RAC1_CAEEL
ID RAC1_CAEEL Reviewed; 191 AA.
AC Q03206; O44463; O44464;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ras-related protein ced-10;
DE AltName: Full=CErac1;
DE AltName: Full=Cell death protein 10;
DE AltName: Full=Cell-corpse engulfment protein ced-10;
DE AltName: Full=Ras-related protein rac-1;
DE Flags: Precursor;
GN Name=ced-10 {ECO:0000312|WormBase:C09G12.8b};
GN Synonyms=rac-1 {ECO:0000312|WormBase:C09G12.8b};
GN ORFNames=C09G12.8 {ECO:0000312|WormBase:C09G12.8b};
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] (ISOFORM B), AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=7677998; DOI=10.1016/s0021-9258(18)54152-1;
RA Chen W., Lim H.H., Lim L.;
RT "A new member of the ras superfamily, the rac1 homologue from
RT Caenorhabditis elegans. Cloning and sequence analysis of cDNA, pattern of
RT developmental expression, and biochemical characterization of the
RT protein.";
RL J. Biol. Chem. 268:320-324(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND FUNCTION.
RX PubMed=10707082; DOI=10.1038/35004000;
RA Reddien P.W., Horvitz H.R.;
RT "CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in
RT Caenorhabditis elegans.";
RL Nat. Cell Biol. 2:131-136(2000).
RN [3]
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 [4]
RP FUNCTION, INTERACTION WITH PAK-1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=8824291; DOI=10.1074/jbc.271.42.26362;
RA Chen W., Chen S., Yap S.F., Lim L.;
RT "The Caenorhabditis elegans p21-activated kinase (CePAK) colocalizes with
RT CeRac1 and CDC42Ce at hypodermal cell boundaries during embryo
RT elongation.";
RL J. Biol. Chem. 271:26362-26368(1996).
RN [5]
RP FUNCTION.
RX PubMed=17050621; DOI=10.1242/dev.02648;
RA Lucanic M., Kiley M., Ashcroft N., L'Etoile N., Cheng H.J.;
RT "The Caenorhabditis elegans P21-activated kinases are differentially
RT required for UNC-6/netrin-mediated commissural motor axon guidance.";
RL Development 133:4549-4559(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MIG-10, AND MUTAGENESIS OF
RP GLY-12 AND GLY-60.
RX PubMed=18499456; DOI=10.1016/j.cub.2008.04.050;
RA Quinn C.C., Pfeil D.S., Wadsworth W.G.;
RT "CED-10/Rac1 mediates axon guidance by regulating the asymmetric
RT distribution of MIG-10/lamellipodin.";
RL Curr. Biol. 18:808-813(2008).
RN [7]
RP FUNCTION.
RX PubMed=19023419; DOI=10.1371/journal.pgen.1000269;
RA Lucanic M., Cheng H.J.;
RT "A RAC/CDC-42-independent GIT/PIX/PAK signaling pathway mediates cell
RT migration in C. elegans.";
RL PLoS Genet. 4:E1000269-E1000269(2008).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLN-61.
RX PubMed=19797046; DOI=10.1534/genetics.109.106880;
RA Locke C.J., Kautu B.B., Berry K.P., Lee S.K., Caldwell K.A., Caldwell G.A.;
RT "Pharmacogenetic analysis reveals a post-developmental role for Rac GTPases
RT in Caenorhabditis elegans GABAergic neurotransmission.";
RL Genetics 183:1357-1372(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20126385; DOI=10.1371/journal.pbio.1000297;
RA Cabello J., Neukomm L.J., Guenesdogan U., Burkart K., Charette S.J.,
RA Lochnit G., Hengartner M.O., Schnabel R.;
RT "The Wnt pathway controls cell death engulfment, spindle orientation, and
RT migration through CED-10/Rac.";
RL PLoS Biol. 8:E1000297-E1000297(2010).
RN [10]
RP FUNCTION.
RX PubMed=24004945; DOI=10.1242/dev.095190;
RA Dalpe G., Tarsitano M., Persico M.G., Zheng H., Culotti J.;
RT "C. elegans PVF-1 inhibits permissive UNC-40 signalling through CED-10
RT GTPase to position the male ray 1 sensillum.";
RL Development 140:4020-4030(2013).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF VAL-190.
