RND3_HUMAN
ID RND3_HUMAN Reviewed; 244 AA.
AC P61587; D3DP95; P52199;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Rho-related GTP-binding protein RhoE;
DE AltName: Full=Protein MemB;
DE AltName: Full=Rho family GTPase 3;
DE AltName: Full=Rho-related GTP-binding protein Rho8;
DE AltName: Full=Rnd3;
DE Flags: Precursor;
GN Name=RND3; Synonyms=ARHE, RHO8, RHOE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=9531558; DOI=10.1083/jcb.141.1.187;
RA Nobes C.D., Lauritzen I., Mattei M.-G., Paris S., Hall A., Chardin P.;
RT "A new member of the Rho family, Rnd1, promotes disassembly of actin
RT filament structures and loss of cell adhesion.";
RL J. Cell Biol. 141:187-197(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA van Groningen J.J.M., Van Rijk A.A.F., Bloemers H.P.J., Swart G.W.M.;
RT "memB, a progression marker of human melanoma cell lines, encodes a member
RT of a rho-related family.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-244, CHARACTERIZATION, AND ISOPRENYLATION
RP AT CYS-241.
RC TISSUE=Fetal brain;
RX PubMed=8649376; DOI=10.1128/mcb.16.6.2689;
RA Foster R., Hu K.-Q., Lu Y., Nolan K.M., Thissen J., Settleman J.;
RT "Identification of a novel human Rho protein with unusual properties:
RT GTPase deficiency and in vivo farnesylation.";
RL Mol. Cell. Biol. 16:2689-2699(1996).
RN [8]
RP INTERACTION WITH UBXD5.
RX PubMed=11940653; DOI=10.1128/mcb.22.9.2952-2964.2002;
RA Katoh H., Harada A., Mori K., Negishi M.;
RT "Socius is a novel Rnd GTPase-interacting protein involved in disassembly
RT of actin stress fibers.";
RL Mol. Cell. Biol. 22:2952-2964(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-200 IN COMPLEX WITH GTP.
RX PubMed=12163169; DOI=10.1016/s0014-5793(02)03094-6;
RA Fiegen D., Blumenstein L., Stege P., Vetter I.R., Ahmadian M.R.;
RT "Crystal structure of Rnd3/RhoE: functional implications.";
RL FEBS Lett. 525:100-104(2002).
CC -!- FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is
CC resistant to Rho-specific GTPase-activating proteins.
CC -!- SUBUNIT: Binds ROCK1 (By similarity). Interacts with UBXD5.
CC {ECO:0000250, ECO:0000269|PubMed:11940653,
CC ECO:0000269|PubMed:12163169}.
CC -!- INTERACTION:
CC P61587; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-1111534, EBI-725606;
CC P61587; Q9BU20: CPLANE2; NbExp=3; IntAct=EBI-1111534, EBI-750332;
CC P61587; O94827-4: PLEKHG5; NbExp=3; IntAct=EBI-1111534, EBI-11980215;
CC P61587; O43157: PLXNB1; NbExp=3; IntAct=EBI-1111534, EBI-1111488;
CC P61587; O15031: PLXNB2; NbExp=2; IntAct=EBI-1111534, EBI-722004;
CC P61587; P31946: YWHAB; NbExp=2; IntAct=EBI-1111534, EBI-359815;
CC P61587; P63104: YWHAZ; NbExp=11; IntAct=EBI-1111534, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RND3ID46247ch2q23.html";
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; X95282; CAA64603.1; -; mRNA.
DR EMBL; X97758; CAA66352.1; -; mRNA.
DR EMBL; AF498969; AAM21116.1; -; mRNA.
DR EMBL; BT006769; AAP35415.1; -; mRNA.
DR EMBL; CH471058; EAX11524.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11526.1; -; Genomic_DNA.
DR EMBL; BC012513; AAH12513.1; -; mRNA.
DR EMBL; S82240; AAB47133.1; -; mRNA.
DR CCDS; CCDS2190.1; -.
DR RefSeq; NP_001241667.1; NM_001254738.1.
DR RefSeq; NP_005159.1; NM_005168.4.
DR PDB; 1M7B; X-ray; 2.00 A; A=19-200.
DR PDB; 2V55; X-ray; 3.70 A; B/D=1-200.
DR PDB; 4BG6; X-ray; 2.30 A; Q/R=232-241.
DR PDBsum; 1M7B; -.
DR PDBsum; 2V55; -.
DR PDBsum; 4BG6; -.
DR AlphaFoldDB; P61587; -.
DR SMR; P61587; -.
DR BioGRID; 106883; 265.
DR IntAct; P61587; 9.
DR MINT; P61587; -.
DR STRING; 9606.ENSP00000364886; -.
DR DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR iPTMnet; P61587; -.
DR PhosphoSitePlus; P61587; -.
DR BioMuta; RND3; -.
DR DMDM; 47606459; -.
DR EPD; P61587; -.
DR jPOST; P61587; -.
DR MassIVE; P61587; -.
DR MaxQB; P61587; -.
DR PaxDb; P61587; -.
DR PeptideAtlas; P61587; -.
DR PRIDE; P61587; -.
DR ProteomicsDB; 57322; -.
DR Antibodypedia; 33646; 232 antibodies from 34 providers.
DR DNASU; 390; -.
DR Ensembl; ENST00000263895.9; ENSP00000263895.4; ENSG00000115963.14.
DR Ensembl; ENST00000375734.6; ENSP00000364886.2; ENSG00000115963.14.
DR GeneID; 390; -.
DR KEGG; hsa:390; -.
DR MANE-Select; ENST00000263895.9; ENSP00000263895.4; NM_005168.5; NP_005159.1.
DR UCSC; uc002txe.4; human.
DR CTD; 390; -.
DR DisGeNET; 390; -.
DR GeneCards; RND3; -.
DR HGNC; HGNC:671; RND3.
DR HPA; ENSG00000115963; Tissue enhanced (esophagus).
DR MIM; 602924; gene.
DR neXtProt; NX_P61587; -.
DR OpenTargets; ENSG00000115963; -.
DR PharmGKB; PA24953; -.
DR VEuPathDB; HostDB:ENSG00000115963; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000157541; -.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; P61587; -.
DR OMA; RPCQKSS; -.
DR OrthoDB; 1283783at2759; -.
DR PhylomeDB; P61587; -.
DR TreeFam; TF330887; -.
DR PathwayCommons; P61587; -.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR SignaLink; P61587; -.
DR SIGNOR; P61587; -.
DR BioGRID-ORCS; 390; 17 hits in 1072 CRISPR screens.
DR ChiTaRS; RND3; human.
DR EvolutionaryTrace; P61587; -.
DR GeneWiki; Rnd3; -.
DR GenomeRNAi; 390; -.
DR Pharos; P61587; Tbio.
DR PRO; PR:P61587; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P61587; protein.
DR Bgee; ENSG00000115963; Expressed in amniotic fluid and 198 other tissues.
DR ExpressionAtlas; P61587; baseline and differential.
DR Genevisible; P61587; HS.
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:0005925; C:focal adhesion; HDA:UniProtKB.
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:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
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 DisProt; DP02804; -.
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_0000198878"
FT PROPEP 242..244
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281230"
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:0000269|PubMed:8649376"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:1M7B"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1M7B"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:1M7B"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:1M7B"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1M7B"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1M7B"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1M7B"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1M7B"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:1M7B"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:1M7B"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1M7B"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:1M7B"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:1M7B"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1M7B"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:1M7B"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1M7B"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1M7B"
FT HELIX 183..198
FT /evidence="ECO:0007829|PDB:1M7B"
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
