
