GPA8_CAEBR
ID GPA8_CAEBR Reviewed; 364 AA.
AC Q61MC6; A8X758;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Guanine nucleotide-binding protein alpha-8 subunit;
GN Name=gpa-8; ORFNames=CBG08544;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=15856303; DOI=10.1007/s00438-004-1105-6;
RA Jovelin R., Phillips P.C.;
RT "Functional constraint and divergence in the G protein family in
RT Caenorhabditis elegans and Caenorhabditis briggsae.";
RL Mol. Genet. Genomics 273:299-310(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; AY634301; AAW02907.1; -; Genomic_DNA.
DR EMBL; HE601197; CAP28469.1; -; Genomic_DNA.
DR RefSeq; XP_002636260.1; XM_002636214.1.
DR AlphaFoldDB; Q61MC6; -.
DR SMR; Q61MC6; -.
DR STRING; 6238.CBG08544; -.
DR EnsemblMetazoa; CBG08544.1; CBG08544.1; WBGene00030312.
DR GeneID; 8578255; -.
DR KEGG; cbr:CBG_08544; -.
DR CTD; 8578255; -.
DR WormBase; CBG08544; CBP02126; WBGene00030312; Cbr-gpa-8.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q61MC6; -.
DR OMA; RIREKDY; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000008549; 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 3: Inferred from homology;
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_0000203642"
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; 42412 MW; 3EF02ACCF61617B9 CRC64;
MGALCSSETY MLDKETYKKQ VEHNKMIEQD LDKDRKLKIL KLLILGPGES GKSTTIKQIK
IIHDEGYSVE EKLIRRHGIF MNILEGIEEI HLAVGRENKS YKNPLSFDHI HEVRMFTENF
KKADEADKIL GAEVINAIQK YVKDETVAMM LRDKTVYNID DSTIYFLDNF SRIIQKDYLP
TEEDILKSRV PTSGVIQYKI MLKNFNFKIF DVGGQRAQRR KWLHVFDDVH AVLFITSLSE
YDQVLREDAT VNRMKESLNL FEKICNGRYF INTAMILFLN KIDLFEIKIK HTNITVALTS
YKGPQERDSA LDYIRKRFVS LNKNKKRSIY EHVTCATDTE QIQVVIDSVI DVVIQHTMQK
VGIQ
