ID   GBG12_BOVIN             Reviewed;          72 AA.
AC   Q28024; A5PJE1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;
DE   AltName: Full=Gamma-S1;
DE   Flags: Precursor;
GN   Name=GNG12; Synonyms=GNGT12;
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], ACETYLATION AT SER-2, METHYLATION AT CYS-69,
RP   ISOPRENYLATION AT CYS-69, PARTIAL PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Spleen;
RX   PubMed=7493986; DOI=10.1074/jbc.270.49.29469;
RA   Morishita R., Nakayama H., Isobe T., Matsuda T., Hashimoto Y., Okano T.,
RA   Fukada Y., Mizuno K., Ohno S., Kozawa O., Kato K., Asano T.;
RT   "Primary structure of a gamma subunit of G protein, gamma 12, and its
RT   phosphorylation by protein kinase C.";
RL   J. Biol. Chem. 270:29469-29475(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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: Present in all tissues tested.
CC   -!- PTM: It is not sure whether phosphorylation by PKC is on Ser-2 or Ser-
CC       3.
CC   -!- MASS SPECTROMETRY: Mass=7925; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:7493986};
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; U37561; AAC48490.1; -; mRNA.
DR   EMBL; BC142068; AAI42069.1; -; mRNA.
DR   RefSeq; NP_777210.1; NM_174785.2.
DR   AlphaFoldDB; Q28024; -.
DR   SMR; Q28024; -.
DR   STRING; 9913.ENSBTAP00000009857; -.
DR   iPTMnet; Q28024; -.
DR   PaxDb; Q28024; -.
DR   PeptideAtlas; Q28024; -.
DR   PRIDE; Q28024; -.
DR   Ensembl; ENSBTAT00000076754; ENSBTAP00000072397; ENSBTAG00000054533.
DR   GeneID; 286850; -.
DR   KEGG; bta:286850; -.
DR   CTD; 55970; -.
DR   VEuPathDB; HostDB:ENSBTAG00000054533; -.
DR   VGNC; VGNC:29463; GNG12.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01050000244858; -.
DR   HOGENOM; CLU_168377_3_1_1; -.
DR   InParanoid; Q28024; -.
DR   OMA; MDIMASN; -.
DR   OrthoDB; 1581168at2759; -.
DR   TreeFam; TF319909; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000054533; Expressed in omental fat pad and 106 other tissues.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; IEA:InterPro.
DR   GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
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:0000269|PubMed:7493986"
FT   CHAIN           2..69
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT                   subunit gamma-12"
FT                   /id="PRO_0000012665"
FT   PROPEP          70..72
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012666"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:7493986"
FT   MOD_RES         3
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DAS9"
FT   MOD_RES         42
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DAS9"
FT   MOD_RES         69
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000269|PubMed:7493986"
FT   LIPID           69
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:7493986"
SQ   SEQUENCE   72 AA;  8057 MW;  050859E0BAE7FABC CRC64;
     MSSKTASTNN IAQARRTVQQ LRMEASIERI KVSKASADLM SYCEEHARND PLLMGIPTSE
     NPFKDKKTCT IL