RHO1_CAEEL
ID RHO1_CAEEL Reviewed; 192 AA.
AC Q22038;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ras-like GTP-binding protein rhoA;
DE Flags: Precursor;
GN Name=rho-1 {ECO:0000312|WormBase:Y51H4A.3a};
GN Synonyms=rhoa {ECO:0000303|PubMed:7798239};
GN ORFNames=Y51H4A.3 {ECO:0000312|WormBase:Y51H4A.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=7798239; DOI=10.1016/s0021-9258(18)31648-x;
RA Chen W., Lim L.;
RT "The Caenorhabditis elegans small GTP-binding protein RhoA is enriched in
RT the nerve ring and sensory neurons during larval development.";
RL J. Biol. Chem. 269:32394-32404(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-14 AND THR-19.
RX PubMed=11687661; DOI=10.1073/pnas.241504098;
RA Spencer A.G., Orita S., Malone C.J., Han M.;
RT "A RHO GTPase-mediated pathway is required during P cell migration in
RT Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13132-13137(2001).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16921365; DOI=10.1038/ncb1459;
RA Motegi F., Sugimoto A.;
RT "Sequential functioning of the ECT-2 RhoGEF, RHO-1 and CDC-42 establishes
RT cell polarity in Caenorhabditis elegans embryos.";
RL Nat. Cell Biol. 8:978-985(2006).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH UNC-89, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18801371; DOI=10.1016/j.jmb.2008.08.083;
RA Qadota H., Blangy A., Xiong G., Benian G.M.;
RT "The DH-PH region of the giant protein UNC-89 activates RHO-1 GTPase in
RT Caenorhabditis elegans body wall muscle.";
RL J. Mol. Biol. 383:747-752(2008).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-14.
RX PubMed=21387015; DOI=10.1371/journal.pone.0017265;
RA McMullan R., Nurrish S.J.;
RT "The RHO-1 RhoGTPase modulates fertility and multiple behaviors in adult C.
RT elegans.";
RL PLoS ONE 6:E17265-E17265(2011).
RN [7]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23064028; DOI=10.1016/j.ydbio.2012.10.001;
RA Spiga F.M., Prouteau M., Gotta M.;
RT "The TAO kinase KIN-18 regulates contractility and establishment of
RT polarity in the C. elegans embryo.";
RL Dev. Biol. 373:26-38(2013).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24016757; DOI=10.1016/j.ydbio.2013.08.024;
RA Fotopoulos N., Wernike D., Chen Y., Makil N., Marte A., Piekny A.;
RT "Caenorhabditis elegans anillin (ani-1) regulates neuroblast cytokinesis
RT and epidermal morphogenesis during embryonic development.";
RL Dev. Biol. 383:61-74(2013).
RN [9]
RP FUNCTION, INTERACTION WITH BLI-3 AND MEMO-1, AND DISRUPTION PHENOTYPE.
RX PubMed=28085666; DOI=10.7554/elife.19493;
RA Ewald C.Y., Hourihan J.M., Bland M.S., Obieglo C., Katic I.,
RA Moronetti Mazzeo L.E., Alcedo J., Blackwell T.K., Hynes N.E.;
RT "NADPH oxidase-mediated redox signaling promotes oxidative stress
RT resistance and longevity through memo-1 in C. elegans.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Required for ventral migration of epidermal cells during
CC ventral enclosure in the embryo and for cell elongation
CC (PubMed:24016757). Also required for ventral migration of P cells
CC during larval development (PubMed:11687661). Involved in asymmetric
CC spindle positioning during anaphase and establishment of cell polarity
CC during embryo development (PubMed:16921365). In adults, involved in
CC regulation of multiple processes including locomotion, pharyngeal
CC pumping, fecundity, ovulation, defecation and body morphology
CC (PubMed:21387015). In body wall muscles, regulates organization of
CC myosin thick filaments downstream of unc-89 (PubMed:18801371).
CC Association with the oxidase bli-3 promotes ROS production and this
CC interaction may be modulated by memo-1, in order to control the
CC oxidative stress response and longevity (PubMed:28085666).
CC {ECO:0000269|PubMed:11687661, ECO:0000269|PubMed:16921365,
CC ECO:0000269|PubMed:18801371, ECO:0000269|PubMed:21387015,
CC ECO:0000269|PubMed:24016757, ECO:0000269|PubMed:28085666}.
CC -!- ACTIVITY REGULATION: GTP hydrolysis is stimulated by unc-89.
CC {ECO:0000269|PubMed:18801371}.
CC -!- SUBUNIT: May interact with unc-89 (via DN and PH domains)
CC (PubMed:18801371). Interacts with bli-3 and memo-1 (PubMed:28085666).
CC {ECO:0000269|PubMed:18801371, ECO:0000269|PubMed:28085666}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7798239};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23064028,
CC ECO:0000269|PubMed:24016757, ECO:0000269|PubMed:7798239}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:23064028}. Note=Associated with the
CC membrane and the cytoskeleton throughout development (PubMed:7798239).
CC Enriched at the anterior cortex in embryos; localization to the
CC anterior cortex requires kin-18 (PubMed:23064028).
CC {ECO:0000269|PubMed:23064028, ECO:0000269|PubMed:7798239}.
