RAP1_CAEEL
ID RAP1_CAEEL Reviewed; 188 AA.
AC Q18246;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ras-related protein Rap-1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61224};
GN Name=rap-1; ORFNames=C27B7.8;
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 [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 [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15525675; DOI=10.1091/mbc.e04-06-0492;
RA Berkel W.P., Verheijen M.H., Cuppen E., Asahina M., de Rooij J., Jansen G.,
RA Plasterk R.H., Bos J.L., Zwartkruis F.J.;
RT "Requirement of the Caenorhabditis elegans RapGEF pxf-1 and rap-1 for
RT epithelial integrity.";
RL Mol. Biol. Cell 16:106-116(2005).
CC -!- FUNCTION: Required in the hypodermis for proper formation of the
CC cuticle. {ECO:0000269|PubMed:15525675}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P61224};
CC -!- DISRUPTION PHENOTYPE: Worms are viable and fertile but display molting
CC defect. Longitudinal ridges termed alae, which are cuticular structures
CC secreted by lateral hypodermal seam cells, are poorly distinct or
CC interrupted. Died as a 'bag of worms' after degeneration of the
CC proximal gonad, or alternatively, as a result of a burst vulva.
CC {ECO:0000269|PubMed:15525675}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; Z54236; CAA90983.1; -; Genomic_DNA.
DR PIR; T19507; T19507.
DR RefSeq; NP_501549.1; NM_069148.4.
DR AlphaFoldDB; Q18246; -.
DR SMR; Q18246; -.
DR BioGRID; 42817; 4.
DR IntAct; Q18246; 1.
DR STRING; 6239.C27B7.8; -.
DR EPD; Q18246; -.
DR PaxDb; Q18246; -.
DR PeptideAtlas; Q18246; -.
DR EnsemblMetazoa; C27B7.8.1; C27B7.8.1; WBGene00004307.
DR GeneID; 177709; -.
DR KEGG; cel:CELE_C27B7.8; -.
DR UCSC; C27B7.8; c. elegans.
DR CTD; 177709; -.
DR WormBase; C27B7.8; CE03037; WBGene00004307; rap-1.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000164058; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q18246; -.
DR OMA; CYRKQWV; -.
DR OrthoDB; 1353024at2759; -.
DR PhylomeDB; Q18246; -.
DR Reactome; R-CEL-170968; Frs2-mediated activation.
DR Reactome; R-CEL-170984; ARMS-mediated activation.
DR Reactome; R-CEL-354192; Integrin signaling.
DR Reactome; R-CEL-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-CEL-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-CEL-392517; Rap1 signalling.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8875555; MET activates RAP1 and RAC1.
DR PRO; PR:Q18246; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004307; Expressed in embryo and 4 other tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISS:WormBase.
DR GO; GO:0071320; P:cellular response to cAMP; IBA:GO_Central.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0008544; P:epidermis development; IMP:WormBase.
DR GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IBA:GO_Central.
DR GO; GO:0032486; P:Rap protein signal transduction; IBA:GO_Central.
DR CDD; cd04175; Rap1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038851; Rap1.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..188
FT /note="Ras-related protein Rap-1"
FT /id="PRO_0000423877"
FT MOTIF 32..40
FT /note="Effector region"
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 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 188 AA; 21248 MW; 45227D8B94C40629 CRC64;
MREYKIVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDGQQ CMLEILDTAG
TEQFTAMRDL YMKNGQGFVL VYSITAQSTF NDLMDLRDQI LRVKDTDEVP MILVGNKCDL
EDERVVGKDQ GQNLARQFGS AFLETSAKAK INVSEVFYDL VRQINRRYPE SGRRQGQSNK
QCCSCVIM
