GBG2_BOVIN
ID GBG2_BOVIN Reviewed; 71 AA.
AC P63212; P16874; Q2KI31; Q61013; Q9TS47;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2;
DE AltName: Full=G gamma-I;
DE Flags: Precursor;
GN Name=GNG2;
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 14-62.
RC TISSUE=Adrenal gland, and Brain;
RX PubMed=2506169; DOI=10.1016/s0021-9258(18)71540-8;
RA Robishaw J.D., Kalman V.K., Moomaw C.R., Slaughter C.A.;
RT "Existence of two gamma subunits of the G proteins in brain.";
RL J. Biol. Chem. 264:15758-15761(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2499046; DOI=10.1126/science.2499046;
RA Gautam N., Baetscher M., Aebersold R., Simon M.I.;
RT "A G protein gamma subunit shares homology with ras proteins.";
RL Science 244:971-974(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-71, ACETYLATION AT ALA-2, AND ISOPRENYLATION AT
RP CYS-68.
RC TISSUE=Brain;
RX PubMed=7626050; DOI=10.1006/bbrc.1995.1979;
RA Wilcox M.D., Schey K.L., Busman M., Hildebrandt J.D.;
RT "Determination of the complete covalent structure of the gamma 2 subunit of
RT bovine brain G proteins by mass spectrometry.";
RL Biochem. Biophys. Res. Commun. 212:367-374(1995).
RN [5]
RP PROTEIN SEQUENCE OF 2-64.
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).
RN [6]
RP ISOPRENYLATION AT CYS-68, AND METHYLATION AT CYS-68.
RX PubMed=1903391; DOI=10.1016/s0021-9258(18)92858-9;
RA Sanford J., Codina J., Birnbaumer L.;
RT "Gamma-subunits of G proteins, but not their alpha- or beta-subunits, are
RT polyisoprenylated. Studies on post-translational modifications using in
RT vitro translation with rabbit reticulocyte lysates.";
RL J. Biol. Chem. 266:9570-9579(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HETEROTRIMER.
RX PubMed=8521505; DOI=10.1016/0092-8674(95)90220-1;
RA Wall M.A., Coleman D.E., Lee E., Iniguez-Lluhi J.A., Posner B.A.,
RA Gilman A.G., Sprang S.R.;
RT "The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2.";
RL Cell 83:1047-1058(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-68 IN COMPLEX WITH GNB1 AND
RP GRK2, SUBCELLULAR LOCATION, AND ISOPRENYLATION AT CYS-68.
RX PubMed=12764189; DOI=10.1126/science.1082348;
RA Lodowski D.T., Pitcher J.A., Capel W.D., Lefkowitz R.J., Tesmer J.J.;
RT "Keeping G proteins at bay: a complex between G protein-coupled receptor
RT kinase 2 and Gbetagamma.";
RL Science 300:1256-1262(2003).
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 (PubMed:8521505). In this context, interacts with GNB2 (By similarity).
CC The heterodimer formed by GNB1 and GNG2 interacts with ARHGEF5 (By
CC similarity). The heterodimer formed by GNB1 and GNG2 interacts with
CC GRK2 (PubMed:12764189). {ECO:0000250|UniProtKB:P59768,
CC ECO:0000269|PubMed:12764189, ECO:0000269|PubMed:8521505}.
CC -!- INTERACTION:
CC P63212; P62871: GNB1; NbExp=6; IntAct=EBI-1036424, EBI-357141;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12764189};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side
CC {ECO:0000269|PubMed:12764189}.
CC -!- TISSUE SPECIFICITY: Adrenal gland and brain.
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; J05071; AAA30541.1; -; mRNA.
DR EMBL; M37183; AAA30555.1; -; mRNA.
DR EMBL; BC112789; AAI12790.1; -; mRNA.
DR PIR; B34228; RGBOG2.
DR RefSeq; NP_776497.1; NM_174072.4.
DR RefSeq; XP_005211711.1; XM_005211654.3.
DR RefSeq; XP_010807541.1; XM_010809239.2.
DR PDB; 1GG2; X-ray; 2.40 A; G=1-71.
DR PDB; 1GP2; X-ray; 2.30 A; G=1-71.
DR PDB; 1OMW; X-ray; 2.50 A; G=1-68.
DR PDB; 1XHM; X-ray; 2.70 A; B=1-71.
DR PDB; 2BCJ; X-ray; 3.06 A; G=1-71.
DR PDB; 3AH8; X-ray; 2.90 A; G=1-71.
DR PDB; 3CIK; X-ray; 2.75 A; G=1-68.
DR PDB; 3KRW; X-ray; 2.90 A; G=1-68.
DR PDB; 3KRX; X-ray; 3.10 A; G=1-68.
DR PDB; 3PSC; X-ray; 2.67 A; G=1-68.
DR PDB; 3PVU; X-ray; 2.48 A; G=1-68.
DR PDB; 3PVW; X-ray; 2.49 A; G=1-68.
DR PDB; 3SN6; X-ray; 3.20 A; G=1-68.
