ID   GBG5_BOVIN              Reviewed;          68 AA.
AC   P63217; P30670; Q3ZCC0; Q61015;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5;
DE   Flags: Precursor;
GN   Name=GNG5; Synonyms=GNGT5;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1549114; DOI=10.1128/mcb.12.4.1585-1591.1992;
RA   Fisher K.J., Aronson N.N. Jr.;
RT   "Characterization of the cDNA and genomic sequence of a G protein gamma
RT   subunit (gamma 5).";
RL   Mol. Cell. Biol. 12:1585-1591(1992).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Spleen;
RX   PubMed=8352779; DOI=10.1006/bbrc.1993.1953;
RA   Morishita R., Masuda K., Niwa M., Kato K., Asano T.;
RT   "Identification of three forms of the gamma subunit of G proteins isolated
RT   from bovine spleen.";
RL   Biochem. Biophys. Res. Commun. 194:1221-1227(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in a variety of tissues.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; M95779; AAA30535.1; -; mRNA.
DR   EMBL; BC102572; AAI02573.1; -; mRNA.
DR   PIR; B42243; B42243.
DR   RefSeq; NP_777236.1; NM_174811.4.
DR   AlphaFoldDB; P63217; -.
DR   SMR; P63217; -.
DR   DIP; DIP-324N; -.
DR   STRING; 9913.ENSBTAP00000010682; -.
DR   PaxDb; P63217; -.
DR   PRIDE; P63217; -.
DR   Ensembl; ENSBTAT00000010682; ENSBTAP00000010682; ENSBTAG00000008122.
DR   GeneID; 287018; -.
DR   KEGG; bta:287018; -.
DR   CTD; 2787; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008122; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01050000244858; -.
DR   HOGENOM; CLU_168377_3_0_1; -.
DR   InParanoid; P63217; -.
DR   OMA; QNALHDP; -.
DR   OrthoDB; 1581168at2759; -.
DR   TreeFam; TF319909; -.
DR   Reactome; R-BTA-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-BTA-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-BTA-416476; G alpha (q) signalling events.
DR   Reactome; R-BTA-418594; G alpha (i) signalling events.
DR   Reactome; R-BTA-418597; G alpha (z) signalling events.
DR   Reactome; R-BTA-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-BTA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-BTA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000008122; Expressed in thyroid gland and 104 other tissues.
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:0030165; F:PDZ domain binding; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Direct protein sequencing; Lipoprotein;
KW   Membrane; Methylation; Phosphoprotein; Prenylation; Reference proteome;
KW   Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P63218"
FT   CHAIN           2..65
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT                   subunit gamma-5"
FT                   /id="PRO_0000012625"
FT   PROPEP          66..68
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012626"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P63218"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P63218"
FT   MOD_RES         65
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           65
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   68 AA;  7318 MW;  9AF7A16558863602 CRC64;
     MSGSSSVAAM KKVVQQLRLE AGLNRVKVSQ AAADLKQFCL QNAQHDPLLT GVSSSTNPFR
     PQKVCSFL