RND3_MOUSE
ID RND3_MOUSE Reviewed; 244 AA.
AC P61588; P52199; Q6ZWS2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Rho-related GTP-binding protein RhoE;
DE AltName: Full=Rho family GTPase 3;
DE AltName: Full=Rnd3;
DE Flags: Precursor;
GN Name=Rnd3; Synonyms=Arhe, Rhoe;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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].
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 INTERACTION WITH ROCK1, AND SUBCELLULAR LOCATION.
RX PubMed=12773565; DOI=10.1128/mcb.23.12.4219-4229.2003;
RA Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J.;
RT "RhoE binds to ROCK I and inhibits downstream signaling.";
RL Mol. Cell. Biol. 23:4219-4229(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 14-200.
RX PubMed=12009891; DOI=10.1021/bi025651h;
RA Garavini H., Riento K., Phelan J.P., McAlister M.S., Ridley A.J.,
RA Keep N.H.;
RT "Crystal structure of the core domain of RhoE/Rnd3: a constitutively
RT activated small G protein.";
RL Biochemistry 41:6303-6310(2002).
CC -!- FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is
CC resistant to Rho-specific GTPase-activating proteins.
CC -!- SUBUNIT: Interacts with UBXD5 (By similarity). Binds ROCK1.
CC {ECO:0000250, ECO:0000269|PubMed:12773565}.
CC -!- INTERACTION:
CC P61588; P70335: Rock1; NbExp=7; IntAct=EBI-6930266, EBI-989293;
CC P61588; Q13017: ARHGAP5; Xeno; NbExp=2; IntAct=EBI-6930266, EBI-7237884;
CC P61588; P31946: YWHAB; Xeno; NbExp=5; IntAct=EBI-6930266, EBI-359815;
CC P61588; P62258: YWHAE; Xeno; NbExp=2; IntAct=EBI-6930266, EBI-356498;
CC P61588; P61981: YWHAG; Xeno; NbExp=2; IntAct=EBI-6930266, EBI-359832;
CC P61588; Q04917: YWHAH; Xeno; NbExp=2; IntAct=EBI-6930266, EBI-306940;
CC P61588; P27348: YWHAQ; Xeno; NbExp=2; IntAct=EBI-6930266, EBI-359854;
CC P61588; P63104: YWHAZ; Xeno; NbExp=3; IntAct=EBI-6930266, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12773565}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12773565}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AK011442; BAB27622.1; -; mRNA.
DR EMBL; AK035195; BAC28975.1; -; mRNA.
DR EMBL; BC009002; AAH09002.1; -; mRNA.
DR CCDS; CCDS16028.1; -.
DR RefSeq; NP_083086.1; NM_028810.2.
DR PDB; 1GWN; X-ray; 2.10 A; A/C=16-200.
DR PDBsum; 1GWN; -.
DR AlphaFoldDB; P61588; -.
DR SMR; P61588; -.
DR BioGRID; 216565; 4.
DR IntAct; P61588; 10.
DR MINT; P61588; -.
DR STRING; 10090.ENSMUSP00000017288; -.
DR iPTMnet; P61588; -.
DR PhosphoSitePlus; P61588; -.
DR MaxQB; P61588; -.
DR PaxDb; P61588; -.
DR PeptideAtlas; P61588; -.
DR PRIDE; P61588; -.
DR ProteomicsDB; 300426; -.
DR Antibodypedia; 33646; 232 antibodies from 34 providers.
DR DNASU; 74194; -.
DR Ensembl; ENSMUST00000017288; ENSMUSP00000017288; ENSMUSG00000017144.
DR GeneID; 74194; -.
DR KEGG; mmu:74194; -.
DR UCSC; uc008jqf.1; mouse.
DR CTD; 390; -.
DR MGI; MGI:1921444; Rnd3.
DR VEuPathDB; HostDB:ENSMUSG00000017144; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000157541; -.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; P61588; -.
DR OMA; RPCQKSS; -.
DR OrthoDB; 1283783at2759; -.
DR PhylomeDB; P61588; -.
DR TreeFam; TF330887; -.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR BioGRID-ORCS; 74194; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Rnd3; mouse.
DR EvolutionaryTrace; P61588; -.
DR PRO; PR:P61588; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P61588; protein.
DR Bgee; ENSMUSG00000017144; Expressed in undifferentiated genital tubercle and 239 other tissues.
DR ExpressionAtlas; P61588; baseline and differential.
DR Genevisible; P61588; 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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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: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: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; cd04172; Rnd3_RhoE_Rho8; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041843; RhoE.
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 3D-structure; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..241
FT /note="Rho-related GTP-binding protein RhoE"
FT /id="PRO_0000198879"
FT PROPEP 242..244
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281231"
FT MOTIF 52..60
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 77..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 241
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 241
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:1GWN"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1GWN"
FT STRAND 56..78
FT /evidence="ECO:0007829|PDB:1GWN"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1GWN"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1GWN"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1GWN"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1GWN"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:1GWN"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:1GWN"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1GWN"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:1GWN"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1GWN"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1GWN"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:1GWN"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1GWN"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1GWN"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:1GWN"
SQ SEQUENCE 244 AA; 27368 MW; DD2D4021CD42BACC CRC64;
MKERRASQKL SSKSIMDPNQ NVKCKIVVVG DSQCGKTALL HVFAKDCFPE NYVPTVFENY
TASFEIDTQR IELSLWDTSG SPYYDNVRPL SYPDSDAVLI CFDISRPETL DSVLKKWKGE
IQEFCPNTKM LLVGCKSDLR TDVSTLVELS NHRQTPVSYD QGANMAKQIG AATYIECSAL
QSENSVRDIF HVATLACVNK TNKNVKRNKS QRATKRISHM PSRPELSAVA TDLRKDKAKS
CTVM