DR PDB; 3UZS; X-ray; 4.52 A; G=1-67.
DR PDB; 3V5W; X-ray; 2.07 A; G=1-71.
DR PDB; 4MK0; X-ray; 2.40 A; G=6-64.
DR PDB; 4PNK; X-ray; 2.56 A; G=1-71.
DR PDB; 5TDH; X-ray; 3.00 A; G/K=1-68.
DR PDB; 5VAI; EM; 4.10 A; G=1-68.
DR PDB; 5WG3; X-ray; 2.90 A; G=1-71.
DR PDB; 5WG4; X-ray; 2.31 A; G=1-71.
DR PDB; 5WG5; X-ray; 3.10 A; G=1-71.
DR PDB; 6C2Y; X-ray; 2.74 A; G=1-71.
DR PDB; 6CMO; EM; 4.50 A; G=1-68.
DR PDB; 6LPB; EM; 3.90 A; G=1-67.
DR PDB; 6NBF; EM; 3.00 A; G=1-71.
DR PDB; 6NBH; EM; 3.50 A; G=1-71.
DR PDB; 6NBI; EM; 4.00 A; G=1-71.
DR PDB; 6PCV; EM; 3.20 A; G=1-71.
DR PDB; 6U7C; X-ray; 2.44 A; G=1-71.
DR PDB; 7BW0; EM; 3.90 A; G=1-71.
DR PDB; 7BZ2; EM; 3.82 A; G=1-71.
DR PDB; 7CZ5; EM; 2.60 A; G=1-71.
DR PDB; 7D3S; EM; 2.90 A; G=1-67.
DR PDB; 7D68; EM; 3.00 A; G=1-71.
DR PDB; 7DB6; EM; 3.30 A; C=1-67.
DR PDB; 7DH5; EM; 3.16 A; G=1-67.
DR PDB; 7DHI; EM; 3.26 A; G=1-71.
DR PDB; 7DHR; EM; 3.80 A; G=1-71.
DR PDB; 7DTY; EM; 2.98 A; G=1-71.
DR PDB; 7DUQ; EM; 2.50 A; G=2-71.
DR PDB; 7DUR; EM; 3.30 A; G=2-71.
DR PDB; 7DW9; EM; 2.60 A; Y=1-71.
DR PDB; 7EIB; EM; 3.00 A; E=1-71.
DR PDB; 7EVM; EM; 2.50 A; G=2-71.
DR PDB; 7F16; EM; 2.80 A; G=1-71.
DR PDB; 7F2O; EM; 2.90 A; Y=1-71.
DR PDB; 7FIG; EM; 3.90 A; G=1-71.
DR PDB; 7FIH; EM; 3.20 A; G=1-71.
DR PDB; 7FII; EM; 4.30 A; G=1-71.
DR PDB; 7FIM; EM; 3.40 A; G=1-71.
DR PDB; 7FIN; EM; 3.10 A; G=1-71.
DR PDB; 7FIY; EM; 3.40 A; G=1-71.
DR PDB; 7JJO; EM; 2.60 A; G=1-71.
DR PDB; 7LJC; EM; 3.00 A; G=2-68.
DR PDB; 7LJD; EM; 3.20 A; G=2-68.
DR PDB; 7PIU; EM; 2.58 A; G=1-71.
DR PDB; 7PWD; X-ray; 2.60 A; G=1-71.
DR PDB; 7S0F; EM; 2.96 A; G=1-71.
DR PDB; 7S0G; EM; 3.86 A; G=1-71.
DR PDB; 7T6S; EM; 3.00 A; C=2-68.
DR PDB; 7T6T; EM; 3.20 A; C=2-68.
DR PDB; 7T6U; EM; 2.90 A; C=2-68.
DR PDB; 7T6V; EM; 3.10 A; C=2-68.
DR PDB; 7TD0; EM; 2.83 A; G=1-71.
DR PDB; 7TD1; EM; 3.08 A; G=1-71.
DR PDB; 7TD2; EM; 3.11 A; G=1-71.
DR PDB; 7TD3; EM; 3.00 A; G=1-71.
DR PDB; 7TD4; EM; 2.60 A; G=1-71.
DR PDB; 7V35; EM; 3.40 A; C=1-71.
DR PDB; 7V9L; EM; 2.60 A; Y=1-71.
DR PDB; 7V9M; EM; 3.29 A; Y=1-71.
DR PDB; 7VAB; EM; 3.20 A; G=1-64.
DR PDB; 7VBH; EM; 3.00 A; G=2-71.
DR PDB; 7VBI; EM; 3.00 A; G=2-71.
DR PDB; 7VGY; EM; 3.10 A; D=2-68.
DR PDB; 7VGZ; EM; 3.30 A; E=2-68.
DR PDBsum; 1GG2; -.
DR PDBsum; 1GP2; -.
DR PDBsum; 1OMW; -.
DR PDBsum; 1XHM; -.
DR PDBsum; 2BCJ; -.
DR PDBsum; 3AH8; -.
DR PDBsum; 3CIK; -.
