GNAO_CAEEL
ID GNAO_CAEEL Reviewed; 354 AA.
AC P51875; Q18205;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Guanine nucleotide-binding protein G(o) subunit alpha;
GN Name=goa-1 {ECO:0000312|WormBase:C26C6.2};
GN ORFNames=C26C6.2 {ECO:0000312|WormBase:C26C6.2};
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].
RC STRAIN=Bristol N2;
RX PubMed=1907494; DOI=10.1091/mbc.2.2.135;
RA Lochrie M.A., Mendel J.E., Sternberg P.W., Simon M.I.;
RT "Homologous and unique G protein alpha subunits in the nematode
RT Caenorhabditis elegans.";
RL Cell Regul. 2:135-154(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RA Cuppen E., Jansen G., Plasterk R.H.A.;
RT "Interaction analysis of the complete G-alpha subfamily of heterotrimeric G
RT proteins from Caenorhabditis elegans.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, 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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14534135; DOI=10.1242/dev.00790;
RA Tsou M.-F.B., Hayashi A., Rose L.S.;
RT "LET-99 opposes Galpha/GPR signaling to generate asymmetry for spindle
RT positioning in response to PAR and MES-1/SRC-1 signaling.";
RL Development 130:5717-5730(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH GPR-1 AND GPB-1.
RX PubMed=12730122; DOI=10.1101/gad.1081203;
RA Srinivasan D.G., Fisk R.M., Xu H., van den Heuvel S.;
RT "A complex of LIN-5 and GPR proteins regulates G protein signaling and
RT spindle function in C elegans.";
RL Genes Dev. 17:1225-1239(2003).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF 52-GLN--TYR-354.
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).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18614679; DOI=10.1523/jneurosci.0378-08.2008;
RA Dittman J.S., Kaplan J.M.;
RT "Behavioral impact of neurotransmitter-activated G-protein-coupled
RT receptors: muscarinic and GABAB receptors regulate Caenorhabditis elegans
RT locomotion.";
RL J. Neurosci. 28:7104-7112(2008).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF 52-GLN--TYR-354.
RX PubMed=19609300; DOI=10.1038/emboj.2009.194;
RA Suo S., Culotti J.G., Van Tol H.H.;
RT "Dopamine counteracts octopamine signalling in a neural circuit mediating
RT food response in C. elegans.";
RL EMBO J. 28:2437-2448(2009).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22897658; DOI=10.1111/j.1365-2443.2012.01627.x;
RA Tada M., Gengyo-Ando K., Kobayashi T., Fukuyama M., Mitani S., Kontani K.,
RA Katada T.;
RT "Neuronally expressed Ras-family GTPase Di-Ras modulates synaptic activity
RT in Caenorhabditis elegans.";
RL Genes Cells 17:778-789(2012).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF GLN-205.
RX PubMed=23072806; DOI=10.1038/ncomms2136;
RA Pastuhov S.I., Fujiki K., Nix P., Kanao S., Bastiani M., Matsumoto K.,
RA Hisamoto N.;
RT "Endocannabinoid-Goalpha signalling inhibits axon regeneration in
RT Caenorhabditis elegans by antagonizing Gqalpha-PKC-JNK signalling.";
RL Nat. Commun. 3:1136-1136(2012).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23954825; DOI=10.1016/j.neulet.2013.08.011;
RA He C., O'Halloran D.M.;
RT "Nuclear PKG localization is regulated by G(0) alpha and is necessary in
RT the AWB neurons to mediate avoidance in Caenorhabditis elegans.";
RL Neurosci. Lett. 553:35-39(2013).
RN [13]
RP INTERACTION WITH GBAS-1, AND MUTAGENESIS OF TRP-212 AND PHE-216.
RX PubMed=26659249; DOI=10.1093/molbev/msv336;
RA Coleman B.D., Marivin A., Parag-Sharma K., DiGiacomo V., Kim S.,
RA Pepper J.S., Casler J., Nguyen L.T., Koelle M.R., Garcia-Marcos M.;
RT "Evolutionary conservation of a GPCR-independent mechanism of trimeric G
RT protein activation.";
RL Mol. Biol. Evol. 33:820-837(2016).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF 52-GLN--TYR-354.
RX PubMed=28662030; DOI=10.1371/journal.pbio.2002047;
RA Hoang H.D., Miller M.A.;
RT "Chemosensory and hyperoxia circuits in C. elegans males influence sperm
RT navigational capacity.";
RL PLoS Biol. 15:E2002047-E2002047(2017).
