GBG7_BOVIN
ID GBG7_BOVIN Reviewed; 68 AA.
AC P30671; A7MB87;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7;
DE AltName: Full=G gamma-II;
DE Flags: Precursor;
GN Name=GNG7; Synonyms=GNGT7;
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 PROTEIN SEQUENCE OF 19-25; 30-44 AND 46-60.
RC TISSUE=Brain;
RX PubMed=1385432; DOI=10.1016/s0021-9258(18)35939-8;
RA Cali J.J., Balcueva E.A., Rybalkin I., Robishaw J.D.;
RT "Selective tissue distribution of G protein gamma subunits, including a new
RT form of the gamma subunits identified by cDNA cloning.";
RL J. Biol. Chem. 267:24023-24027(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-59.
RC TISSUE=Brain;
RX PubMed=8439334; DOI=10.1006/bbrc.1993.1126;
RA Sohma H., Hashimoto H., Hiraike N., Ohguro H., Akino T.;
RT "Identification of a novel gamma-subunit from bovine brain GTP binding
RT regulatory proteins (Gi/o).";
RL Biochem. Biophys. Res. Commun. 190:849-856(1993).
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 -!- PTM: Ser-2 is probably acetylated.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR EMBL; M99393; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC151397; AAI51398.1; -; mRNA.
DR PIR; A45128; A45128.
DR RefSeq; NP_001106785.1; NM_001113314.1.
DR AlphaFoldDB; P30671; -.
DR SMR; P30671; -.
DR DIP; DIP-203N; -.
DR STRING; 9913.ENSBTAP00000010058; -.
DR PaxDb; P30671; -.
DR PRIDE; P30671; -.
DR Ensembl; ENSBTAT00000010058; ENSBTAP00000010058; ENSBTAG00000007644.
DR GeneID; 618399; -.
DR KEGG; bta:618399; -.
DR CTD; 2788; -.
DR VEuPathDB; HostDB:ENSBTAG00000007644; -.
DR VGNC; VGNC:29468; GNG7.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244858; -.
DR HOGENOM; CLU_168377_3_1_1; -.
DR InParanoid; P30671; -.
DR OMA; CDQHARS; -.
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 7.
DR Bgee; ENSBTAG00000007644; Expressed in floor plate of diencephalon and 102 other tissues.
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: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 Acetylation; Cell membrane; Direct protein sequencing; Lipoprotein;
KW Membrane; Methylation; Prenylation; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60262,
FT ECO:0000269|PubMed:8439334"
FT CHAIN 2..65
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-7"
FT /id="PRO_0000012633"
FT PROPEP 66..68
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012634"
FT MOD_RES 2
FT /note="Blocked amino end (Ser); alternate"
FT MOD_RES 2
FT /note="N-acetylserine; alternate"
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"
FT CONFLICT 27..29
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 68 AA; 7552 MW; 7041326CBD906312 CRC64;
MSATNNIAQA RKLVEQLRIE AGIERIKVSK ASSELMSYCE QHARNDPLLV GVPASENPFK
DKKPCIIL
