GBG_CAEBR
ID GBG_CAEBR Reviewed; 62 AA.
AC Q4VT26; A8WM74; Q629E8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Guanine nucleotide-binding protein subunit gamma;
DE Flags: Precursor;
GN Name=gpc-1; ORFNames=CBG00049;
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 a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC Interacts with gpb-1 and gpb-2. {ECO:0000250|UniProtKB:P54406,
CC ECO:0000250|UniProtKB:P63212}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR EMBL; AY634304; AAW02910.1; -; Genomic_DNA.
DR EMBL; HE601409; CAP21578.2; -; Genomic_DNA.
DR AlphaFoldDB; Q4VT26; -.
DR SMR; Q4VT26; -.
DR STRING; 6238.CBG00049; -.
DR PRIDE; Q4VT26; -.
DR EnsemblMetazoa; CBG00049.1; CBG00049.1; WBGene00023553.
DR WormBase; CBG00049; CBP37073; WBGene00023553; Cbr-gpc-1.
DR eggNOG; KOG4119; Eukaryota.
DR HOGENOM; CLU_168377_3_1_1; -.
DR InParanoid; Q4VT26; -.
DR OMA; MDIMASN; -.
DR OrthoDB; 1581168at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050909; P:sensory perception of taste; IEA:EnsemblMetazoa.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR13809; PTHR13809; 1.
DR Pfam; PF00631; G-gamma; 1.
DR PRINTS; PR00321; GPROTEING.
DR SMART; SM00224; GGL; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW Reference proteome; Transducer.
FT CHAIN 1..59
FT /note="Guanine nucleotide-binding protein subunit gamma"
FT /id="PRO_0000042165"
FT PROPEP 60..62
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042166"
FT MOD_RES 59
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 59
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 62 AA; 7023 MW; 3C9C1318B215ECAE CRC64;
MENIKTTTEQ LRTEANIQRK KVSEVAKDLV EFCEKNKATD MLVSGPLDAH NPFQEKKSCS
VL