RRC1_CAEEL
ID RRC1_CAEEL Reviewed; 759 AA.
AC Q20498; Q5WRQ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=GTPase-activating protein rrc-1;
DE AltName: Full=RhoGAP for Rac-1 and Cdc-42;
GN Name=rrc-1; ORFNames=F47A4.3;
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], AND ALTERNATIVE SPLICING
RP (ISOFORMS A AND B).
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, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=17434147; DOI=10.1016/j.bbrc.2007.03.192;
RA Delawary M., Nakazawa T., Tezuka T., Sawa M., Iino Y., Takenawa T.,
RA Yamamoto T.;
RT "Molecular characterization of a novel RhoGAP, RRC-1 of the nematode
RT Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 357:377-382(2007).
CC -!- FUNCTION: Functions as a GTPase-activating protein (GAP) for ced-
CC 10/rac-1 and CDC42. {ECO:0000269|PubMed:17434147}.
CC -!- INTERACTION:
CC Q20498; O17099: CELE_F42G2.5; NbExp=5; IntAct=EBI-2316401, EBI-2316398;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q20498-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q20498-2; Sequence=VSP_031596;
CC -!- TISSUE SPECIFICITY: Expressed in coelomocytes, excretory cells,
CC uterine-seam cells and GLR cells. {ECO:0000269|PubMed:17434147}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all life stages with high expression
CC in L1-L4 larvae stages. {ECO:0000269|PubMed:17434147}.
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DR EMBL; Z49888; CAA90063.2; -; Genomic_DNA.
DR EMBL; Z49888; CAH60776.1; -; Genomic_DNA.
DR PIR; T22329; T22329.
DR RefSeq; NP_001024683.1; NM_001029512.2. [Q20498-1]
DR RefSeq; NP_001024684.1; NM_001029513.2. [Q20498-2]
DR AlphaFoldDB; Q20498; -.
DR SMR; Q20498; -.
DR BioGRID; 46110; 31.
DR IntAct; Q20498; 31.
DR STRING; 6239.F47A4.3a; -.
DR EPD; Q20498; -.
DR PaxDb; Q20498; -.
DR PRIDE; Q20498; -.
DR EnsemblMetazoa; F47A4.3a.1; F47A4.3a.1; WBGene00009800. [Q20498-1]
DR EnsemblMetazoa; F47A4.3b.1; F47A4.3b.1; WBGene00009800. [Q20498-2]
DR GeneID; 181195; -.
DR UCSC; F47A4.3a; c. elegans. [Q20498-1]
DR CTD; 181195; -.
DR WormBase; F47A4.3a; CE34188; WBGene00009800; rrc-1. [Q20498-1]
DR WormBase; F47A4.3b; CE37375; WBGene00009800; rrc-1. [Q20498-2]
DR eggNOG; KOG1449; Eukaryota.
DR GeneTree; ENSGT00940000168991; -.
DR InParanoid; Q20498; -.
DR OMA; ARRYMTT; -.
DR OrthoDB; 279430at2759; -.
DR PhylomeDB; Q20498; -.
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-9013148; CDC42 GTPase cycle.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR Reactome; R-CEL-9013420; RHOU GTPase cycle.
DR Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR PRO; PR:Q20498; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00009800; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q20498; baseline and differential.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Reference proteome; SH3 domain.
FT CHAIN 1..759
FT /note="GTPase-activating protein rrc-1"
FT /id="PRO_0000320116"
FT DOMAIN 164..243
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 280..473
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 591..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..24
FT /note="MEGIEESFAPLSPKSPFARRNGRS -> MDPEIPG (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_031596"
SQ SEQUENCE 759 AA; 87020 MW; 45A9592D40D9D7F1 CRC64;
MEGIEESFAP LSPKSPFARR NGRSLRIQRL VDCQHFHYSS VELGPVRVAI IAINADENAT
ERIKMRVESE SNSWLVERSR EDWAVFDRQL HRCVFERRHS RLDELFPLIH LETAKFEEVL
VKYTERLSEL TGSIITCYPV LKFLEIDSRG GHFEPAEETS INVPAIAAAV VTKDFEPTES
SQLRLRVGDI VSITEMSTAS PSEQTFWKAK LTISNQKIVD PQNARLGFEI GYFPRDCVML
IDDKRLPNPL NNEQKASTRN ARRYMTTMFR NRRREPIFGL ELTDLYMRTG KKVPVIVEKC
CASIEDQGIV TGIYRQCGIQ SNIQRLRAKF DSGAEPDLHE FGQRDIYSVS SLLKQYFRQL
PNPLFTYQAY PKLIEAFEKE DSLSEKVESL RFSLETMPEA HYRTAKFLME HLTRLCKSKS
LTDMTSKNLA IVWSPNLFRP PPTLNGADTH LLSGLNVHTA ICDFFIENSE SLFVNDIDEE
QSKCTSVENS FTTISKSATM SDMRSESESK WPRFFRGKSV EGFWKFNRKQ QTSTGELCGS
PTSEVKWRSR STRSHSTDAA FQSSRTDSFI QLMHTGMDQI REGMRIFRAR ARSMRPTSRP
PPSPRTRRAR FSNGSSNNVQ KLNESDIQHE IPLATTEPSI TPEPKNTVDP HQIMTRTISV
NDSDDQSFEE NGLREMRERK VMFKAATQEH VATFHERSSP VEEWSSDSRE SLHLEMSRYD
NVSPSGTITR NQREPITNLS PAAQMLFFES SRASHLFSA
