ID RND1_HUMAN Reviewed; 232 AA. AC Q92730; A8K9P7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JAN-2024, entry version 205. 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 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=Brain; 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 Tanaka S., Sugimachi K.; RT "Human Rnd1 in carcinogenesis."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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]. RC TISSUE=Lung; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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). RN [7] RP FUNCTION. RX PubMed=11095956; DOI=10.1006/bbrc.2000.3842; RA Aoki J., Katoh H., Mori K., Negishi M.; RT "Rnd1, a novel rho family GTPase, induces the formation of neuritic RT processes in PC12 cells."; RL Biochem. Biophys. Res. Commun. 278:604-608(2000). RN [8] RP INTERACTION WITH GRB7. RX PubMed=10664463; DOI=10.1016/s0014-5793(99)01530-6; RA Vayssiere B., Zalcman G., Mahe Y., Mirey G., Ligensa T., Weidner K.M., RA Chardin P., Camonis J.; RT "Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho RT family."; RL FEBS Lett. 467:91-96(2000). RN [9] RP INTERACTION WITH UBXD5, MUTAGENESIS OF THR-27 AND THR-45, AND SUBCELLULAR RP LOCATION. 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 [10] RP INTERACTION WITH PLXNB1. RX PubMed=12730235; DOI=10.1074/jbc.m303047200; RA Oinuma I., Katoh H., Harada A., Negishi M.; RT "Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated RT Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells."; RL J. Biol. Chem. 278:25671-25677(2003). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 5-200 IN COMPLEX WITH GDP AND RP PLXNB1. RX PubMed=19843518; DOI=10.1074/jbc.m109.056275; RA Tong Y., Hota P.K., Penachioni J.Y., Hamaneh M.B., Kim S., Alviani R.S., RA Shen L., He H., Tempel W., Tamagnone L., Park H.W., Buck M.; RT "Structure and function of the intracellular region of the plexin-B1 RT transmembrane receptor."; RL J. Biol. Chem. 284:35962-35972(2009). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 5-200 IN COMPLEX WITH PLXNA2. RG Structural genomics consortium (SGC); RT "Crystal structure of plexin A2 RBD in complex with RND1."; RL Submitted (JAN-2011) to the PDB data bank. 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. {ECO:0000269|PubMed:11095956}. CC -!- SUBUNIT: Binds GRB7 and PLXNB1. Interacts with UBXD5. Interacts with CC PLXNA2. {ECO:0000269|PubMed:10664463, ECO:0000269|PubMed:11940653, CC ECO:0000269|PubMed:12730235, ECO:0000269|PubMed:19843518, CC ECO:0000269|Ref.12}. CC -!- INTERACTION: CC Q92730; P53365: ARFIP2; NbExp=3; IntAct=EBI-448618, EBI-638194; CC Q92730; Q8TED1: GPX8; NbExp=3; IntAct=EBI-448618, EBI-11721746; CC Q92730; Q14451: GRB7; NbExp=4; IntAct=EBI-448618, EBI-970191; CC Q92730; O43157: PLXNB1; NbExp=4; IntAct=EBI-448618, EBI-1111488; CC Q92730; O43157-1: PLXNB1; NbExp=2; IntAct=EBI-448618, EBI-15880891; CC Q92730; O15031: PLXNB2; NbExp=2; IntAct=EBI-448618, EBI-722004; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11940653}; CC Lipid-anchor {ECO:0000269|PubMed:11940653}; Cytoplasmic side CC {ECO:0000269|PubMed:11940653}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:11940653}. CC -!- TISSUE SPECIFICITY: Mostly expressed in brain and liver. 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; Y07923; CAA69228.1; -; mRNA. DR EMBL; AB040147; BAB17851.1; -; mRNA. DR EMBL; AF498967; AAM21114.1; -; mRNA. DR EMBL; AK292762; BAF85451.1; -; mRNA. DR EMBL; CH471111; EAW58019.1; -; Genomic_DNA. DR EMBL; BC026356; AAH26356.1; -; mRNA. DR CCDS; CCDS8771.1; -. DR RefSeq; NP_055285.1; NM_014470.3. DR PDB; 2CLS; X-ray; 2.31 A; A/B=5-200. DR PDB; 2REX; X-ray; 2.30 A; B/D=5-200. DR PDB; 3Q3J; X-ray; 1.97 A; B=5-200. DR PDBsum; 2CLS; -. DR PDBsum; 2REX; -. DR PDBsum; 3Q3J; -. DR AlphaFoldDB; Q92730; -. DR SMR; Q92730; -. DR BioGRID; 118113; 241. DR DIP; DIP-36741N; -. DR IntAct; Q92730; 10. DR MINT; Q92730; -. DR STRING; 9606.ENSP00000308461; -. DR iPTMnet; Q92730; -. DR PhosphoSitePlus; Q92730; -. DR BioMuta; RND1; -. DR DMDM; 2500182; -. DR MassIVE; Q92730; -. DR PaxDb; 9606-ENSP00000308461; -. DR PeptideAtlas; Q92730; -. DR ProteomicsDB; 75420; -. DR Antibodypedia; 25722; 165 antibodies from 27 providers. DR DNASU; 27289; -. DR Ensembl; ENST00000309739.6; ENSP00000308461.5; ENSG00000172602.11. DR