GBG5_MOUSE
ID GBG5_MOUSE Reviewed; 68 AA.
AC Q80SZ7; P30670; Q5I0W4; Q61015;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
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 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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-53.
RC STRAIN=CF-1 / Harlan;
RX PubMed=8858601;
RX DOI=10.1002/(sici)1098-2795(199607)44:3<315::aid-mrd5>3.0.co;2-p;
RA Williams C.J., Schultz R.M., Kopf G.S.;
RT "G protein gene expression during mouse oocyte growth and maturation, and
RT preimplantation embryo development.";
RL Mol. Reprod. Dev. 44:315-323(1996).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
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).
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; BC002316; AAH02316.3; -; mRNA.
DR EMBL; BC087872; AAH87872.1; -; mRNA.
DR EMBL; U38498; AAB01729.1; -; mRNA.
DR CCDS; CCDS17903.1; -.
DR RefSeq; NP_034448.2; NM_010318.2.
DR RefSeq; XP_003945606.1; XM_003945557.2.
DR AlphaFoldDB; Q80SZ7; -.
DR SMR; Q80SZ7; -.
DR BioGRID; 199991; 3.
DR IntAct; Q80SZ7; 1.
DR STRING; 10090.ENSMUSP00000087485; -.
DR iPTMnet; Q80SZ7; -.
DR PhosphoSitePlus; Q80SZ7; -.
DR EPD; Q80SZ7; -.
DR jPOST; Q80SZ7; -.
DR MaxQB; Q80SZ7; -.
DR PaxDb; Q80SZ7; -.
DR PRIDE; Q80SZ7; -.
DR ProteomicsDB; 266777; -.
DR DNASU; 14707; -.
DR Ensembl; ENSMUST00000090031; ENSMUSP00000087485; ENSMUSG00000068523.
DR Ensembl; ENSMUST00000118280; ENSMUSP00000114014; ENSMUSG00000068523.
DR GeneID; 14707; -.
DR KEGG; mmu:14707; -.
DR UCSC; uc008rrk.1; mouse.
DR CTD; 2787; -.
DR MGI; MGI:109164; Gng5.
DR VEuPathDB; HostDB:ENSMUSG00000068523; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244858; -.
DR HOGENOM; CLU_168377_3_0_1; -.
DR InParanoid; Q80SZ7; -.
DR OMA; QNALHDP; -.
DR OrthoDB; 1581168at2759; -.
DR PhylomeDB; Q80SZ7; -.
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; 14707; 10 hits in 67 CRISPR screens.
DR ChiTaRS; Gng5; mouse.
DR PRO; PR:Q80SZ7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80SZ7; protein.
DR Bgee; ENSMUSG00000068523; Expressed in right kidney and 117 other tissues.
DR ExpressionAtlas; Q80SZ7; baseline and differential.
DR Genevisible; Q80SZ7; MM.
DR GO; GO:0031680; C:G-protein beta/gamma-subunit complex; ISO:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0072513; P:positive regulation of secondary heart field cardioblast proliferation; IMP: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 Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW Phosphoprotein; Prenylation; Reference proteome; 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_0000012629"
FT PROPEP 66..68
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012630"
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