CC -!- TISSUE SPECIFICITY: In larvae and adults, enriched at the tip of the
CC head where the anterior sensory organ is located and in the pharyngeal
CC nerve ring (at protein level). In embryos, enriched at the boundaries
CC of dorsal cells undergoing intercalation, ventral enclosure and
CC elongation. {ECO:0000269|PubMed:7798239}.
CC -!- DEVELOPMENTAL STAGE: Highest expression during larval development with
CC a peak at L3 and lower levels in the embryo and adult (at protein
CC level). {ECO:0000269|PubMed:24016757, ECO:0000269|PubMed:7798239}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown predominantly results in
CC embryonic arrest with surviving embryos developing elongation-defective
CC uncoordinated kinky larvae (PubMed:24016757, PubMed:11687661).
CC Defective ventral migration of P cells leading to defective gonad
CC development (PubMed:11687661). Defective establishment of anterior-
CC posterior cell polarity in one-cell embryos (PubMed:16921365).
CC Abolished cortical contractility in early embryos (PubMed:23064028).
CC RNAi-mediated knockdown results in disorganized myosin thick filaments
CC in the body wall muscles of the few surviving adults, which is
CC characterized by the formation of abnormal myosin heavy chain myo-3
CC aggregates, V-shaped crossing of A-bands and areas in which the myosin
CC heavy chain is missing (PubMed:18801371). RNAi-mediated knockdown
CC suppresses reactive oxygen species induction and longevity in the memo-
CC 1 mutant (PubMed:28085666). Double RNAi-mediated knockdown with memo-1
CC eliminates the resistance to oxidative stress in the memo-1 single
CC mutant (PubMed:28085666). {ECO:0000269|PubMed:11687661,
CC ECO:0000269|PubMed:16921365, ECO:0000269|PubMed:18801371,
CC ECO:0000269|PubMed:23064028, ECO:0000269|PubMed:24016757,
CC ECO:0000269|PubMed:28085666}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; L36965; AAC37216.1; -; mRNA.
DR EMBL; AL132952; CAB63379.1; -; Genomic_DNA.
DR PIR; A55492; A55492.
DR RefSeq; NP_502959.1; NM_070558.6.
DR AlphaFoldDB; Q22038; -.
DR SMR; Q22038; -.
DR BioGRID; 43536; 22.
DR IntAct; Q22038; 2.
DR MINT; Q22038; -.
DR STRING; 6239.Y51H4A.3; -.
DR EPD; Q22038; -.
DR PaxDb; Q22038; -.
DR PeptideAtlas; Q22038; -.
DR EnsemblMetazoa; Y51H4A.3a.1; Y51H4A.3a.1; WBGene00004357.
DR GeneID; 178458; -.
DR KEGG; cel:CELE_Y51H4A.3; -.
DR UCSC; Y51H4A.3; c. elegans.
DR CTD; 178458; -.
DR WormBase; Y51H4A.3a; CE25369; WBGene00004357; rho-1.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000163656; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q22038; -.
DR OMA; RWIPEIK; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; Q22038; -.
DR Reactome; R-CEL-114604; GPVI-mediated activation cascade.
DR Reactome; R-CEL-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-CEL-198203; PI3K/AKT activation.
DR Reactome; R-CEL-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
DR Reactome; R-CEL-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-CEL-4086400; PCP/CE pathway.
DR Reactome; R-CEL-416482; G alpha (12/13) signalling events.
DR Reactome; R-CEL-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-CEL-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-CEL-5625740; RHO GTPases activate PKNs.
DR Reactome; R-CEL-5625900; RHO GTPases activate CIT.
DR Reactome; R-CEL-5663220; RHO GTPases Activate Formins.
DR Reactome; R-CEL-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-CEL-5689896; Ovarian tumor domain proteases.
DR Reactome; R-CEL-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013026; RHOB GTPase cycle.
DR Reactome; R-CEL-9013106; RHOC GTPase cycle.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR SignaLink; Q22038; -.
DR PRO; PR:Q22038; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004357; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IDA:WormBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:WormBase.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:WormBase.
DR GO; GO:0003924; F:GTPase activity; IDA:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:WormBase.
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:0031034; P:myosin filament assembly; IMP:WormBase.
DR GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IMP:WormBase.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0032970; P:regulation of actin filament-based process; IMP:WormBase.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IMP:WormBase.
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 Cell cycle; Cell division; Cell membrane; Cytoplasm; Cytoskeleton;
KW Developmental protein; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Mitosis; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..189
FT /note="Ras-like GTP-binding protein rhoA"
FT /id="PRO_0000198884"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281237"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 14
FT /note="G->V: Constitutively active. Normal P cell
FT migration. No effect on viability or fertility."
FT /evidence="ECO:0000269|PubMed:11687661,
FT ECO:0000269|PubMed:21387015"
FT MUTAGEN 19
FT /note="T->N: Dominant negative. Defective ventral migration
FT of P cells leading to defective gonad development. Severely
FT uncoordinated."
FT /evidence="ECO:0000269|PubMed:11687661"
SQ SEQUENCE 192 AA; 21635 MW; 0B10A744D8D0CF81 CRC64;
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PDVYVPTVFE NYVADIEVDG KQVELALWDT
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVRHFCPNV PIILVGNKRD
LRSDPQTVRE LAKMKQEPVK PEQGRAIAEQ IGAFAYLECS AKTKDGIREV FEKATQAALQ
QKKKKKSKCM IL
