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Ras-related protein ced-10 (CErac1) (Cell death protein 10) (Cell-corpse engulfment protein ced-10) (Ras-related protein rac-1)

 RAC1_CAEEL              Reviewed;         191 AA.
Q03206; O44463; O44464;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
23-MAY-2018, entry version 155.
RecName: Full=Ras-related protein ced-10;
AltName: Full=CErac1;
AltName: Full=Cell death protein 10;
AltName: Full=Cell-corpse engulfment protein ced-10;
AltName: Full=Ras-related protein rac-1;
Flags: Precursor;
Name=ced-10; Synonyms=rac-1; ORFNames=C09G12.8;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND DEVELOPMENTAL STAGE.
STRAIN=Bristol N2;
PubMed=7677998;
Chen W., Lim H.H., Lim L.;
"A new member of the ras superfamily, the rac1 homologue from
Caenorhabditis elegans. Cloning and sequence analysis of cDNA, pattern
of developmental expression, and biochemical characterization of the
protein.";
J. Biol. Chem. 268:320-324(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
PubMed=10707082; DOI=10.1038/35004000;
Reddien P.W., Horvitz H.R.;
"CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in
Caenorhabditis elegans.";
Nat. Cell Biol. 2:131-136(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4]
FUNCTION, INTERACTION WITH PAK-1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=Bristol N2;
PubMed=8824291; DOI=10.1074/jbc.271.42.26362;
Chen W., Chen S., Yap S.F., Lim L.;
"The Caenorhabditis elegans p21-activated kinase (CePAK) colocalizes
with CeRac1 and CDC42Ce at hypodermal cell boundaries during embryo
elongation.";
J. Biol. Chem. 271:26362-26368(1996).
[5]
FUNCTION.
PubMed=17050621; DOI=10.1242/dev.02648;
Lucanic M., Kiley M., Ashcroft N., L'Etoile N., Cheng H.J.;
"The Caenorhabditis elegans P21-activated kinases are differentially
required for UNC-6/netrin-mediated commissural motor axon guidance.";
Development 133:4549-4559(2006).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MIG-10, AND
MUTAGENESIS OF GLY-12 AND GLY-60.
PubMed=18499456; DOI=10.1016/j.cub.2008.04.050;
Quinn C.C., Pfeil D.S., Wadsworth W.G.;
"CED-10/Rac1 mediates axon guidance by regulating the asymmetric
distribution of MIG-10/lamellipodin.";
Curr. Biol. 18:808-813(2008).
[7]
FUNCTION.
PubMed=19023419; DOI=10.1371/journal.pgen.1000269;
Lucanic M., Cheng H.J.;
"A RAC/CDC-42-independent GIT/PIX/PAK signaling pathway mediates cell
migration in C. elegans.";
PLoS Genet. 4:E1000269-E1000269(2008).
[8]
FUNCTION, AND MUTAGENESIS OF GLN-61.
PubMed=19797046; DOI=10.1534/genetics.109.106880;
Locke C.J., Kautu B.B., Berry K.P., Lee S.K., Caldwell K.A.,
Caldwell G.A.;
"Pharmacogenetic analysis reveals a post-developmental role for Rac
GTPases in Caenorhabditis elegans GABAergic neurotransmission.";
Genetics 183:1357-1372(2009).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20126385; DOI=10.1371/journal.pbio.1000297;
Cabello J., Neukomm L.J., Guenesdogan U., Burkart K., Charette S.J.,
Lochnit G., Hengartner M.O., Schnabel R.;
"The Wnt pathway controls cell death engulfment, spindle orientation,
and migration through CED-10/Rac.";
PLoS Biol. 8:E1000297-E1000297(2010).
[10]
FUNCTION.
PubMed=24004945; DOI=10.1242/dev.095190;
Dalpe G., Tarsitano M., Persico M.G., Zheng H., Culotti J.;
"C. elegans PVF-1 inhibits permissive UNC-40 signalling through CED-10
GTPase to position the male ray 1 sensillum.";
Development 140:4020-4030(2013).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26292279; DOI=10.1371/journal.pgen.1005446;
Levy-Strumpf N., Krizus M., Zheng H., Brown L., Culotti J.G.;
"The Wnt frizzled receptor MOM-5 regulates the UNC-5 Netrin receptor
through small GTPase-dependent signaling to determine the polarity of
migrating cells.";
PLoS Genet. 11:E1005446-E1005446(2015).
-!- FUNCTION: Required in engulfing to control the phagocytosis of
apoptotic cell corpses (PubMed:10707082, PubMed:20126385).
