RND1_MOUSE
ID RND1_MOUSE Reviewed; 232 AA.
AC Q8BLR7; Q3TSQ9; Q80ZR7; Q8BYF2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Rho-related GTP-binding protein Rho6;
DE AltName: Full=Rho family GTPase 1;
DE AltName: Full=Rnd1;
DE Flags: Precursor;
GN Name=Rnd1; Synonyms=Rho6;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Medulla oblongata, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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: Lacks intrinsic GTPase activity. Has a low affinity for GDP,
CC and constitutively binds GTP. Controls rearrangements of the actin
CC cytoskeleton. Induces the Rac-dependent neuritic process formation in
CC part by disruption of the cortical actin filaments. Causes the
CC formation of many neuritic processes from the cell body with disruption
CC of the cortical actin filaments (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds GRB7 and PLXNB1. Interacts with PLXNA2. Interacts with
CC UBXD5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BLR7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLR7-2; Sequence=VSP_012768;
CC Name=3;
CC IsoId=Q8BLR7-3; Sequence=VSP_012769;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK039992; BAC30492.1; -; mRNA.
DR EMBL; AK043639; BAC31604.1; -; mRNA.
DR EMBL; AK161870; BAE36616.1; -; mRNA.
DR EMBL; BC048531; AAH48531.1; -; mRNA.
DR CCDS; CCDS27801.1; -. [Q8BLR7-1]
DR RefSeq; NP_766200.1; NM_172612.3. [Q8BLR7-1]
DR AlphaFoldDB; Q8BLR7; -.
DR SMR; Q8BLR7; -.
DR IntAct; Q8BLR7; 1.
DR STRING; 10090.ENSMUSP00000003451; -.
DR iPTMnet; Q8BLR7; -.
DR PhosphoSitePlus; Q8BLR7; -.
DR EPD; Q8BLR7; -.
DR MaxQB; Q8BLR7; -.
DR PaxDb; Q8BLR7; -.
DR PRIDE; Q8BLR7; -.
DR ProteomicsDB; 301619; -. [Q8BLR7-1]
DR ProteomicsDB; 301620; -. [Q8BLR7-2]
DR ProteomicsDB; 301621; -. [Q8BLR7-3]
DR Antibodypedia; 25722; 148 antibodies from 27 providers.
DR DNASU; 223881; -.
DR Ensembl; ENSMUST00000003451; ENSMUSP00000003451; ENSMUSG00000054855. [Q8BLR7-1]
DR Ensembl; ENSMUST00000109149; ENSMUSP00000104777; ENSMUSG00000054855. [Q8BLR7-2]
DR Ensembl; ENSMUST00000120997; ENSMUSP00000113830; ENSMUSG00000054855. [Q8BLR7-3]
DR GeneID; 223881; -.
DR KEGG; mmu:223881; -.
DR UCSC; uc007xnh.1; mouse. [Q8BLR7-2]
DR UCSC; uc007xni.1; mouse. [Q8BLR7-1]
DR UCSC; uc007xnj.1; mouse. [Q8BLR7-3]
DR CTD; 27289; -.
DR MGI; MGI:2444878; Rnd1.
DR VEuPathDB; HostDB:ENSMUSG00000054855; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000158666; -.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; Q8BLR7; -.
DR OMA; ISRPDTF; -.
DR OrthoDB; 1395905at2759; -.
DR PhylomeDB; Q8BLR7; -.
DR TreeFam; TF330887; -.
DR Reactome; R-MMU-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-MMU-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 223881; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8BLR7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BLR7; protein.
DR Bgee; ENSMUSG00000054855; Expressed in lumbar subsegment of spinal cord and 126 other tissues.
DR Genevisible; Q8BLR7; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
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:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
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:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0016322; P:neuron remodeling; 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: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 Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1..229
FT /note="Rho-related GTP-binding protein Rho6"
FT /id="PRO_0000198875"
FT PROPEP 230..232
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281227"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 23..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 38..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 169..170
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT MOD_RES 229
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 229
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 152..232
FT /note="GCAIAKQLGAEIYLEGSAFTSETSIHSIFRTASMVCLNKSSPVPPKSPVRSL
FT SKRLLHLPSRSELISTTFKKEKAKSCSIM -> RVLTVLFEPKRKEVGLRLEEKFGGLM
FT YGEPEGRHQQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012768"
FT VAR_SEQ 152..232
FT /note="GCAIAKQLGAEIYLEGSAFTSETSIHSIFRTASMVCLNKSSPVPPKSPVRSL
FT SKRLLHLPSRSELISTTFKKEKAKSCSIM -> VCVHVCVCVCVCVCVCV (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012769"
SQ SEQUENCE 232 AA; 26034 MW; 3C85447748B39F51 CRC64;
MKERRAPQPV VVRCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY TACLETEEQR
VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETM DSALKKWRTE ILDYCPSTRV
LLIGCKTDLR TDLSTLMELS HQKQAPISYE QGCAIAKQLG AEIYLEGSAF TSETSIHSIF
RTASMVCLNK SSPVPPKSPV RSLSKRLLHL PSRSELISTT FKKEKAKSCS IM
