RND2_MOUSE
ID RND2_MOUSE Reviewed; 227 AA.
AC Q9QYM5; O35279;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Rho-related GTP-binding protein RhoN;
DE AltName: Full=Rho family GTPase 2;
DE AltName: Full=Rho-related GTP-binding protein Rho7;
DE AltName: Full=Rnd2;
DE Flags: Precursor;
GN Name=Rnd2; Synonyms=Arhn, Rho7, Rhon {ECO:0000303|PubMed:10101234};
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=10101234; DOI=10.1016/s0169-328x(99)00039-x;
RA Nishi M., Takeshima H., Houtani T., Nakagawara K., Noda T., Sugimoto T.;
RT "RhoN, a novel small GTP-binding protein expressed predominantly in neurons
RT and hepatic stellate cells.";
RL Brain Res. Mol. Brain Res. 67:74-81(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-227.
RA Stuart R.O., Nigam S.K.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be specifically involved in neuronal and hepatic
CC functions. Is a C3 toxin-insensitive member of the Rho subfamily (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the Rho-GAP domain of RACGAP1. Interacts with
CC UBXD5. Interacts with PRAG1 (By similarity).
CC {ECO:0000250|UniProtKB:P52198, ECO:0000250|UniProtKB:Q5HZE6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Note=Colocalizes with RACGAP1 in Golgi-derived
CC proacrosomal vesicles and the acrosome. {ECO:0000250|UniProtKB:P52198}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in neurons in the brain and
CC spinal cord and also in hepatic stellate cells.
CC {ECO:0000269|PubMed:10101234}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AB017787; BAA76545.1; -; Genomic_DNA.
DR EMBL; AF016482; AAB68844.1; -; mRNA.
DR CCDS; CCDS25473.1; -.
DR RefSeq; NP_033838.1; NM_009708.1.
DR AlphaFoldDB; Q9QYM5; -.
DR SMR; Q9QYM5; -.
DR BioGRID; 198202; 2.
DR STRING; 10090.ENSMUSP00000001347; -.
DR iPTMnet; Q9QYM5; -.
DR PhosphoSitePlus; Q9QYM5; -.
DR MaxQB; Q9QYM5; -.
DR PaxDb; Q9QYM5; -.
DR PRIDE; Q9QYM5; -.
DR ProteomicsDB; 299852; -.
DR Antibodypedia; 29498; 124 antibodies from 26 providers.
DR DNASU; 11858; -.
DR Ensembl; ENSMUST00000001347; ENSMUSP00000001347; ENSMUSG00000001313.
DR GeneID; 11858; -.
DR KEGG; mmu:11858; -.
DR UCSC; uc007lpa.1; mouse.
DR CTD; 8153; -.
DR MGI; MGI:1338755; Rnd2.
DR VEuPathDB; HostDB:ENSMUSG00000001313; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000157020; -.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; Q9QYM5; -.
DR OMA; QMPSRTN; -.
DR OrthoDB; 1283783at2759; -.
DR PhylomeDB; Q9QYM5; -.
DR TreeFam; TF330887; -.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR BioGRID-ORCS; 11858; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Rnd2; mouse.
DR PRO; PR:Q9QYM5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QYM5; protein.
DR Bgee; ENSMUSG00000001313; Expressed in ganglionic eminence and 86 other tissues.
DR ExpressionAtlas; Q9QYM5; baseline and differential.
DR Genevisible; Q9QYM5; MM.
DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
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; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; 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:0048668; P:collateral sprouting; IMP:MGI.
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:0048672; P:positive regulation of collateral sprouting; IMP: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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd04173; Rnd2_Rho7; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041842; RhoN.
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 Cytoplasmic vesicle; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..224
FT /note="Rho-related GTP-binding protein RhoN"
FT /id="PRO_0000198877"
FT PROPEP 225..227
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281229"
FT REGION 186..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 210..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 224
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 224
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 25399 MW; DB3576F96F479F97 CRC64;
MEGQSGRCKI VVVGDAECGK TALLQVFAKD AYPGSYVPTV FENYTASFEI DKRRIELNMW
DTSGSSYYDN VRPLAYPDSD AVLICFDISR PETLDSVLKK WQGETQEFCP NAKVVLVGCK
LDMRTDLATL RELSKQRLIP VTHEQGTVLA KQVGAVSYVE CSSRSSERSV RDVFHVATVA
SLGRGHRQLR RTDSRRGLQR STQLSGRPDR GNEGEMHKDR AKSCNLM
