GBG4_MOUSE
ID GBG4_MOUSE Reviewed; 75 AA.
AC P50153;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4;
DE Flags: Precursor;
GN Name=Gng4; Synonyms=Gngt4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7488078; DOI=10.1006/bbrc.1995.2600;
RA Kalyanaraman S., Kalyanaraman V., Gautam N.;
RT "A brain-specific G protein gamma subunit.";
RL Biochem. Biophys. Res. Commun. 216:126-132(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9570961; DOI=10.1006/geno.1998.5223;
RA Kalyanaraman S., Copeland N.G., Gilbert D.G., Jenkins N.A., Gautam N.;
RT "Structure and chromosomal localization of mouse G protein subunit gamma4
RT gene.";
RL Genomics 49:147-151(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH KCNK1.
RX PubMed=24496152; DOI=10.1038/ncomms4227;
RA Hwang E.M., Kim E., Yarishkin O., Woo D.H., Han K.S., Park N., Bae Y.,
RA Woo J., Kim D., Park M., Lee C.J., Park J.Y.;
RT "A disulphide-linked heterodimer of TWIK-1 and TREK-1 mediates passive
RT conductance in astrocytes.";
RL Nat. Commun. 5:3227-3227(2014).
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. {ECO:0000305}.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC Interacts with beta-1 and beta-2, but not with beta-3 (By similarity).
CC Interacts with KCNK1. {ECO:0000250|UniProtKB:P50150,
CC ECO:0000269|PubMed:24496152}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:7488078}.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR EMBL; U37527; AAB93460.1; -; mRNA.
DR EMBL; AF038594; AAC40090.1; -; Genomic_DNA.
DR EMBL; AF038593; AAC40090.1; JOINED; Genomic_DNA.
DR EMBL; BC016506; AAH16506.1; -; mRNA.
DR CCDS; CCDS36598.1; -.
DR PIR; JC4339; JC4339.
DR RefSeq; NP_001289926.1; NM_001302997.1.
DR RefSeq; NP_034447.1; NM_010317.3.
DR AlphaFoldDB; P50153; -.
DR SMR; P50153; -.
DR BioGRID; 199990; 1.
DR DIP; DIP-494N; -.
DR IntAct; P50153; 1.
DR STRING; 10090.ENSMUSP00000021734; -.
DR iPTMnet; P50153; -.
DR PhosphoSitePlus; P50153; -.
DR MaxQB; P50153; -.
DR PaxDb; P50153; -.
DR PeptideAtlas; P50153; -.
DR PRIDE; P50153; -.
DR ProteomicsDB; 272936; -.
DR Antibodypedia; 34696; 98 antibodies from 23 providers.
DR DNASU; 14706; -.
DR Ensembl; ENSMUST00000021734; ENSMUSP00000021734; ENSMUSG00000021303.
DR GeneID; 14706; -.
DR KEGG; mmu:14706; -.
DR UCSC; uc007pml.2; mouse.
DR CTD; 2786; -.
DR MGI; MGI:102703; Gng4.
DR VEuPathDB; HostDB:ENSMUSG00000021303; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244876; -.
DR HOGENOM; CLU_168377_0_1_1; -.
DR InParanoid; P50153; -.
DR OMA; HMGEDPL; -.
DR OrthoDB; 1581168at2759; -.
DR PhylomeDB; P50153; -.
DR TreeFam; TF319909; -.
DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-MMU-202040; G-protein activation.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-MMU-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-MMU-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-MMU-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-418597; G alpha (z) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-MMU-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-MMU-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-MMU-9634597; GPER1 signaling.
DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 14706; 1 hit in 73 CRISPR screens.
DR PRO; PR:P50153; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P50153; protein.
DR Bgee; ENSMUSG00000021303; Expressed in facial nucleus and 156 other tissues.
DR Genevisible; P50153; MM.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISA:MGI.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISA:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
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; Lipoprotein; Membrane; Methylation; Prenylation;
KW Reference proteome; Transducer.
FT CHAIN 1..72
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-4"
FT /id="PRO_0000012623"
FT PROPEP 73..75
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012624"
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; 8405 MW; 42FAEF47311FA195 CRC64;
MKEGMSNNST TSISQARKAV EQLKMEACMD RVKVSQAASD LLAYCEAHVR EDPLIIPVPA
SENPFREKKF FCTIL
