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GBG1_CANLF
ID   GBG1_CANLF              Reviewed;          74 AA.
AC   P63210; O43835; Q08447; Q16026;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 111.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9300552; DOI=10.1016/s0034-5288(97)90208-3;
RA   Kylma T., Paulin L., Hurwitz M.Y., Hurwitz R.L., Kommonen B.;
RT   "Cloning of the cDNA encoding rod photoreceptor cGMP-phosphodiesterase
RT   alpha and gamma subunits from the retinal degenerate Labrador retriever
RT   dog.";
RL   Res. Vet. Sci. 62:293-296(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Dekomien G., Epplen J.T.;
RT   "Characterization of the canine GNGT1 gene.";
RL   Submitted (AUG-2002) 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.
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}.
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DR   EMBL; Z75156; CAA99470.1; -; mRNA.
DR   EMBL; AJ507014; CAD44991.1; -; Genomic_DNA.
DR   EMBL; AJ507015; CAD44991.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001003225.1; NM_001003225.1.
DR   RefSeq; XP_005628403.1; XM_005628346.2.
DR   AlphaFoldDB; P63210; -.
DR   SMR; P63210; -.
DR   STRING; 9615.ENSCAFP00000003005; -.
DR   PaxDb; P63210; -.
DR   Ensembl; ENSCAFT00030027907; ENSCAFP00030024354; ENSCAFG00030015119.
DR   Ensembl; ENSCAFT00040020630; ENSCAFP00040017906; ENSCAFG00040011163.
DR   Ensembl; ENSCAFT00845028968; ENSCAFP00845022789; ENSCAFG00845016275.
DR   GeneID; 403895; -.
DR   KEGG; cfa:403895; -.
DR   CTD; 2792; -.
DR   VEuPathDB; HostDB:ENSCAFG00845016275; -.
DR   GeneTree; ENSGT01050000244876; -.
DR   HOGENOM; CLU_168377_2_0_1; -.
DR   InParanoid; P63210; -.
DR   OMA; CEEVMEY; -.
DR   Reactome; R-CFA-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-CFA-202040; G-protein activation.
DR   Reactome; R-CFA-2485179; Activation of the phototransduction cascade.
DR   Reactome; R-CFA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-CFA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-CFA-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-CFA-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-CFA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-CFA-4086398; Ca2+ pathway.
DR   Reactome; R-CFA-416476; G alpha (q) signalling events.
DR   Reactome; R-CFA-416482; G alpha (12/13) signalling events.
DR   Reactome; R-CFA-418217; G beta:gamma signalling through PLC beta.
DR   Reactome; R-CFA-418555; G alpha (s) signalling events.
DR   Reactome; R-CFA-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-CFA-418594; G alpha (i) signalling events.
DR   Reactome; R-CFA-418597; G alpha (z) signalling events.
DR   Reactome; R-CFA-420092; Glucagon-type ligand receptors.
DR   Reactome; R-CFA-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-CFA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-CFA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-CFA-500657; Presynaptic function of Kainate receptors.
DR   Reactome; R-CFA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Reactome; R-CFA-8964315; G beta:gamma signalling through BTK.
DR   Reactome; R-CFA-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-CFA-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-CFA-9634597; GPER1 signaling.
DR   Reactome; R-CFA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   Proteomes; UP000002254; Chromosome 14.
DR   Bgee; ENSCAFG00000002044; Expressed in testis and 1 other tissue.
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:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007602; P:phototransduction; IEA:Ensembl.
DR   GO; GO:0008104; P:protein localization; IEA:Ensembl.
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   Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW   Reference proteome; Transducer.
FT   CHAIN           1..71
FT                   /note="Guanine nucleotide-binding protein G(T) subunit
FT                   gamma-T1"
FT                   /id="PRO_0000012603"
FT   PROPEP          72..74
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012604"
FT   MOD_RES         71
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           71
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   74 AA;  8496 MW;  B12B42BE00DB1C05 CRC64;
     MPVINIEDLT EKDKLKMEVD QLKKEVTLER MLVSKCCEEV RDYVEERSGE DPLVKGIPED
     KNPFKELKGG CVIS
 
 
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