GBG5_RAT
ID GBG5_RAT Reviewed; 68 AA.
AC P63219; P30670; Q61015;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1549114; DOI=10.1128/mcb.12.4.1585-1591.1992;
RA Fisher K.J., Aronson N.N. Jr.;
RT "Characterization of the cDNA and genomic sequence of a G protein gamma
RT subunit (gamma 5).";
RL Mol. Cell. Biol. 12:1585-1591(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M95780; AAA41188.1; -; mRNA.
DR EMBL; BC058469; AAH58469.1; -; mRNA.
DR RefSeq; NP_077353.1; NM_024377.1.
DR RefSeq; XP_017445483.1; XM_017589994.1.
DR RefSeq; XP_017460456.1; XM_017604967.1.
DR AlphaFoldDB; P63219; -.
DR SMR; P63219; -.
DR STRING; 10116.ENSRNOP00000021358; -.
DR jPOST; P63219; -.
DR PaxDb; P63219; -.
DR Ensembl; ENSRNOT00000105080; ENSRNOP00000087679; ENSRNOG00000063636.
DR GeneID; 108349548; -.
DR GeneID; 79218; -.
DR KEGG; rno:108349548; -.
DR KEGG; rno:79218; -.
DR CTD; 2787; -.
DR RGD; 620807; Gng5.
DR VEuPathDB; HostDB:ENSRNOG00000038205; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244858; -.
DR HOGENOM; CLU_168377_3_0_1; -.
DR InParanoid; P63219; -.
DR OMA; QNALHDP; -.
DR OrthoDB; 1581168at2759; -.
DR PhylomeDB; P63219; -.
DR TreeFam; TF319909; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-202040; G-protein activation.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-RNO-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-RNO-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-418597; G alpha (z) signalling events.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-RNO-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:P63219; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015936; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; P63219; RN.
DR GO; GO:0031680; C:G-protein beta/gamma-subunit complex; IDA:MGI.
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:0030165; F:PDZ domain binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0072513; P:positive regulation of secondary heart field cardioblast proliferation; ISO:RGD.
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 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_0000012631"
FT PROPEP 66..68
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012632"
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