GPA8_CAEEL
ID GPA8_CAEEL Reviewed; 364 AA.
AC Q20907;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Guanine nucleotide-binding protein alpha-8 subunit;
GN Name=gpa-8; ORFNames=F56H9.3;
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 [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).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AY008131; AAG32084.1; -; mRNA.
DR EMBL; Z74473; CAA98948.1; -; Genomic_DNA.
DR PIR; T22807; T22807.
DR RefSeq; NP_506160.1; NM_073759.1.
DR AlphaFoldDB; Q20907; -.
DR SMR; Q20907; -.
DR STRING; 6239.F56H9.3; -.
DR PaxDb; Q20907; -.
DR PeptideAtlas; Q20907; -.
DR EnsemblMetazoa; F56H9.3.1; F56H9.3.1; WBGene00001670.
DR GeneID; 179731; -.
DR KEGG; cel:CELE_F56H9.3; -.
DR UCSC; F56H9.3; c. elegans.
DR CTD; 179731; -.
DR WormBase; F56H9.3; CE05973; WBGene00001670; gpa-8.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00970000196357; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q20907; -.
DR OMA; RIREKDY; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q20907; -.
DR PRO; PR:Q20907; -.
DR Proteomes; UP000001940; Chromosome V.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
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; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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 CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..364
FT /note="Guanine nucleotide-binding protein alpha-8 subunit"
FT /id="PRO_0000203643"
FT DOMAIN 38..364
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 41..54
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 184..192
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 207..216
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 276..283
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 334..339
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 186..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 211..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 280..283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 336
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 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 364 AA; 42416 MW; C6B230DB78D9F4EA CRC64;
MGALCSSETY MLDKEEYKKQ VEHNKSIEND LEKDRKIKIL KLLILGPGES GKSTTIKQIK
IIHDEGYSAE EKMVRKHGIY MNILEGIEEI HLSVGRENKS YKNPLSFDHI NEVRMFTENF
KKADDSEKLL GPEVINAIQK YIKDETIAMM LRDKTVYNID DSTIYFLENF SRIIQKDYLP
TEEDILKSRV PTSGVIQYKI MLKNFNFRIF DVGGQRAQRR KWLHVFDDVQ AVLFITSLSE
YDQVLREDAT VNRMKESLNL FEKICNGRYF LNTAMILFLN KIDLFKIKIK HTNITVALTS
YKGPQECDSA LDYIRKRFIS LNKNKKRSIY EHVTCATDTE QIQVVIDSVI DVVIQHTMQK
VGIQ
