GBGT2_BOVIN
ID GBGT2_BOVIN Reviewed; 69 AA.
AC P50154; A6QLH8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2;
DE AltName: Full=G gamma-C;
DE AltName: Full=G-gamma-8;
DE Flags: Precursor;
GN Name=GNGT2; Synonyms=GNG8, GNGT8;
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=Retina;
RX PubMed=7721746; DOI=10.1074/jbc.270.15.8495;
RA Ong O.C., Yamane H.K., Phan K.B., Fong H.K., Bok D., Lee R.H.,
RA Fung B.K.-K.;
RT "Molecular cloning and characterization of the G protein gamma subunit of
RT cone photoreceptors.";
RL J. Biol. Chem. 270:8495-8500(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
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 -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR EMBL; U20085; AAB61306.1; -; mRNA.
DR EMBL; BC147970; AAI47971.1; -; mRNA.
DR PIR; A56378; A56378.
DR RefSeq; NP_776753.1; NM_174328.2.
DR RefSeq; XP_005220538.1; XM_005220481.3.
DR RefSeq; XP_010814418.1; XM_010816116.2.
DR AlphaFoldDB; P50154; -.
DR SMR; P50154; -.
DR STRING; 9913.ENSBTAP00000054464; -.
DR PaxDb; P50154; -.
DR Ensembl; ENSBTAT00000066198; ENSBTAP00000054464; ENSBTAG00000047325.
DR GeneID; 281797; -.
DR KEGG; bta:281797; -.
DR CTD; 2793; -.
DR VEuPathDB; HostDB:ENSBTAG00000047325; -.
DR VGNC; VGNC:29471; GNGT2.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244876; -.
DR HOGENOM; CLU_168377_2_1_1; -.
DR InParanoid; P50154; -.
DR OMA; KNPFREK; -.
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 19.
DR Bgee; ENSBTAG00000047325; Expressed in retina and 75 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:0003924; F:GTPase activity; 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 3: Inferred from homology;
KW Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW Reference proteome; Transducer.
FT CHAIN 1..66
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-T2"
FT /id="PRO_0000012641"
FT PROPEP 67..69
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012642"
FT MOD_RES 66
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 66
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 69 AA; 7728 MW; 210C8319D1520314 CRC64;
MAQELSEKEL LKMEVEQLKK EVKNPRALIS KTGKEIKDYV EAEAGNDPLL KGIPEDKNPF
KEKGGCIIS
