EGL10_CAEEL
ID EGL10_CAEEL Reviewed; 555 AA.
AC P49809; Q19855;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Regulator of G-protein signaling egl-10;
DE AltName: Full=Egg-laying defective protein 10;
GN Name=egl-10 {ECO:0000312|WormBase:F28C1.2a};
GN ORFNames=F28C1.2 {ECO:0000312|WormBase:F28C1.2a};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=8548815; DOI=10.1016/s0092-8674(00)80998-8;
RA Koelle M.R., Horvitz H.R.;
RT "EGL-10 regulates G protein signaling in the C. elegans nervous system and
RT shares a conserved domain with many mammalian proteins.";
RL Cell 84:115-125(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 INTERACTION WITH GPB-1 AND GPB-2.
RC STRAIN=Bristol N2;
RX PubMed=11333232; DOI=10.1093/genetics/158.1.221;
RA van Der Linden A.M., Simmer F., Cuppen E., Plasterk R.H.A.;
RT "The G protein beta subunit gpb-2 in Caenorhabditis elegans regulates the
RT G(o)alpha-G(q)alpha signaling network through interactions with the
RT regulator of G protein signaling proteins egl-10 and eat-16.";
RL Genetics 158:221-235(2001).
RN [4]
RP FUNCTION.
RX PubMed=15378064; DOI=10.1038/nn1316;
RA Chase D.L., Pepper J.S., Koelle M.R.;
RT "Mechanism of extrasynaptic dopamine signaling in Caenorhabditis elegans.";
RL Nat. Neurosci. 7:1096-1103(2004).
CC -!- FUNCTION: Involved in egg-laying and locomotion. May regulate G protein
CC goa-1 signaling. Plays a role in regulating dopamine-mediated
CC locomotion behavior (PubMed:15378064). {ECO:0000269|PubMed:15378064,
CC ECO:0000269|PubMed:8548815}.
CC -!- SUBUNIT: Interacts with gpb-1 and gpb-2. {ECO:0000269|PubMed:11333232}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000269|PubMed:8548815}.
CC -!- TISSUE SPECIFICITY: Expressed in nerve ring and ventral nerve cord.
CC {ECO:0000269|PubMed:11333232}.
CC -!- DISRUPTION PHENOTYPE: Impaired egg laying; the few laid eggs are at the
CC post comma stage. Impaired locomotion. {ECO:0000269|PubMed:8548815}.
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DR EMBL; U32326; AAC46965.1; -; mRNA.
DR EMBL; BX284605; CAA99844.2; -; Genomic_DNA.
DR PIR; T21468; T21468.
DR RefSeq; NP_001256420.1; NM_001269491.1.
DR AlphaFoldDB; P49809; -.
DR SMR; P49809; -.
DR BioGRID; 44728; 2.
DR STRING; 6239.F28C1.2b; -.
DR iPTMnet; P49809; -.
DR EPD; P49809; -.
DR PaxDb; P49809; -.
DR EnsemblMetazoa; F28C1.2a.1; F28C1.2a.1; WBGene00001179.
DR GeneID; 179707; -.
DR UCSC; F28C1.2; c. elegans.
DR CTD; 179707; -.
DR WormBase; F28C1.2a; CE24928; WBGene00001179; egl-10.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000170966; -.
DR HOGENOM; CLU_025092_4_1_1; -.
DR InParanoid; P49809; -.
DR PhylomeDB; P49809; -.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR Reactome; R-CEL-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR PRO; PR:P49809; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001179; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; P49809; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:WormBase.
DR GO; GO:0007631; P:feeding behavior; IMP:WormBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IGI:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0007622; P:rhythmic behavior; IMP:WormBase.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR034483; Egl-10.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR040759; RGS_DHEX.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45746:SF6; PTHR45746:SF6; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00631; G-gamma; 1.
DR Pfam; PF00615; RGS; 1.
DR Pfam; PF18148; RGS_DHEX; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00224; GGL; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Cell projection; Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..555
FT /note="Regulator of G-protein signaling egl-10"
FT /id="PRO_0000204236"
FT DOMAIN 37..112
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 330..395
FT /note="G protein gamma"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00592"
FT DOMAIN 421..537
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 253..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 63278 MW; 2CDBA33A82876BBE CRC64;
MALPRLRVNA SNEERLVHPN HMVYRKMEML VNQMLDAEAG VPIKTVKSFL SKVPSVFTGQ
DLIGWIMKNL EMTDLSDALH LAHLIASHGY LFQIDDHVLT VKNDGTFYRF QTPYFWPSNC
WDPENTDYAV YLCKRTMQNK AHLELEDFEA ENLAKLQKMF SRKWEFVFMQ AEAQYKVDKK
RDRQERQILD SQERAFWDVH RPVPGCVNTT EVDFRKLSRS GRPKYSSGGH AALAASTSGI
GCTQYSQSVA AAHASLPSTS NGSATSPRKN DQEPSTSSGG ESPSTSSAAA GTATTSAPST
STPPVTTITA TINAGSFRNN YYTRPGLRRC TQVQDTLKLE IVQLNSRLSK NVLRTSKVVE
NYLAYYEQRR VFDPLLTPPG SQADPFQSQP NPWINDTVDF WQHDKITGDI QTRRLKLWED
SFEELLADSL GRETLQKFLD KEYSGENLRF WWEVQKLRKC SSRMVPVMVT EIYNEFIDTN
AATSPVNVDC KVMEVTEDNL KNPNRWSFDE AADHIYCLMK NDSYQRFLRS EIYKDLVLQS
RKKVSLNCSF SIFAS
