GBG7_RAT
ID GBG7_RAT Reviewed; 68 AA.
AC P43425; Q45QK4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7;
DE Flags: Precursor;
GN Name=Gng7; Synonyms=Gngt7;
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].
RX PubMed=7807587; DOI=10.1002/jnr.490390113;
RA Watson J.B., Coulter P.M. II, Margulies J.E., de Lecea L., Danielson P.E.,
RA Erlander M.G., Sutcliffe J.G.;
RT "G-protein gamma 7 subunit is selectively expressed in medium-sized neurons
RT and dendrites of the rat neostriatum.";
RL J. Neurosci. Res. 39:108-116(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SHR, and Wistar Kyoto;
RA Jackson E.K., Zhu C.;
RT "Genetic similarity between spontaneously hypertensive rats and Wistar-
RT Kyoto rats in the coding regions of signal transduction proteins.";
RL Submitted (JUL-2005) 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. Plays a role in the regulation of adenylyl cyclase
CC signaling in certain regions of the brain. Plays a role in the
CC formation or stabilzation of a G protein heterotrimer (G(olf) subunit
CC alpha-beta-gamma-7) that is required for adenylyl cyclase activity in
CC the striatum (By similarity). {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Expressed in a variety of tissues.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA65640.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L23219; AAA65640.1; ALT_INIT; mRNA.
DR EMBL; DQ120497; AAZ23836.1; -; mRNA.
DR EMBL; DQ120498; AAZ23837.1; -; mRNA.
DR PIR; I56580; I56580.
DR RefSeq; NP_077052.1; NM_024138.1.
DR RefSeq; XP_017450559.1; XM_017595070.1.
DR RefSeq; XP_017450560.1; XM_017595071.1.
DR AlphaFoldDB; P43425; -.
DR SMR; P43425; -.
DR BioGRID; 248710; 2.
DR IntAct; P43425; 1.
DR MINT; P43425; -.
DR STRING; 10116.ENSRNOP00000026893; -.
DR jPOST; P43425; -.
DR PaxDb; P43425; -.
DR PRIDE; P43425; -.
DR GeneID; 58979; -.
DR KEGG; rno:58979; -.
DR UCSC; RGD:61860; rat.
DR CTD; 2788; -.
DR RGD; 61860; Gng7.
DR eggNOG; KOG4119; Eukaryota.
DR InParanoid; P43425; -.
DR OMA; CDQHARS; -.
DR OrthoDB; 1581168at2759; -.
DR PhylomeDB; P43425; -.
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:P43425; -.
DR Proteomes; UP000002494; Unplaced.
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:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISO:RGD.
DR GO; GO:0045761; P:regulation of adenylate cyclase activity; 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 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW Prenylation; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60262"
FT CHAIN 2..65
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-7"
FT /id="PRO_0000012639"
FT PROPEP 66..68
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012640"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O60262"
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; 7524 MW; 62C607CCB82ADC12 CRC64;
MSGTNNVAQA RKLVEQLRIE AGIERIKVSK ASSELMSYCE QHARNDPLLV GVPASENPFK
DKKPCIIL
