RHOG_MOUSE
ID RHOG_MOUSE Reviewed; 191 AA.
AC P84096; P35238; Q8NI04;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Rho-related GTP-binding protein RhoG;
DE AltName: Full=Sid 10750;
DE Flags: Precursor;
GN Name=Rhog; Synonyms=Arhg, Sid10750;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT "Mouse homolog of GTP-binding protein rhoG.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for the formation of membrane ruffles during
CC macropinocytosis. Plays a role in cell migration and is required for
CC the formation of cup-like structures during trans-endothelial migration
CC of leukocytes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARHGEF26. Interacts with ARHGEF16 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AB025943; BAA84696.1; -; mRNA.
DR EMBL; BC059775; AAH59775.1; -; mRNA.
DR CCDS; CCDS21529.1; -.
DR RefSeq; NP_062512.1; NM_019566.3.
DR AlphaFoldDB; P84096; -.
DR SMR; P84096; -.
DR BioGRID; 207846; 6.
DR CORUM; P84096; -.
DR IntAct; P84096; 1.
DR MINT; P84096; -.
DR STRING; 10090.ENSMUSP00000095832; -.
DR ChEMBL; CHEMBL4523268; -.
DR iPTMnet; P84096; -.
DR PhosphoSitePlus; P84096; -.
DR SwissPalm; P84096; -.
DR EPD; P84096; -.
DR jPOST; P84096; -.
DR PaxDb; P84096; -.
DR PeptideAtlas; P84096; -.
DR PRIDE; P84096; -.
DR ProteomicsDB; 255336; -.
DR Antibodypedia; 23440; 201 antibodies from 33 providers.
DR DNASU; 56212; -.
DR Ensembl; ENSMUST00000098230; ENSMUSP00000095832; ENSMUSG00000073982.
DR Ensembl; ENSMUST00000106923; ENSMUSP00000102536; ENSMUSG00000073982.
DR GeneID; 56212; -.
DR KEGG; mmu:56212; -.
DR UCSC; uc009irk.1; mouse.
DR CTD; 391; -.
DR MGI; MGI:1928370; Rhog.
DR VEuPathDB; HostDB:ENSMUSG00000073982; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000155158; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P84096; -.
DR OMA; DNVASKW; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P84096; -.
DR TreeFam; TF101109; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-5625970; RHO GTPases activate KTN1.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 56212; 3 hits in 71 CRISPR screens.
DR PRO; PR:P84096; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P84096; protein.
DR Bgee; ENSMUSG00000073982; Expressed in granulocyte and 236 other tissues.
DR ExpressionAtlas; P84096; baseline and differential.
DR Genevisible; P84096; MM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:1902622; P:regulation of neutrophil migration; IBA:GO_Central.
DR GO; GO:1900027; P:regulation of ruffle assembly; IDA:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
DR CDD; cd01875; RhoG; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR042734; RhoG.
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 Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Rho-related GTP-binding protein RhoG"
FT /id="PRO_0000042030"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042031"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84095"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84095"
FT MOD_RES 188
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 188
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 191 AA; 21309 MW; 0C4FE9C54140F499 CRC64;
MQSIKCVVVG DGAVGKTCLL ICYTTNAFPK EYIPTVFDNY SAQSAVDGRT VNLNLWDTAG
QEEYDRLRTL SYPQTNVFVI CFSIASPPSY ENVRHKWHPE VCHHCPDVPI LLVGTKKDLR
AQPDTLRRLK EQGQAPITPQ QGQALAKQIH AVRYLECSAL QQDGVKEVFA EAVRAVLNPT
PIKRGRSCIL L