DR PDBsum; 3KRW; -.
DR PDBsum; 3KRX; -.
DR PDBsum; 3PSC; -.
DR PDBsum; 3PVU; -.
DR PDBsum; 3PVW; -.
DR PDBsum; 3SN6; -.
DR PDBsum; 3UZS; -.
DR PDBsum; 3V5W; -.
DR PDBsum; 4MK0; -.
DR PDBsum; 4PNK; -.
DR PDBsum; 5TDH; -.
DR PDBsum; 5VAI; -.
DR PDBsum; 5WG3; -.
DR PDBsum; 5WG4; -.
DR PDBsum; 5WG5; -.
DR PDBsum; 6C2Y; -.
DR PDBsum; 6CMO; -.
DR PDBsum; 6LPB; -.
DR PDBsum; 6NBF; -.
DR PDBsum; 6NBH; -.
DR PDBsum; 6NBI; -.
DR PDBsum; 6PCV; -.
DR PDBsum; 6U7C; -.
DR PDBsum; 7BW0; -.
DR PDBsum; 7BZ2; -.
DR PDBsum; 7CZ5; -.
DR PDBsum; 7D3S; -.
DR PDBsum; 7D68; -.
DR PDBsum; 7DB6; -.
DR PDBsum; 7DH5; -.
DR PDBsum; 7DHI; -.
DR PDBsum; 7DHR; -.
DR PDBsum; 7DTY; -.
DR PDBsum; 7DUQ; -.
DR PDBsum; 7DUR; -.
DR PDBsum; 7DW9; -.
DR PDBsum; 7EIB; -.
DR PDBsum; 7EVM; -.
DR PDBsum; 7F16; -.
DR PDBsum; 7F2O; -.
DR PDBsum; 7FIG; -.
DR PDBsum; 7FIH; -.
DR PDBsum; 7FII; -.
DR PDBsum; 7FIM; -.
DR PDBsum; 7FIN; -.
DR PDBsum; 7FIY; -.
DR PDBsum; 7JJO; -.
DR PDBsum; 7LJC; -.
DR PDBsum; 7LJD; -.
DR PDBsum; 7PIU; -.
DR PDBsum; 7PWD; -.
DR PDBsum; 7S0F; -.
DR PDBsum; 7S0G; -.
DR PDBsum; 7T6S; -.
DR PDBsum; 7T6T; -.
DR PDBsum; 7T6U; -.
DR PDBsum; 7T6V; -.
DR PDBsum; 7TD0; -.
DR PDBsum; 7TD1; -.
DR PDBsum; 7TD2; -.
DR PDBsum; 7TD3; -.
DR PDBsum; 7TD4; -.
DR PDBsum; 7V35; -.
DR PDBsum; 7V9L; -.
DR PDBsum; 7V9M; -.
DR PDBsum; 7VAB; -.
DR PDBsum; 7VBH; -.
DR PDBsum; 7VBI; -.
DR PDBsum; 7VGY; -.
DR PDBsum; 7VGZ; -.
DR AlphaFoldDB; P63212; -.
DR SMR; P63212; -.
DR BioGRID; 158562; 1.
DR CORUM; P63212; -.
DR DIP; DIP-586N; -.
DR IntAct; P63212; 7.
DR STRING; 9913.ENSBTAP00000003959; -.
DR iPTMnet; P63212; -.
DR PaxDb; P63212; -.
DR PeptideAtlas; P63212; -.
DR PRIDE; P63212; -.
DR Ensembl; ENSBTAT00000003959; ENSBTAP00000003959; ENSBTAG00000003043.
DR GeneID; 281203; -.
DR KEGG; bta:281203; -.
DR CTD; 54331; -.
DR VEuPathDB; HostDB:ENSBTAG00000003043; -.
DR VGNC; VGNC:29465; GNG2.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244876; -.
DR HOGENOM; CLU_168377_0_1_1; -.
DR InParanoid; P63212; -.
DR OMA; GKQQPPM; -.
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 EvolutionaryTrace; P63212; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000003043; Expressed in omental fat pad and 104 other tissues.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISS:CAFA.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; IDA:BHF-UCL.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA: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 3D-structure; Acetylation; Cell membrane; Direct protein sequencing;
KW Lipoprotein; Membrane; Methylation; Prenylation; Reference proteome;
KW Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7626050,
FT ECO:0000269|PubMed:8439334"
FT CHAIN 2..68
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-2"
FT /id="PRO_0000012609"
FT PROPEP 69..71
FT /note="Removed in mature form"
FT /id="PRO_0000012610"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:7626050"
FT MOD_RES 68
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:1903391"
FT LIPID 68
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:12764189,
FT ECO:0000269|PubMed:1903391, ECO:0000269|PubMed:7626050"
FT HELIX 9..23
FT /evidence="ECO:0007829|PDB:3V5W"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:3V5W"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3V5W"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3V5W"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3V5W"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:3V5W"
SQ SEQUENCE 71 AA; 7850 MW; EDB74E4135E7A37A CRC64;
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP
FREKKFFCAI L
