GBG3_BOVIN
ID GBG3_BOVIN Reviewed; 75 AA.
AC P63214; P29798; Q32KX4; Q61014;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3;
DE Flags: Precursor;
GN Name=GNG3; Synonyms=GNGT3;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=2122451; DOI=10.1073/pnas.87.20.7973;
RA Gautam N., Northup J., Tamir H., Simon M.I.;
RT "G protein diversity is increased by associations with a variety of gamma
RT subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7973-7977(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-19.
RC TISSUE=Brain;
RX PubMed=8276106; DOI=10.1016/0014-5793(94)80622-5;
RA Morishita R., Kato K., Asano T.;
RT "A brain-specific gamma subunit of G protein freed from the corresponding
RT beta subunit under non-denaturing conditions.";
RL FEBS Lett. 337:23-26(1994).
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 SCN8A. {ECO:0000250|UniProtKB:P63215}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain. Low levels in
CC testis. {ECO:0000269|PubMed:2122451}.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR EMBL; M58349; AAA30539.1; -; mRNA.
DR EMBL; BC109874; AAI09875.1; -; mRNA.
DR PIR; A36204; RGBOG3.
DR RefSeq; NP_776498.1; NM_174073.2.
DR AlphaFoldDB; P63214; -.
DR SMR; P63214; -.
DR DIP; DIP-587N; -.
DR STRING; 9913.ENSBTAP00000003257; -.
DR PaxDb; P63214; -.
DR Ensembl; ENSBTAT00000003257; ENSBTAP00000003257; ENSBTAG00000002508.
DR GeneID; 281204; -.
DR KEGG; bta:281204; -.
DR CTD; 2785; -.
DR VEuPathDB; HostDB:ENSBTAG00000002508; -.
DR VGNC; VGNC:29466; GNG3.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244876; -.
DR HOGENOM; CLU_168377_0_1_1; -.
DR InParanoid; P63214; -.
DR OMA; CEAHACD; -.
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 29.
DR Bgee; ENSBTAG00000002508; Expressed in Ammon's horn and 104 other tissues.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
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 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 Cell membrane; Direct protein sequencing; Lipoprotein; Membrane;
KW Methylation; Phosphoprotein; Prenylation; Reference proteome; Transducer.
FT CHAIN 1..72
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-3"
FT /id="PRO_0000012615"
FT PROPEP 73..75
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012616"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63216"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63216"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63216"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63216"
FT MOD_RES 72
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 72
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 75 AA; 8305 MW; 35CC03965FE69A9D CRC64;
MKGETPVNST MSIGQARKMV EQLKIEASLC RIKVSKAAAD LMTYCDAHAC EDPLITPVPT
SENPFREKKF FCALL