RX PubMed=25371370; DOI=10.1242/dev.110437;
RA Norris A.D., Sundararajan L., Morgan D.E., Roberts Z.J., Lundquist E.A.;
RT "The UNC-6/Netrin receptors UNC-40/DCC and UNC-5 inhibit growth cone
RT filopodial protrusion via UNC-73/Trio, Rac-like GTPases and UNC-33/CRMP.";
RL Development 141:4395-4405(2014).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26292279; DOI=10.1371/journal.pgen.1005446;
RA Levy-Strumpf N., Krizus M., Zheng H., Brown L., Culotti J.G.;
RT "The Wnt frizzled receptor MOM-5 regulates the UNC-5 Netrin receptor
RT through small GTPase-dependent signaling to determine the polarity of
RT migrating cells.";
RL PLoS Genet. 11:E1005446-E1005446(2015).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF VAL-190.
RX PubMed=30045855; DOI=10.1534/genetics.118.301234;
RA Gujar M.R., Sundararajan L., Stricker A., Lundquist E.A.;
RT "Control of Growth Cone Polarity, Microtubule Accumulation, and Protrusion
RT by UNC-6/Netrin and Its Receptors in Caenorhabditis elegans.";
RL Genetics 210:235-255(2018).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF GLY-60.
RX PubMed=29346382; DOI=10.1371/journal.pgen.1007125;
RA Offenburger S.L., Ho X.Y., Tachie-Menson T., Coakley S., Hilliard M.A.,
RA Gartner A.;
RT "6-OHDA-induced dopaminergic neurodegeneration in Caenorhabditis elegans is
RT promoted by the engulfment pathway and inhibited by the transthyretin-
RT related protein TTR-33.";
RL PLoS Genet. 14:E1007125-E1007125(2018).
CC -!- FUNCTION: Required in engulfing to control the phagocytosis of
CC apoptotic cell corpses (PubMed:10707082, PubMed:20126385). Required in
CC embryonic development for the correct positioning and orientation of
CC the mitotic spindles and division planes in blastomere cells
CC (PubMed:20126385). Involved in hypodermal cell fusion, together with
CC pak-1 and cdc-42, leading to embryonic body elongation, which involves
CC dramatic cytoskeletal reorganization (PubMed:8824291). ced-2 and ced-5
CC function to activate ced-10 in a GTPase signaling pathway that controls
CC the polarized extension of cell surfaces (PubMed:10707082). Plays a
CC redundant role with mig-2 in dorsal axonal guidance in ventral cord
CC commissural motoneurons and in P neuroblast migration. May regulate
CC these 2 processes by activating pak-1 and/or max-2 (PubMed:17050621).
CC Plays a role, probably via mig-10, in orientating axonal growth of HSN
CC and AVM neurons in response to guidance cues such as slt-1. Regulates
CC mig-10 asymmetric distribution in HSN neurons (PubMed:18499456). During
CC the dorso-ventral axonal guidance and outgrowth of VD neurons, required
CC together with mig-2 to inhibit growth cone filopodial protrusion
CC mediated by netrin guidance cue unc-6 and its receptors unc-5 and unc-
CC 40 (PubMed:25371370, PubMed:30045855). Specifically, regulates growth
CC cone filopodial protrusion polarity, and thus migration, by promoting
CC F-actin polarization and, together with mig-2, by restricting plus-end
CC microtubule accumulation in the growth cone (PubMed:30045855). Plays a
CC role in protecting dopaminergic neurons from oxidative stress-induced
CC degeneration (PubMed:29346382). During gonad morphogenesis, plays a
CC role in distal tip cell (DTC)-mediated guidance of gonad elongation,
CC probably by activating max-2 (PubMed:19797046, PubMed:19023419).
CC Furthermore, plays a role in distal tip cell polarity and migration by
CC negatively regulating the unc-6/Netrin receptor unc-5
CC (PubMed:26292279). May be involved in signal transduction during cell
CC migration (PubMed:10707082). May be involved in the positioning of ray
CC 1, the most anterior ray sensilium, in the male tail (PubMed:24004945).
