RND1_HUMAN
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 03-AUG-2022, entry version 197.
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}.
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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; 240.
DR DIP; DIP-36741N; -.
DR IntAct; Q92730; 9.
DR MINT; Q92730; -.
DR STRING; 9606.ENSP00000308461; -.
DR iPTMnet; Q92730; -.
DR PhosphoSitePlus; Q92730; -.
DR BioMuta; RND1; -.
DR DMDM; 2500182; -.
DR MassIVE; Q92730; -.
DR PaxDb; Q92730; -.
DR PeptideAtlas; Q92730; -.
DR PRIDE; Q92730; -.
DR ProteomicsDB; 75420; -.
DR Antibodypedia; 25722; 148 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 CTD; 27289; -.
DR DisGeNET; 27289; -.
DR GeneCards; RND1; -.
DR HGNC; HGNC:18314; RND1.
DR HPA; ENSG00000172602; Tissue enhanced (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; ISRPDTF; -.
DR OrthoDB; 1395905at2759; -.
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; 33 hits in 1068 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 tissues.
DR ExpressionAtlas; Q92730; baseline and differential.
DR Genevisible; Q92730; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
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: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: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; IDA:UniProtKB.
DR GO; GO:0016322; P:neuron remodeling; IDA:UniProtKB.
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 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
