RHOD_MOUSE
ID RHOD_MOUSE Reviewed; 210 AA.
AC P97348; O09104;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Rho-related GTP-binding protein RhoD;
DE Flags: Precursor;
GN Name=Rhod; Synonyms=Arhd, Rhom;
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], AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=8945468; DOI=10.1038/384427a0;
RA Murphy C., Saffrich R., Grummt M., Gournier H., Rybin V., Rubino M.,
RA Auvinen P., Luetcke A., Parton R.G., Zerial M.;
RT "Endosome dynamics regulated by a Rho protein.";
RL Nature 384:427-432(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=9395237; DOI=10.1038/sj.onc.1201416;
RA Matsumoto K., Asano T., Endo T.;
RT "Novel small GTPase M-Ras participates in reorganization of actin
RT cytoskeleton.";
RL Oncogene 15:2409-2417(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
RN [5]
RP FUNCTION, AND INTERACTION WITH FILIP1 AND WHAMM.
RX PubMed=23087206; DOI=10.1091/mbc.e12-07-0555;
RA Gad A.K., Nehru V., Ruusala A., Aspenstrom P.;
RT "RhoD regulates cytoskeletal dynamics via the actin nucleation-promoting
RT factor WASp homologue associated with actin Golgi membranes and
RT microtubules.";
RL Mol. Biol. Cell 23:4807-4819(2012).
RN [6]
RP FUNCTION, AND INTERACTION WITH DAPK3.
RX PubMed=23454120; DOI=10.1016/j.bbrc.2013.02.046;
RA Nehru V., Almeida F.N., Aspenstrom P.;
RT "Interaction of RhoD and ZIP kinase modulates actin filament assembly and
RT focal adhesion dynamics.";
RL Biochem. Biophys. Res. Commun. 433:163-169(2013).
RN [7]
RP FUNCTION, INTERACTION WITH ANKFY1, AND SUBCELLULAR LOCATION.
RX PubMed=24102721; DOI=10.1111/tra.12121;
RA Nehru V., Voytyuk O., Lennartsson J., Aspenstroem P.;
RT "RhoD binds the Rab5 effector Rabankyrin-5 and has a role in trafficking of
RT the platelet-derived growth factor receptor.";
RL Traffic 14:1242-1254(2013).
CC -!- FUNCTION: Involved in endosome dynamics. May coordinate membrane
CC transport with the function of the cytoskeleton. Involved in the
CC internalization and trafficking of activated tyrosine kinase receptors
CC such as PDGFRB. Participates in the reorganization of actin
CC cytoskeleton; the function seems to involve WHAMM and includes
CC regulation of filopodia formation and actin filament bundling. Can
CC modulate the effect of DAPK3 in reorganization of actin cytoskeleton
CC and focal adhesion dissolution. {ECO:0000269|PubMed:23087206,
CC ECO:0000269|PubMed:23454120, ECO:0000269|PubMed:24102721,
CC ECO:0000269|PubMed:8945468}.
CC -!- SUBUNIT: Interacts with PAK5. Interacts (in GTP-bound form) with DAPK3,
CC FILIP1 and WHAMM. Interacts (independent of GTP-loaded status) with
CC ANKFY1. {ECO:0000269|PubMed:23087206, ECO:0000269|PubMed:23454120,
CC ECO:0000269|PubMed:24102721}.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Early endosome
CC {ECO:0000269|PubMed:24102721}. Note=Colocalizes with RAB5 to early
CC endosomes. {ECO:0000269|PubMed:24102721}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; X84325; CAA59064.1; -; mRNA.
DR EMBL; D89821; BAA14023.1; -; mRNA.
DR EMBL; BC047989; AAH47989.1; -; mRNA.
DR CCDS; CCDS29427.1; -.
DR RefSeq; NP_031511.1; NM_007485.5.
DR AlphaFoldDB; P97348; -.
DR SMR; P97348; -.
DR BioGRID; 198198; 6.
DR IntAct; P97348; 1.
DR MINT; P97348; -.
DR STRING; 10090.ENSMUSP00000036031; -.
DR iPTMnet; P97348; -.
DR PhosphoSitePlus; P97348; -.
DR SwissPalm; P97348; -.
DR jPOST; P97348; -.
DR PaxDb; P97348; -.
DR PRIDE; P97348; -.
DR ProteomicsDB; 254878; -.
DR Antibodypedia; 16425; 235 antibodies from 28 providers.
DR DNASU; 11854; -.
DR Ensembl; ENSMUST00000048197; ENSMUSP00000036031; ENSMUSG00000041845.
DR GeneID; 11854; -.
DR KEGG; mmu:11854; -.
DR UCSC; uc008gaa.1; mouse.
DR CTD; 29984; -.
DR MGI; MGI:108446; Rhod.
DR VEuPathDB; HostDB:ENSMUSG00000041845; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000161731; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; P97348; -.
DR OMA; PTVFERH; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; P97348; -.
DR TreeFam; TF331746; -.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR BioGRID-ORCS; 11854; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Rhod; mouse.
DR PRO; PR:P97348; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P97348; protein.
DR Bgee; ENSMUSG00000041845; Expressed in saccule of membranous labyrinth and 127 other tissues.
DR ExpressionAtlas; P97348; baseline and differential.
DR Genevisible; P97348; 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:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:MGI.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0006605; P:protein targeting; IMP:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IDA:UniProtKB.
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 Cell membrane; Endosome; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..207
FT /note="Rho-related GTP-binding protein RhoD"
FT /id="PRO_0000198864"
FT PROPEP 208..210
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000223366"
FT MOTIF 46..54
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 71..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 129..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 207
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 207
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 23562 MW; 0D9C1C39AA6D56E9 CRC64;
MNASQVAGEE APQSGHSVKV VLVGDGGCGK TSLMMVFAKG AFPESYSPTV FERYNATLQM
KGKPVHLQIW DTAGQDDYDR LRPLFYPDAN VLLLCFDVTN PNSFDNVSNR WYPEVTHFCK
GVPIIVVGCK IDLRKDKVLV NNLRKKRLEP VTYHRGHDMA RSVGAVAYLE CSARLHDNVE
AVFQEAAEVA LSSRRHNFWR RITQNCCLAT
