RHOQ_RAT
ID RHOQ_RAT Reviewed; 205 AA.
AC Q9JJL4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Rho-related GTP-binding protein RhoQ;
DE AltName: Full=Ras-like protein TC10;
DE Flags: Precursor;
GN Name=Rhoq; Synonyms=Tc10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10818149; DOI=10.1523/jneurosci.20-11-04138.2000;
RA Tanabe K., Tachibana T., Yamashita T., Che Y.H., Yoneda Y., Ochi T.,
RA Tohyama M., Yoshikawa H., Kiyama H.;
RT "The small GTP-binding protein TC10 promotes nerve elongation in neuronal
RT cells, and its expression is induced during nerve regeneration in rats.";
RL J. Neurosci. 20:4138-4144(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
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 -!- 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. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4 and
CC EXO70 in a GTP-dependent manner. Interacts with ARHGAP33/TCGAP and GOPC
CC (By similarity). Interacts with PARD6A, PARD6G (and probably PARD6B) in
CC a GTP-dependent manner. Part of a quaternary complex containing PARD3,
CC some PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC
CC protein (PRKCI or PRKCZ). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC -!- PTM: May be post-translationally modified by both palmitoylation and
CC polyisoprenylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AB031482; BAA96292.1; -; mRNA.
DR EMBL; BC061760; AAH61760.1; -; mRNA.
DR RefSeq; NP_445974.1; NM_053522.1.
DR AlphaFoldDB; Q9JJL4; -.
DR SMR; Q9JJL4; -.
DR STRING; 10116.ENSRNOP00000020822; -.
DR jPOST; Q9JJL4; -.
DR PaxDb; Q9JJL4; -.
DR PRIDE; Q9JJL4; -.
DR GeneID; 85428; -.
DR UCSC; RGD:621626; rat.
DR CTD; 23433; -.
DR RGD; 621626; Rhoq.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q9JJL4; -.
DR OMA; EKPICME; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q9JJL4; -.
DR TreeFam; TF101109; -.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR PRO; PR:Q9JJL4; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000015415; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; Q9JJL4; RN.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032427; F:GBD domain binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0005522; F:profilin binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..202
FT /note="Rho-related GTP-binding protein RhoQ"
FT /id="PRO_0000198873"
FT PROPEP 203..205
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281224"
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"
SQ SEQUENCE 205 AA; 22645 MW; 827BD9DF8FBF146A CRC64;
MAHGPGALML KCVVVGDGAV GKTCLLMSYA NDAFPEEYVP TVFDHYAVSV TVGGKQYLLG
LYDTAGQEDY DRLRPLSYPM TDVFLICFSV VNPASFQNVK EEWVPELKEY APNVPFLLIG
TQIDLRDDPK TLARLNDMKE KPVCVEQGQK LAKEIGACCY VECSALTQKG LKTVFDEAII
AILTPKKHTV KKRIGSRCIN CCLIT