Required in embryonic development for the correct positioning and
orientation of the mitotic spindles and division planes in
blastomere cells (PubMed:20126385). Involved in hypodermal cell
fusion, together with pak-1 and cdc-42, leading to embryonic body
elongation, which involves dramatic cytoskeletal reorganization
(PubMed:8824291). Ced-2 and ced-5 function to activate ced-10 in a
GTPase signaling pathway that controls the polarized extension of
cell surfaces (PubMed:10707082). Plays a redundant role with mig-2
in dorsal axonal guidance in ventral cord commissural motoneurons
and in P neuroblast migration. May regulate these 2 processes by
activating pak-1 and/or max-2 (PubMed:17050621). Plays a role,
probably via mig-10, in orientating axonal growth of HSN and AVM
neurons in response to guidance cues such as slt-1. Regulates mig-
10 asymmetric distribution in HSN neurons (PubMed:18499456).
During gonad morphogenesis, plays a role in distal tip cell (DTC)-
mediated guidance of gonad elongation, probably by activating max-
2 (PubMed:19797046, PubMed:19023419). Furthermore, plays a role in
distal tip cell polarity and migration by negatively regulating
the unc-6/Netrin receptor unc-5 (PubMed:26292279). May be involved
in signal transduction during cell migration (PubMed:10707082).
May be involved in the positioning of ray 1, the most anterior ray
sensilium, in the male tail (PubMed:24004945).
{ECO:0000269|PubMed:10707082, ECO:0000269|PubMed:17050621,
ECO:0000269|PubMed:18499456, ECO:0000269|PubMed:19023419,
ECO:0000269|PubMed:19797046, ECO:0000269|PubMed:20126385,
ECO:0000269|PubMed:24004945, ECO:0000269|PubMed:26292279,
ECO:0000269|PubMed:8824291}.
-!- SUBUNIT: Interacts (GTP-bound form) with pak-1 (PubMed:8824291).
May interact (GTP-bound form) with mig-10 (via Ras-associating and
PH domains) (PubMed:18499456). {ECO:0000269|PubMed:18499456,
ECO:0000269|PubMed:8824291}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8824291};
Lipid-anchor {ECO:0000305}; Cytoplasmic side
{ECO:0000269|PubMed:8824291}. Note=Co-localizes with pak-1 and
cdc-42 at hypodermal cell boundaries during embryo elongation.
{ECO:0000269|PubMed:8824291}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a;
IsoId=Q03206-1; Sequence=Displayed;
Name=b;
IsoId=Q03206-2; Sequence=VSP_005711;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Colocalizes with pak-1 to hypodermal cell
boundaries during embryo elongation throughout the second phase of
embryogenesis. {ECO:0000269|PubMed:8824291}.
-!- DEVELOPMENTAL STAGE: Most abundant at embryonic stage, its
expression decreases dramatically during development.
{ECO:0000269|PubMed:7677998}.
-!- DISRUPTION PHENOTYPE: In the second generation, there is defective
mitotic spindle orientation in the EMS and ABar blastomeres which
results in disrupted left-right asymmetry and failure to undergo
morphogenesis (PubMed:20126385). Due to defective apoptotic cell
clearance, embryos accumulate apoptotic cell corpses
(PubMed:20126385). Distal tip cell migratory defects
(PubMed:26292279). Double knockout with unc-5 RNAi suppresses the
distal tip cell migratory defect in the ced-10 single mutant
(PubMed:26292279). {ECO:0000269|PubMed:20126385,
ECO:0000269|PubMed:26292279}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L03711; AAA28140.1; -; mRNA.
EMBL; L04287; AAA28141.1; -; mRNA.
EMBL; X68492; CAA48506.1; -; mRNA.
EMBL; AF226867; AAF33846.1; -; mRNA.
EMBL; FO080481; CCD64025.1; -; Genomic_DNA.
EMBL; FO080481; CCD64024.1; -; Genomic_DNA.
PIR; A45324; A45324.
PIR; G88650; G88650.
RefSeq; NP_500362.3; NM_067961.4. [Q03206-2]
RefSeq; NP_500363.1; NM_067962.5. [Q03206-1]
UniGene; Cel.19354; -.
ProteinModelPortal; Q03206; -.
SMR; Q03206; -.
BioGrid; 42251; 14.
IntAct; Q03206; 1.
STRING; 6239.C09G12.8b.1; -.
EPD; Q03206; -.
PaxDb; Q03206; -.
PeptideAtlas; Q03206; -.
PRIDE; Q03206; -.
EnsemblMetazoa; C09G12.8b; C09G12.8b; WBGene00000424. [Q03206-1]
GeneID; 177111; -.
