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Protein

Guanine nucleotide-binding protein G(o) subunit alpha

Gene

goa-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. In the 1-cell embryo, probably together with gpa-16, controls nuclear rotation and spindle elongation during mitosis (PubMed:14534135). During the first embryonic cell divisons, plays a role in gpr-1/2 cortical localization and in the proper orientation of EMS blastomere mitotic spindle (PubMed:14534135). Polarity determinants (par genes) may regulate lin-5/gpr-1/gpr-2/goa-1 locally to create the asymmetric forces that drive spindle movement (PubMed:12730122). Involved in chemosensory responses to attractive and repellent odors detected by AWC and AWB sensory neurons, respectively (PubMed:23954825). Negatively regulates axon regeneration after injury donwstream of the inhibitory compound arachidonoyl ethanolamide (AEA) by antagonozing the activation of the JNK pathway (mlk-1/mek-1/kgb-1) (PubMed:23072806). Involved in egg-laying and locomotion (PubMed:8548815).5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471MagnesiumBy similarity
Metal bindingi182 – 1821MagnesiumBy similarity
Binding sitei326 – 3261GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 478GTPBy similarity
Nucleotide bindingi176 – 1827GTPBy similarity
Nucleotide bindingi201 – 2055GTPBy similarity
Nucleotide bindingi270 – 2734GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: WormBase
  • GTP binding Source: WormBase
  • metal ion binding Source: UniProtKB-KW
  • protein kinase binding Source: WormBase
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: InterPro
  • cell division Source: UniProtKB-KW
  • chemotaxis Source: UniProtKB-KW
  • defense response to Gram-negative bacterium Source: UniProtKB
  • dopamine receptor signaling pathway Source: WormBase
  • G-protein coupled receptor signaling pathway Source: WormBase
  • mitotic nuclear division Source: UniProtKB-KW
  • regulation of feeding behavior Source: WormBase
  • regulation of locomotion Source: WormBase
  • regulation of oviposition Source: WormBase
  • regulation of pharyngeal pumping Source: WormBase
  • response to food Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Cell cycle, Cell division, Chemotaxis, Mitosis

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-CEL-112043. PLC beta mediated events.
R-CEL-202040. G-protein activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(o) subunit alpha
Gene namesi
Name:goa-1
ORF Names:C26C6.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiC26C6.2; CE05311; WBGene00001648; goa-1.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: WormBase
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Prolonged exposure to attractive odorant benzaldehyde results in a loss of adaptive response characterized by a decrease in odor seeking behavior and in a loss of egl-4 nuclear translocation. Loss of chemotaxis response to the repellent odor 2-nonanone (PubMed:23954825). Increased egg laying; eggs are prematurely laid at one-cell to 8-cell stage (PubMed:8548815). Increased locomotion (PubMed:8548815). Simultaneous RNAi-mediated knockdown of both goa-1 and gpa-16 causes, in the one-cell embryo, a lack of nuclear rocking movements from prophase to metaphase and symmetric spindle elongation without transversal oscillations of the poles during anaphase. At the 2-cell stage embryo, nuclei are mispositioned and fail to exhibit nuclear rotation. In addition, causes a loss of gpr-1/2 cortical localization in 2-cell and 4-cell stage embryos (PubMed:14534135).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi205 – 2051Q → L: Probably constitutively active. Inhibition of axon regeneration. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 354353Guanine nucleotide-binding protein G(o) subunit alphaPRO_0000203710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence analysis
Lipidationi3 – 31S-palmitoyl cysteineSequence analysis

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

EPDiP51875.
PaxDbiP51875.
PRIDEiP51875.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (By similarity). Interacts (in GDP-bound form) with gpr-1; gpr-1 forms a complex with gpr-2 and lin-5. Interacts (in GDP-bound form) with gpb-1 (PubMed:12730122).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q86RS94EBI-316062,EBI-6094513
ags-3Q199557EBI-316062,EBI-2913838
gbas-1Q9TZI43EBI-316062,EBI-6094450
lin-36P344273EBI-316062,EBI-322214
ric-8Q9GSX9-19EBI-316062,EBI-1004494

GO - Molecular functioni

  • protein kinase binding Source: WormBase

Protein-protein interaction databases

BioGridi37947. 8 interactions.
DIPiDIP-25342N.
IntActiP51875. 12 interactions.
MINTiMINT-1063958.
STRINGi6239.C26C6.2.2.