RN [15]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=31474366; DOI=10.1016/j.cell.2019.07.034;
RA Gong J., Liu J., Ronan E.A., He F., Cai W., Fatima M., Zhang W., Lee H.,
RA Li Z., Kim G.H., Pipe K.P., Duan B., Liu J., Xu X.Z.S.;
RT "A Cold-Sensing Receptor Encoded by a Glutamate Receptor Gene.";
RL Cell 178:1375-1386.e11(2019).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. In the 1-cell embryo, probably together with gpa-16, controls
CC nuclear rotation and spindle elongation during mitosis
CC (PubMed:14534135). During the first embryonic cell divisions, plays a
CC role in gpr-1/2 cortical localization and in the proper orientation of
CC EMS blastomere mitotic spindle (PubMed:14534135). Polarity determinants
CC (par genes) may regulate lin-5/gpr-1/gpr-2/goa-1 locally to create the
CC asymmetric forces that drive spindle movement (PubMed:12730122).
CC Involved in chemosensory responses to attractive and repellent odors
CC detected by AWC and AWB sensory neurons, respectively
CC (PubMed:23954825). In ASER neurons, acts downstream of glr-3 to
CC regulate cold avoidance behavior via calcium signaling, and it may also
CC play a role in sensing cold in the intestine (PubMed:31474366).
CC Negatively regulates axon regeneration after injury downstream of the
CC inhibitory compound arachidonoyl ethanolamide (AEA) by antagonizing the
CC activation of the JNK pathway (mlk-1/mek-1/kgb-1) (PubMed:23072806). In
CC neurons, may negatively regulate diacylglycerol (DAG) production
CC mediated by egl-30 signaling cascade and thereby negatively regulates
CC acetylcholine release (PubMed:22897658). Couples to the muscarinic
CC acetylcholine receptor gar-2 to negatively regulate cholinergic
CC receptor activity in the presence of high levels of acetylcholine in
CC ventral cord motor neurons (PubMed:18614679). Plays a role in the
CC navigational capacity of sperm and the targeting of sperm derived from
CC males to the fertilization site in the uterus of hermaphrodites
CC (PubMed:28662030). Involved in egg-laying and in regulating dopamine-
CC mediated locomotion (PubMed:8548815, PubMed:15378064). Most likely
CC couples to the dopamine receptors dop-2 and dop-3 to positively
CC regulate the dopamine-mediated suppression of crh-1/CREB1 transcription
CC factor activation in cholinergic SIA neurons in the presence of food
CC (PubMed:19609300). {ECO:0000269|PubMed:12730122,
CC ECO:0000269|PubMed:14534135, ECO:0000269|PubMed:15378064,
CC ECO:0000269|PubMed:18614679, ECO:0000269|PubMed:19609300,
CC ECO:0000269|PubMed:22897658, ECO:0000269|PubMed:23072806,
CC ECO:0000269|PubMed:23954825, ECO:0000269|PubMed:28662030,
CC ECO:0000269|PubMed:31474366, ECO:0000269|PubMed:8548815}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site (By
CC similarity). Interacts (in GDP-bound form) with gpr-1; gpr-1 forms a
CC complex with gpr-2 and lin-5 (PubMed:12730122). Interacts (in GDP-bound
CC form) with gpb-1 (PubMed:12730122). Interacts (in GDP-bound form) with
CC gbas-1 (via GBA motif); the interaction leads to activation of goa-1
CC (PubMed:26659249). {ECO:0000250|UniProtKB:P63212,
CC ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:26659249}.
CC -!- INTERACTION:
CC P51875; Q19955: ags-3; NbExp=7; IntAct=EBI-316062, EBI-2913838;
CC P51875; Q9TZI4: gbas-1; NbExp=3; IntAct=EBI-316062, EBI-6094450;
CC P51875; P34427: lin-36; NbExp=3; IntAct=EBI-316062, EBI-322214;
CC P51875; Q9GSX9-1: ric-8; NbExp=9; IntAct=EBI-316062, EBI-1004494;
CC P51875; Q86RS9; NbExp=4; IntAct=EBI-316062, EBI-6094513;
CC -!- TISSUE SPECIFICITY: Expressed in the ASER neuron and the intestine.
CC {ECO:0000269|PubMed:31474366}.
CC -!- DISRUPTION PHENOTYPE: Prolonged exposure to attractive odorant
CC benzaldehyde results in a loss of adaptive response characterized by a
CC decrease in odor seeking behavior and in a loss of egl-4 nuclear
CC translocation. Loss of chemotaxis response to the repellent odor 2-
CC nonanone (PubMed:23954825). Increased egg laying; eggs are prematurely
CC laid at one-cell to 8-cell stage (PubMed:8548815). Increased locomotion
CC (PubMed:8548815). Increases diacylglycerol (DAG) levels along axons.
CC Increases paralysis following treatment with acetylcholinesterase
CC inhibitor aldicarb which is partially reduced in a drn-1 mutant
CC background (PubMed:22897658). In a mutant background which expresses
CC gar-2 in all cholinergic motor neurons, eliminates the resistance to
CC Aldicarb that is characteristic of the gar-2 single mutant
CC (PubMed:18614679). Simultaneous RNAi-mediated knockdown of both goa-1
CC and gpa-16 causes, in the one-cell embryo, a lack of nuclear rocking
CC movements from prophase to metaphase and symmetric spindle elongation
CC without transversal oscillations of the poles during anaphase
CC (PubMed:14534135). At the 2-cell stage embryo, nuclei are mispositioned
CC and fail to exhibit nuclear rotation (PubMed:14534135). In addition,
CC causes a loss of gpr-1/2 cortical localization in 2-cell and 4-cell
CC stage embryos (PubMed:14534135). {ECO:0000269|PubMed:14534135,
CC ECO:0000269|PubMed:18614679, ECO:0000269|PubMed:22897658,
CC ECO:0000269|PubMed:23954825, ECO:0000269|PubMed:8548815}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; M38251; AAA28059.1; -; mRNA.
