GPA16_CAEEL
ID GPA16_CAEEL Reviewed; 357 AA.
AC Q9N2V6;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Guanine nucleotide-binding protein alpha-16 subunit;
GN Name=gpa-16; Synonyms=spn-1; ORFNames=Y95B8A.5;
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;
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 [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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=10192394; DOI=10.1038/7753;
RA Jansen G., Thijssen K.L., Werner P., van der Horst M., Hazendonk E.,
RA Plasterk R.H.A.;
RT "The complete family of genes encoding G proteins of Caenorhabditis
RT elegans.";
RL Nat. Genet. 21:414-419(1999).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-202.
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).
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 goa-1, controls
CC nuclear rotation and spindle elongation during mitosis
CC (PubMed:14534135). During the first embryonic cell divisons, plays a
CC role in gpr-1/2 cortical localization and in the proper orientation of
CC EMS blastomere mitotic spindle (PubMed:14534135).
CC {ECO:0000269|PubMed:14534135, ECO:0000305}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- INTERACTION:
CC Q9N2V6; Q95QJ7: gpr-1; NbExp=2; IntAct=EBI-1005005, EBI-316069;
CC Q9N2V6; Q9GSX9-1: ric-8; NbExp=2; IntAct=EBI-1005005, EBI-1004494;
CC -!- DISRUPTION PHENOTYPE: Simultaneous RNAi-mediated knockdown of both gpa-
CC 16 and goa-1 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. At the
CC 2-cell stage embryo, nuclei are mispositioned and fail to exhibit
CC nuclear rotation. In addition, causes a loss of gpr-1/2 cortical
CC localization in 2-cell and 4-cell stage embryos.
CC {ECO:0000269|PubMed:14534135}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AY008138; AAG32091.1; -; mRNA.
DR EMBL; FO081787; CCD73543.1; -; Genomic_DNA.
DR RefSeq; NP_490790.1; NM_058389.3.
DR AlphaFoldDB; Q9N2V6; -.
DR SMR; Q9N2V6; -.
DR BioGRID; 37175; 5.
DR IntAct; Q9N2V6; 2.
DR STRING; 6239.Y95B8A.5; -.
DR EPD; Q9N2V6; -.
DR PaxDb; Q9N2V6; -.
DR PeptideAtlas; Q9N2V6; -.
DR PRIDE; Q9N2V6; -.
DR EnsemblMetazoa; Y95B8A.5a.1; Y95B8A.5a.1; WBGene00001678.
DR GeneID; 171675; -.
DR KEGG; cel:CELE_Y95B8A.5; -.
DR UCSC; Y95B8A.5; c. elegans.
DR CTD; 171675; -.
DR WormBase; Y95B8A.5a; CE24692; WBGene00001678; gpa-16.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q9N2V6; -.
DR OMA; MRIIHDV; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q9N2V6; -.
DR Reactome; R-CEL-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-CEL-2485179; Activation of the phototransduction cascade.
DR Reactome; R-CEL-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-CEL-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-CEL-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-CEL-4086398; Ca2+ pathway.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR Reactome; R-CEL-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR PRO; PR:Q9N2V6; -.
DR Proteomes; UP000001940; Chromosome I.
DR ExpressionAtlas; Q9N2V6; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISS:WormBase.
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:0019003; F:GDP binding; ISS:WormBase.
DR GO; GO:0005525; F:GTP binding; ISS:WormBase.
DR GO; GO:0003924; F:GTPase activity; ISS:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000578; P:embryonic axis specification; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:WormBase.
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; GTP-binding; Lipoprotein; Magnesium;
KW Metal-binding; Mitosis; Myristate; Nucleotide-binding; Palmitate;
KW Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..357
FT /note="Guanine nucleotide-binding protein alpha-16 subunit"
FT /id="PRO_0000203657"
FT DOMAIN 32..357
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 173..181
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 196..205
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 265..272
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 327..332
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 175..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 200..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 329
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 202
FT /note="G->D: In it143ts; temperature sensitive mutant. 70
FT percent of embryonic lethality. In 31 percent of EMS
FT blastomeres, loss of nuclear rotation resulting in the
FT transversal localization of the mitotic spindle."
FT /evidence="ECO:0000269|PubMed:14534135"
SQ SEQUENCE 357 AA; 41328 MW; C0CDB733D06EE6C9 CRC64;
MGCIMSQEDE AAKRRSKKID RLLKEDGENS MRTIKLLLLG AGESGKSTIL KQMRIIHDVG
YTTEERKVFR GVVYGNIILS LNAIIHAMEQ LKISFTTLDH ESDARKLLMF STTGEEDELP
EELVVLMKSV WSDSGIQKAL ERSREYQLND SAGYYLSQLD RICAPNYIPT QDDILRTRIK
TTGIVETQFV YKDRLFLVFD VGGQRSERKK WIHCFEDVTA LIFCVALSEY DMVLVEDCQT
NRMRESLKLF DSICNNKWFV ETSIILFLNK KDLFEEKIVR SPLTHCFPEY TGANNYEEAS
AYIQQQFEDM NKRTTGEKNQ EIYTQFTCAT DTNNIRFVFD AVTDIIIRDN LRTCGLY