KEGG; cel:CELE_C09G12.8; -.
UCSC; C09G12.8b; c. elegans. [Q03206-1]
CTD; 177111; -.
WormBase; C09G12.8a; CE16832; WBGene00000424; ced-10. [Q03206-2]
WormBase; C09G12.8b; CE16833; WBGene00000424; ced-10. [Q03206-1]
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000118978; -.
HOGENOM; HOG000233974; -.
InParanoid; Q03206; -.
KO; K04392; -.
OMA; KAKWFPE; -.
OrthoDB; EOG091G0KCM; -.
PhylomeDB; Q03206; -.
Reactome; R-CEL-114604; GPVI-mediated activation cascade.
Reactome; R-CEL-1433557; Signaling by SCF-KIT.
Reactome; R-CEL-193648; NRAGE signals death through JNK.
Reactome; R-CEL-194840; Rho GTPase cycle.
Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-CEL-389359; CD28 dependent Vav1 pathway.
Reactome; R-CEL-3928662; EPHB-mediated forward signaling.
Reactome; R-CEL-3928664; Ephrin signaling.
Reactome; R-CEL-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-CEL-4086400; PCP/CE pathway.
Reactome; R-CEL-416482; G alpha (12/13) signalling events.
Reactome; R-CEL-418885; DCC mediated attractive signaling.
Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-CEL-445144; Signal transduction by L1.
Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-CEL-5625740; RHO GTPases activate PKNs.
Reactome; R-CEL-5626467; RHO GTPases activate IQGAPs.
Reactome; R-CEL-5627123; RHO GTPases activate PAKs.
Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-CEL-5687128; MAPK6/MAPK4 signaling.
Reactome; R-CEL-6798695; Neutrophil degranulation.
Reactome; R-CEL-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-CEL-8875555; MET activates RAP1 and RAC1.
Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; Q03206; -.
PRO; PR:Q03206; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00000424; -.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IDA:WormBase.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0048846; P:axon extension involved in axon guidance; IGI:WormBase.
GO; GO:0031103; P:axon regeneration; IMP:WormBase.
GO; GO:0010171; P:body morphogenesis; IGI:WormBase.
GO; GO:0016477; P:cell migration; IMP:WormBase.
GO; GO:0097628; P:distal tip cell migration; IMP:WormBase.
GO; GO:0033563; P:dorsal/ventral axon guidance; IGI:WormBase.
GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
GO; GO:0043652; P:engulfment of apoptotic cell; IMP:WormBase.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
GO; GO:0007369; P:gastrulation; IMP:WormBase.
GO; GO:0070986; P:left/right axis specification; IMP:UniProtKB.
GO; GO:0008045; P:motor neuron axon guidance; IGI:UniProtKB.
GO; GO:0002119; P:nematode larval development; IGI:WormBase.
GO; GO:0045138; P:nematode male tail tip morphogenesis; IGI:WormBase.
GO; GO:0001764; P:neuron migration; IGI:WormBase.
GO; GO:0048812; P:neuron projection morphogenesis; IGI:WormBase.
GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Cell membrane; Complete proteome;
Developmental protein; GTP-binding; Lipoprotein; Membrane;
Methylation; Neurogenesis; Nucleotide-binding; Phagocytosis;
Prenylation; Reference proteome.
CHAIN 1 188 Ras-related protein ced-10.
/FTId=PRO_0000198891.
PROPEP 189 191 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281242.
NP_BIND 10 17 GTP. {ECO:0000250}.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 115 118 GTP. {ECO:0000250}.
MOTIF 32 40 Effector region. {ECO:0000255}.
MOD_RES 188 188 Cysteine methyl ester. {ECO:0000250}.
LIPID 188 188 S-geranylgeranyl cysteine. {ECO:0000250}.
VAR_SEQ 69 130 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_005711.
MUTAGEN 12 12 G->V: May be constitutively active.
Formation of ectopic processes often
branched in PDE neurons.
{ECO:0000269|PubMed:18499456}.
MUTAGEN 60 60 G->R: In n3246; in HSN neurons, severe
reduction in mig-10 ventral enrichment
and mild defect in axonal guidance but
normal final migration to the ventral
nerve cord.
{ECO:0000269|PubMed:18499456}.
MUTAGEN 61 61 Q->L: May lock enzyme in its GTP-bound
active state. Defect in distal tip cell
(DTC) migration.
{ECO:0000269|PubMed:19797046}.
CONFLICT 177 177 L -> V (in Ref. 1; AAA28140/AAA28141/
CAA48506). {ECO:0000305}.
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


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