DR EMBL; AY008140; AAG32093.1; -; mRNA.
DR EMBL; BX284601; CAA96595.1; -; Genomic_DNA.
DR PIR; T19476; T19476.
DR RefSeq; NP_492108.1; NM_059707.5.
DR AlphaFoldDB; P51875; -.
DR SMR; P51875; -.
DR BioGRID; 37947; 31.
DR DIP; DIP-25342N; -.
DR IntAct; P51875; 11.
DR STRING; 6239.C26C6.2; -.
DR EPD; P51875; -.
DR PaxDb; P51875; -.
DR PeptideAtlas; P51875; -.
DR EnsemblMetazoa; C26C6.2.1; C26C6.2.1; WBGene00001648.
DR GeneID; 172505; -.
DR KEGG; cel:CELE_C26C6.2; -.
DR UCSC; C26C6.2; c. elegans.
DR CTD; 172505; -.
DR WormBase; C26C6.2; CE05311; WBGene00001648; goa-1.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000155883; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P51875; -.
DR OMA; QVIWADA; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P51875; -.
DR Reactome; R-CEL-4086398; Ca2+ pathway.
DR PRO; PR:P51875; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001648; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003925; F:G protein activity; IDA:WormBase.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IMP:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:WormBase.
DR GO; GO:0003924; F:GTPase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IPI:WormBase.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:UniProtKB.
DR GO; GO:0120169; P:detection of cold stimulus involved in thermoception; IMP:UniProtKB.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:WormBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:WormBase.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:UniProtKB.
DR GO; GO:0032223; P:negative regulation of synaptic transmission, cholinergic; IMP:UniProtKB.
DR GO; GO:0060259; P:regulation of feeding behavior; IMP:WormBase.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IGI:WormBase.
DR GO; GO:0032094; P:response to food; IMP:WormBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001408; Gprotein_alpha_I.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chemotaxis; GTP-binding; Lipoprotein; Magnesium;
KW Metal-binding; Mitosis; Myristate; Nucleotide-binding; Palmitate;
KW Reference proteome; Sensory transduction; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..354
FT /note="Guanine nucleotide-binding protein G(o) subunit
FT alpha"
FT /id="PRO_0000203710"
FT DOMAIN 32..354
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 324..329
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT MUTAGEN 52..354
FT /note="Missing: In sa734; abnormal distribution of male-
FT derived sperm in the hermaphrodite uterus following mating,
FT with sperm accumulating at the spermathecal-uterine valve 1
FT hour following mating. Defective dopamine signaling, with
FT defective locomotion and irregular activation of the crh-
FT 1/CREB1 transcription factor in cholinergic SIA neurons in
FT the presence of food."
FT /evidence="ECO:0000269|PubMed:15378064,
FT ECO:0000269|PubMed:19609300, ECO:0000269|PubMed:28662030"
FT MUTAGEN 205
FT /note="Q->L: Probably constitutively active. Inhibition of
FT axon regeneration."
FT /evidence="ECO:0000269|PubMed:23072806"
FT MUTAGEN 212
FT /note="W->A: Abolishes binding to gbas-1."
FT /evidence="ECO:0000269|PubMed:26659249"
FT MUTAGEN 216
FT /note="F->A: Abolishes binding to gbas-1."
FT /evidence="ECO:0000269|PubMed:26659249"
FT CONFLICT 174
FT /note="D -> H (in Ref. 1; AAA28059)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="V -> L (in Ref. 1; AAA28059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40451 MW; 8C98245C8E9C48B0 CRC64;
MGCTMSQEER AALERSRMIE KNLKEDGMQA AKDIKLLLLG AGESGKSTIV KQMKIIHESG
FTAEDYKQYK PVVYSNTVQS LVAILRAMSN LGVSFGSADR EVDAKLVMDV VARMEDTEPF
SEELLSSMKR LWGDAGVQDC FSRSNEYQLN DSAKYFLDDL ERLGEAIYQP TEQDILRTRV
KTTGIVEVHF TFKNLNFKLF DVGGQRSERK KWIHCFEDVT AIIFCVAMSE YDQVLHEDET
TNRMHESLKL FDSICNNKWF TDTSIILFLN KKDLFEEKIK KSPLTICFPE YSGRQDYHEA
SAYIQAQFEA KNKSANKEIY CHMTCATDTT NIQFVFDAVT DVIIANNLRG CGLY