CC {ECO:0000269|PubMed:10707082, ECO:0000269|PubMed:17050621,
CC ECO:0000269|PubMed:18499456, ECO:0000269|PubMed:19023419,
CC ECO:0000269|PubMed:19797046, ECO:0000269|PubMed:20126385,
CC ECO:0000269|PubMed:24004945, ECO:0000269|PubMed:25371370,
CC ECO:0000269|PubMed:26292279, ECO:0000269|PubMed:29346382,
CC ECO:0000269|PubMed:30045855, ECO:0000269|PubMed:8824291}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with pak-1 (PubMed:8824291). May
CC interact (GTP-bound form) with mig-10 (via Ras-associating and PH
CC domains) (PubMed:18499456). {ECO:0000269|PubMed:18499456,
CC ECO:0000269|PubMed:8824291}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8824291};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000269|PubMed:8824291}. Note=Co-localizes with pak-1 and cdc-42
CC at hypodermal cell boundaries during embryo elongation.
CC {ECO:0000269|PubMed:8824291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:C09G12.8b};
CC IsoId=Q03206-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C09G12.8a};
CC IsoId=Q03206-2; Sequence=VSP_005711;
CC -!- TISSUE SPECIFICITY: Colocalizes with pak-1 to hypodermal cell
CC boundaries during embryo elongation throughout the second phase of
CC embryogenesis. {ECO:0000269|PubMed:8824291}.
CC -!- DEVELOPMENTAL STAGE: Most abundant at embryonic stage, its expression
CC decreases dramatically during development.
CC {ECO:0000269|PubMed:7677998}.
CC -!- DISRUPTION PHENOTYPE: In the second generation, there is defective
CC mitotic spindle orientation in the EMS and ABar blastomeres which
CC results in disrupted left-right asymmetry and failure to undergo
CC morphogenesis (PubMed:20126385). Due to defective apoptotic cell
CC clearance, embryos accumulate apoptotic cell corpses (PubMed:20126385).
CC Distal tip cell migratory defects (PubMed:26292279). Double knockout
CC with unc-5 RNAi suppresses the distal tip cell migratory defect in the
CC ced-10 single mutant (PubMed:26292279). {ECO:0000269|PubMed:20126385,
CC ECO:0000269|PubMed:26292279}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; L03711; AAA28140.1; -; mRNA.
DR EMBL; L04287; AAA28141.1; -; mRNA.
DR EMBL; X68492; CAA48506.1; -; mRNA.
DR EMBL; AF226867; AAF33846.1; -; mRNA.
DR EMBL; BX284604; CCD64025.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD64024.1; -; Genomic_DNA.
DR PIR; A45324; A45324.
DR PIR; G88650; G88650.
DR RefSeq; NP_500362.3; NM_067961.4. [Q03206-2]
DR RefSeq; NP_500363.1; NM_067962.5. [Q03206-1]
DR AlphaFoldDB; Q03206; -.
DR SMR; Q03206; -.
DR BioGRID; 42251; 27.
DR IntAct; Q03206; 1.
DR STRING; 6239.C09G12.8b; -.
DR EPD; Q03206; -.
DR PaxDb; Q03206; -.
DR PeptideAtlas; Q03206; -.
DR EnsemblMetazoa; C09G12.8a.1; C09G12.8a.1; WBGene00000424. [Q03206-2]
DR EnsemblMetazoa; C09G12.8b.1; C09G12.8b.1; WBGene00000424. [Q03206-1]
DR GeneID; 177111; -.
DR KEGG; cel:CELE_C09G12.8; -.
DR UCSC; C09G12.8b; c. elegans. [Q03206-1]
DR CTD; 177111; -.
DR WormBase; C09G12.8a; CE16832; WBGene00000424; ced-10. [Q03206-2]
DR WormBase; C09G12.8b; CE16833; WBGene00000424; ced-10. [Q03206-1]
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000155205; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q03206; -.
DR OMA; EINAVKF; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q03206; -.
DR Reactome; R-CEL-114604; GPVI-mediated activation cascade.
DR Reactome; R-CEL-1433557; Signaling by SCF-KIT.
