GBG1_BOVIN
ID GBG1_BOVIN Reviewed; 74 AA.
AC P02698;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Guanine nucleotide-binding protein G(T) subunit gamma-T1;
DE AltName: Full=Transducin gamma chain;
DE Flags: Precursor;
GN Name=GNGT1;
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].
RX PubMed=6438626; DOI=10.1073/pnas.81.22.6948;
RA Hurley J.B., Fong H.K.W., Teplow D.B., Dreyer W.J., Simon M.I.;
RT "Isolation and characterization of a cDNA clone for the gamma subunit of
RT bovine retinal transducin.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6948-6952(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2984674; DOI=10.1073/pnas.82.7.1936;
RA Yatsunami K., Pandya B.V., Oprian D.D., Khorana H.G.;
RT "cDNA-derived amino acid sequence of the gamma subunit of GTPase from
RT bovine rod outer segments.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1936-1940(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8500562; DOI=10.1006/exer.1993.1063;
RA Tao L., Pandey S., Simon M.I., Fong H.K.;
RT "Structure of the bovine transducin gamma subunit gene and analysis of
RT promoter function in transgenic mice.";
RL Exp. Eye Res. 56:497-507(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-40.
RX PubMed=6149748; DOI=10.1016/0006-291x(84)90944-6;
RA van Dop C., Medynski D.C., Sullivan K., Wu A.M., Fung B.K.-K., Bourne H.R.;
RT "Partial cDNA sequence of the gamma subunit of transducin.";
RL Biochem. Biophys. Res. Commun. 124:250-255(1984).
RN [5]
RP PROTEIN SEQUENCE OF 2-70.
RX PubMed=3917402; DOI=10.1016/0014-5793(85)80201-5;
RA Ovchinnikov Y.A., Lipkin V.M., Shuvaeva T.M., Bogachuk A.P.,
RA Shemyakin V.V.;
RT "Complete amino acid sequence of gamma-subunit of the GTP-binding protein
RT from cattle retina.";
RL FEBS Lett. 179:107-110(1985).
RN [6]
RP ISOPRENYLATION AT CYS-71, AND METHYLATION AT CYS-71.
RX PubMed=2385292; DOI=10.1038/346658a0;
RA Fukuda Y., Takao T., Ohguro H., Yoshizawa T., Akino T., Shimonishi Y.;
RT "Farnesylated gamma-subunit of photoreceptor G protein indispensable for
RT GTP-binding.";
RL Nature 346:658-660(1990).
RN [7]
RP ISOPRENYLATION AT CYS-71.
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 [8]
RP ISOPRENYLATION AT CYS-71.
RX PubMed=2217200; DOI=10.1073/pnas.87.19.7673;
RA Lai R.K., Perez-Sala D., Canada F.J., Rando R.R.;
RT "The gamma subunit of transducin is farnesylated.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7673-7677(1990).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF BETA-GAMMA DIMER.
RX PubMed=8552196; DOI=10.1038/379369a0;
RA Sondek J., Bohm A., Lambright D.G., Hamm H.E., Sigler P.B.;
RT "Crystal structure of a G-protein beta gamma dimer at 2.1-A resolution.";
RL Nature 379:369-374(1996).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH PHOSDUCIN.
RX PubMed=9739091; DOI=10.1016/s0969-2126(98)00102-6;
RA Loew A., Ho Y.K., Blundell T., Bax B.;
RT "Phosducin induces a structural change in transducin beta gamma.";
RL Structure 6:1007-1019(1998).
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 -!- TISSUE SPECIFICITY: Retinal rod outer segment.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
CC -!- CAUTION: In PubMed:3917402 the authors propose that Cys-36 and Cys-37
CC are disulfide bonded because they could not be observed during peptide
CC sequencing, but were observed after reduction by dithiothreitol and
CC reaction with labeled iodoacetamide. The crystallographic structures do
CC not support these cysteines being disulfide bonded. Artifactual
CC oxidation and some other cysteine modifications might be consistent
CC with these observations. {ECO:0000305}.
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DR EMBL; K03255; AAA30794.1; -; mRNA.
DR EMBL; K02199; AAA30793.1; -; mRNA.
DR EMBL; S62031; AAB26895.1; -; Genomic_DNA.