GeneID; 27289; -. DR KEGG; hsa:27289; -. DR MANE-Select; ENST00000309739.6; ENSP00000308461.5; NM_014470.4; NP_055285.1. DR UCSC; uc001rsn.4; human. DR AGR; HGNC:18314; -. DR CTD; 27289; -. DR DisGeNET; 27289; -. DR GeneCards; RND1; -. DR HGNC; HGNC:18314; RND1. DR HPA; ENSG00000172602; Tissue enhanced (brain, liver). DR MIM; 609038; gene. DR neXtProt; NX_Q92730; -. DR OpenTargets; ENSG00000172602; -. DR PharmGKB; PA134972408; -. DR VEuPathDB; HostDB:ENSG00000172602; -. DR eggNOG; KOG0393; Eukaryota. DR GeneTree; ENSGT00940000158666; -. DR HOGENOM; CLU_041217_21_1_1; -. DR InParanoid; Q92730; -. DR OMA; KAKSCCL; -. DR OrthoDB; 20499at2759; -. DR PhylomeDB; Q92730; -. DR TreeFam; TF330887; -. DR PathwayCommons; Q92730; -. DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion. DR Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration. DR Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse. DR Reactome; R-HSA-9696273; RND1 GTPase cycle. DR SignaLink; Q92730; -. DR SIGNOR; Q92730; -. DR BioGRID-ORCS; 27289; 37 hits in 1146 CRISPR screens. DR ChiTaRS; RND1; human. DR EvolutionaryTrace; Q92730; -. DR GeneWiki; Rnd1; -. DR GenomeRNAi; 27289; -. DR Pharos; Q92730; Tbio. DR PRO; PR:Q92730; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q92730; Protein. DR Bgee; ENSG00000172602; Expressed in vena cava and 143 other cell types or tissues. DR ExpressionAtlas; Q92730; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. 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; IPI:UniProtKB. DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB. DR GO; GO:0016322; P:neuron remodeling; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR CDD; cd04174; Rnd1_Rho6; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1. DR PANTHER; PTHR24072:SF23; RHO-RELATED GTP-BINDING PROTEIN RHO6; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51420; RHO; 1. DR Genevisible; Q92730; HS. PE 1: Evidence at protein level; KW 3D-structure; 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_0000198874" FT PROPEP 230..232 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000281226" 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:0000269|PubMed:19843518, FT ECO:0007744|PDB:2CLS" FT BINDING 38..45 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:19843518, FT ECO:0007744|PDB:2CLS" FT BINDING 67..71 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:19843518, FT ECO:0007744|PDB:2CLS" FT BINDING 125..128 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:19843518, FT ECO:0007744|PDB:2CLS" FT BINDING 169..170 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:19843518, FT ECO:0007744|PDB:2CLS" 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 VARIANT 44 FT /note="P -> R (in dbSNP:rs2270577)" FT /id="VAR_020188" FT MUTAGEN 27 FT /note="T->N: Impairs interaction with UBXD5." FT /evidence="ECO:0000269|PubMed:11940653" FT MUTAGEN 45 FT /note="T->A: Abolishes interaction with UBXD5." FT /evidence="ECO:0000269|PubMed:11940653" FT STRAND 10..12 FT /evidence="ECO:0007829|PDB:2REX" FT STRAND 14..19 FT /evidence="ECO:0007829|PDB:3Q3J" FT HELIX 26..35 FT /evidence="ECO:0007829|PDB:3Q3J" FT STRAND 46..55 FT /evidence="ECO:0007829|PDB:3Q3J" FT STRAND 60..68 FT /evidence="ECO:0007829|PDB:3Q3J" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:3Q3J" FT TURN 75..77 FT /evidence="ECO:0007829|PDB:3Q3J" FT HELIX 78..81 FT /evidence="ECO:0007829|PDB:3Q3J" FT STRAND 86..93 FT /evidence="ECO:0007829|PDB:3Q3J" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:3Q3J" FT HELIX 106..114 FT /evidence="ECO:0007829|PDB:3Q3J" FT STRAND 118..125 FT /evidence="ECO:0007829|PDB:3Q3J" FT HELIX 127..131 FT /evidence="ECO:0007829|PDB:3Q3J" FT HELIX 133..141 FT /evidence="ECO:0007829|PDB:3Q3J" FT HELIX 149..159 FT /evidence="ECO:0007829|PDB:3Q3J" FT STRAND 162..166 FT /evidence="ECO:0007829|PDB:3Q3J" FT TURN 169..171 FT /evidence="ECO:0007829|PDB:3Q3J" FT HELIX 173..188 FT /evidence="ECO:0007829|PDB:3Q3J" SQ SEQUENCE 232 AA; 26056 MW; 9FD56ACB878FBCCA CRC64; MKERRAPQPV VARCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY TACLETEEQR VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETV DSALKKWRTE ILDYCPSTRV LLIGCKTDLR TDLSTLMELS HQKQAPISYE QGCAIAKQLG AEIYLEGSAF TSEKSIHSIF RTASMLCLNK PSPLPQKSPV RSLSKRLLHL PSRSELISST FKKEKAKSCS IM //