Structurei

3D structure databases

ProteinModelPortaliP51875.
SMRiP51875. Positions 35-345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-alpha family. G(i/o/t/z) subfamily.Curated

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
InParanoidiP51875.
KOiK04534.
OMAiEDFKQYK.
PhylomeDBiP51875.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51875-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCTMSQEER AALERSRMIE KNLKEDGMQA AKDIKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHESG FTAEDYKQYK PVVYSNTVQS LVAILRAMSN LGVSFGSADR
110 120 130 140 150
EVDAKLVMDV VARMEDTEPF SEELLSSMKR LWGDAGVQDC FSRSNEYQLN
160 170 180 190 200
DSAKYFLDDL ERLGEAIYQP TEQDILRTRV KTTGIVEVHF TFKNLNFKLF
210 220 230 240 250
DVGGQRSERK KWIHCFEDVT AIIFCVAMSE YDQVLHEDET TNRMHESLKL
260 270 280 290 300
FDSICNNKWF TDTSIILFLN KKDLFEEKIK KSPLTICFPE YSGRQDYHEA
310 320 330 340 350
SAYIQAQFEA KNKSANKEIY CHMTCATDTT NIQFVFDAVT DVIIANNLRG

CGLY
Length:354
Mass (Da):40,451
Last modified:January 23, 2007 - v3
Checksum:i8C98245C8E9C48B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741D → H in AAA28059 (PubMed:1907494).Curated
Sequence conflicti234 – 2341V → L in AAA28059 (PubMed:1907494).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38251 mRNA. Translation: AAA28059.1.
AY008140 mRNA. Translation: AAG32093.1.
Z72503 Genomic DNA. Translation: CAA96595.1.
PIRiT19476.
RefSeqiNP_492108.1. NM_059707.5.
UniGeneiCel.17339.

Genome annotation databases

EnsemblMetazoaiC26C6.2; C26C6.2; WBGene00001648.
GeneIDi172505.
KEGGicel:CELE_C26C6.2.
UCSCiC26C6.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38251 mRNA. Translation: AAA28059.1.
AY008140 mRNA. Translation: AAG32093.1.
Z72503 Genomic DNA. Translation: CAA96595.1.
PIRiT19476.
RefSeqiNP_492108.1. NM_059707.5.
UniGeneiCel.17339.

3D structure databases

ProteinModelPortaliP51875.
SMRiP51875. Positions 35-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi37947. 8 interactions.
DIPiDIP-25342N.
IntActiP51875. 12 interactions.
MINTiMINT-1063958.
STRINGi6239.C26C6.2.2.

Proteomic databases

EPDiP51875.
PaxDbiP51875.
PRIDEiP51875.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC26C6.2; C26C6.2; WBGene00001648.
GeneIDi172505.
KEGGicel:CELE_C26C6.2.
UCSCiC26C6.2. c. elegans.

Organism-specific databases

CTDi172505.
WormBaseiC26C6.2; CE05311; WBGene00001648; goa-1.

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
InParanoidiP51875.
KOiK04534.
OMAiEDFKQYK.
PhylomeDBiP51875.

Enzyme and pathway databases

ReactomeiR-CEL-112043. PLC beta mediated events.
R-CEL-202040. G-protein activation.

Miscellaneous databases

PROiP51875.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Homologous and unique G protein alpha subunits in the nematode Caenorhabditis elegans."
    Lochrie M.A., Mendel J.E., Sternberg P.W., Simon M.I.
    Cell Regul. 2:135-154(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Bristol N2.
  2. "Interaction analysis of the complete G-alpha subfamily of heterotrimeric G proteins from Caenorhabditis elegans."
    Cuppen E., Jansen G., Plasterk R.H.A.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Bristol N2.
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  4. "EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins."
    Koelle M.R., Horvitz H.R.
    Cell 84:115-125(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: Bristol N2.
  5. "LET-99 opposes Galpha/GPR signaling to generate asymmetry for spindle positioning in response to PAR and MES-1/SRC-1 signaling."
    Tsou M.-F.B., Hayashi A., Rose L.S.
    Development 130:5717-5730(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "A complex of LIN-5 and GPR proteins regulates G protein signaling and spindle function in C elegans."
    Srinivasan D.G., Fisk R.M., Xu H., van den Heuvel S.
    Genes Dev. 17:1225-1239(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GPR-1 AND GPB-1.
  7. "Endocannabinoid-Goalpha signalling inhibits axon regeneration in Caenorhabditis elegans by antagonizing Gqalpha-PKC-JNK signalling."
    Pastuhov S.I., Fujiki K., Nix P., Kanao S., Bastiani M., Matsumoto K., Hisamoto N.
    Nat. Commun. 3:1136-1136(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLN-205.
  8. "Nuclear PKG localization is regulated by G(0) alpha and is necessary in the AWB neurons to mediate avoidance in Caenorhabditis elegans."
    He C., O'Halloran D.M.
    Neurosci. Lett. 553:35-39(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiGNAO_CAEEL
AccessioniPrimary (citable) accession number: P51875
Secondary accession number(s): Q18205
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.