DR Reactome; R-CEL-193648; NRAGE signals death through JNK.
DR Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-CEL-376172; DSCAM interactions.
DR Reactome; R-CEL-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
DR Reactome; R-CEL-3928664; Ephrin signaling.
DR Reactome; R-CEL-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-CEL-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-CEL-4086400; PCP/CE pathway.
DR Reactome; R-CEL-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-CEL-418885; DCC mediated attractive signaling.
DR Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-CEL-445144; Signal transduction by L1.
DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-CEL-5625740; RHO GTPases activate PKNs.
DR Reactome; R-CEL-5625900; RHO GTPases activate CIT.
DR Reactome; R-CEL-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-CEL-5627123; RHO GTPases activate PAKs.
DR Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-CEL-5663220; RHO GTPases Activate Formins.
DR Reactome; R-CEL-5687128; MAPK6/MAPK4 signaling.
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-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR Reactome; R-CEL-9706019; RHOBTB3 ATPase cycle.
DR Reactome; R-CEL-9748787; Azathioprine ADME.
DR Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q03206; -.
DR PRO; PR:Q03206; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000424; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IGI:WormBase.
DR GO; GO:0031103; P:axon regeneration; IMP:WormBase.
DR GO; GO:0010171; P:body morphogenesis; IGI:WormBase.
DR GO; GO:0016477; P:cell migration; IMP:WormBase.
DR GO; GO:0061643; P:chemorepulsion of axon; IGI:UniProtKB.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0097628; P:distal tip cell migration; IMP:WormBase.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IGI:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IMP:WormBase.
DR GO; GO:0070986; P:left/right axis specification; IMP:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:UniProtKB.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IGI:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IGI:WormBase.
DR GO; GO:0038007; P:netrin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IGI:WormBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IGI:WormBase.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:1905815; P:regulation of dorsal/ventral axon guidance; IMP:UniProtKB.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:UniProtKB.
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 Alternative splicing; Apoptosis; Cell membrane; Developmental protein;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Neurogenesis;
KW Nucleotide-binding; Phagocytosis; Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Ras-related protein ced-10"
FT /id="PRO_0000198891"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281242"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 188
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 188
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 69..130
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_005711"
FT MUTAGEN 12
FT /note="G->V: May be constitutively active. Formation of
FT ectopic processes often branched in PDE neurons."
FT /evidence="ECO:0000269|PubMed:18499456"
FT MUTAGEN 60
FT /note="G->R: In n3246; in HSN neurons, severe reduction in
FT mig-10 ventral enrichment and mild defect in axonal
FT guidance but normal final migration to the ventral nerve
FT cord. Dopaminergic neurodegeneration in 20% of animals in
FT response to oxidative stress-induced by the neurotoxin 6-
FT hydroxydopamine (6-OHDA). Dopaminergic neurodegeneration is
FT partially suppressed in a ttr-33 (gt1983) mutant background
FT in response to 6-OHDA."
FT /evidence="ECO:0000269|PubMed:18499456,
FT ECO:0000269|PubMed:29346382"
FT MUTAGEN 61
FT /note="Q->L: May lock enzyme in its GTP-bound active state.
FT Defect in distal tip cell (DTC) migration."
FT /evidence="ECO:0000269|PubMed:19797046"
FT MUTAGEN 190
FT /note="V->G: In n1993; Disrupts F-actin polarization in VD
FT neuron growth cone. In VD neurons, increases growth cone
FT filopodial protrusion, characterized by an accumulation of
FT plus-end microtubule, and formation of ectopic axons in a
FT mig-2 mu28 mutant background."
FT /evidence="ECO:0000269|PubMed:25371370,
FT ECO:0000269|PubMed:30045855"
FT CONFLICT 177
FT /note="L -> V (in Ref. 1; AAA28140/AAA28141/CAA48506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21455 MW; 1DE85C308B996AFB CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGRP INLGLWDTAG
QEDYDRLRPL SYPQTDVFLV CFALNNPASF ENVRAKWYPE VSHHCPNTPI ILVGTKADLR
EDRDTVERLR ERRLQPVSQT QGYVMAKEIK AVKYLECSAL TQRGLKQVFD EAIRAVLTPP
QRAKKSKCTV L