DR EMBL; S62029; AAB26895.1; JOINED; Genomic_DNA.
DR EMBL; K02436; AAA30788.1; -; mRNA.
DR PIR; I46939; RGBOGT.
DR RefSeq; NP_776752.1; NM_174327.3.
DR RefSeq; XP_010802285.1; XM_010803983.2.
DR PDB; 1A0R; X-ray; 2.80 A; G=2-66.
DR PDB; 1B9X; X-ray; 3.00 A; B=1-68.
DR PDB; 1B9Y; X-ray; 3.00 A; B=1-68.
DR PDB; 1GOT; X-ray; 2.00 A; G=2-66.
DR PDB; 1MF6; NMR; -; A=60-71.
DR PDB; 1TBG; X-ray; 2.10 A; E/F/G/H=2-68.
DR PDB; 2TRC; X-ray; 2.40 A; G=1-68.
DR PDB; 5KDO; X-ray; 1.90 A; G=1-74.
DR PDB; 6B20; X-ray; 2.34 A; C/D=7-66.
DR PDB; 6OY9; EM; 3.90 A; G=2-74.
DR PDB; 6OYA; EM; 3.30 A; G=2-74.
DR PDB; 6QNO; EM; 4.38 A; G=1-74.
DR PDB; 7O7F; EM; 3.15 A; G=1-74.
DR PDBsum; 1A0R; -.
DR PDBsum; 1B9X; -.
DR PDBsum; 1B9Y; -.
DR PDBsum; 1GOT; -.
DR PDBsum; 1MF6; -.
DR PDBsum; 1TBG; -.
DR PDBsum; 2TRC; -.
DR PDBsum; 5KDO; -.
DR PDBsum; 6B20; -.
DR PDBsum; 6OY9; -.
DR PDBsum; 6OYA; -.
DR PDBsum; 6QNO; -.
DR PDBsum; 7O7F; -.
DR AlphaFoldDB; P02698; -.
DR SMR; P02698; -.
DR BioGRID; 159110; 1.
DR CORUM; P02698; -.
DR DIP; DIP-29228N; -.
DR IntAct; P02698; 1.
DR MINT; P02698; -.
DR STRING; 9913.ENSBTAP00000003465; -.
DR PaxDb; P02698; -.
DR PRIDE; P02698; -.
DR ABCD; P02698; 3 sequenced antibodies.
DR Ensembl; ENSBTAT00000003465; ENSBTAP00000003465; ENSBTAG00000002674.
DR Ensembl; ENSBTAT00000082378; ENSBTAP00000060879; ENSBTAG00000002674.
DR GeneID; 281796; -.
DR KEGG; bta:281796; -.
DR CTD; 2792; -.
DR VEuPathDB; HostDB:ENSBTAG00000002674; -.
DR VGNC; VGNC:29470; GNGT1.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244876; -.
DR HOGENOM; CLU_168377_2_0_1; -.
DR InParanoid; P02698; -.
DR OMA; CEEVMEY; -.
DR OrthoDB; 1573820at2759; -.
DR TreeFam; TF319909; -.
DR EvolutionaryTrace; P02698; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000002674; Expressed in retina and 56 other tissues.
DR ExpressionAtlas; P02698; baseline.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
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 3D-structure; Cell membrane; Direct protein sequencing; Lipoprotein;
KW Membrane; Methylation; Prenylation; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3917402"
FT CHAIN 2..71
FT /note="Guanine nucleotide-binding protein G(T) subunit
FT gamma-T1"
FT /id="PRO_0000012601"
FT PROPEP 72..74
FT /note="Removed in mature form"
FT /id="PRO_0000012602"
FT MOD_RES 71
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:2385292"
FT LIPID 71
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:1903391,
FT ECO:0000269|PubMed:2217200, ECO:0000269|PubMed:2385292"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1TBG"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1A0R"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:5KDO"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:5KDO"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5KDO"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:5KDO"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5KDO"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:1MF6"
SQ SEQUENCE 74 AA; 8544 MW; B12B580FABDB1C05 CRC64;
MPVINIEDLT EKDKLKMEVD QLKKEVTLER MLVSKCCEEF RDYVEERSGE DPLVKGIPED
KNPFKELKGG CVIS
