RAC2_CAEEL
ID RAC2_CAEEL Reviewed; 195 AA.
AC Q94124; O45648; Q95QD0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ras-related protein rac-2;
DE Flags: Precursor;
GN Name=rac-2; ORFNames=K03D3.10;
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 [GENOMIC DNA].
RX PubMed=8973370; DOI=10.1016/s0378-1119(96)00414-3;
RA Chen W., Yap S.F., Lim L.;
RT "Isolation of the gene coding for Caenorhabditis elegans Rac2 homologue, a
RT Ras-related small GTP-binding protein.";
RL Gene 180:217-219(1996).
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, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: During gonad morphogenesis, plays a role in distal tip cell
CC (DTC)-mediated guidance of gonad elongation (PubMed:19023419).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes distal tip cells
CC (DTC) to make extra turns in approximately 20 percent of animals during
CC the last phase of gonad morphogenesis. {ECO:0000269|PubMed:19023419}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; U55018; AAB40386.1; -; Genomic_DNA.
DR EMBL; Z82276; CAB05247.2; -; Genomic_DNA.
DR PIR; JC5328; JC5328.
DR PIR; T23283; T23283.
DR RefSeq; NP_001040961.1; NM_001047496.1.
DR AlphaFoldDB; Q94124; -.
DR SMR; Q94124; -.
DR BioGRID; 51651; 16.
DR STRING; 6239.K03D3.10; -.
DR PaxDb; Q94124; -.
DR PeptideAtlas; Q94124; -.
DR EnsemblMetazoa; K03D3.10.1; K03D3.10.1; WBGene00004287.
DR GeneID; 186939; -.
DR KEGG; cel:CELE_K03D3.10; -.
DR UCSC; K03D3.10; c. elegans.
DR CTD; 186939; -.
DR WormBase; K03D3.10; CE25698; WBGene00004287; rac-2.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000153500; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q94124; -.
DR OMA; AAMYIEC; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q94124; -.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR Reactome; R-CEL-9706019; RHOBTB3 ATPase cycle.
DR PRO; PR:Q94124; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004287; Expressed in embryo.
DR GO; GO:0030424; C:axon; IDA:WormBase.
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:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005525; F:GTP binding; IDA:WormBase.
DR GO; GO:0003924; F:GTPase activity; IDA:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IGI:UniProtKB.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IGI:WormBase.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IGI:WormBase.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:WormBase.
DR GO; GO:0001764; P:neuron migration; IGI:WormBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IGI:WormBase.
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 3: Inferred from homology;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..192
FT /note="Ras-related protein rac-2"
FT /id="PRO_0000198892"
FT PROPEP 193..195
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281243"
FT REGION 176..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 177..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 192
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 192
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 195 AA; 21915 MW; C7F82946A4D8E7DF CRC64;
MQAIKCVVVG DGAVGKTCLL LSYTTNAFPG EYILTVFDTY STNVMVDGRP INLSLWDTAG
QDDYDQFRHL SFPQTDVFLV CFALNNPASF ENVRAKWYPE VSHHCPNTPI ILVGTKADLR
EDRDTIERLR ERRLQPVSHT QGYVMAKEIK AVKYLECSAL TQIGLKQVFD EAIRTGLTPP
QTPQTRAKKS NCTVL
