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GBGT2_CANLF
ID   GBGT2_CANLF             Reviewed;          69 AA.
AC   O97564;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2;
DE   AltName: Full=G gamma-C;
DE   AltName: Full=Tgamma c;
DE   Flags: Precursor;
GN   Name=GNGT2;
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=9727399;
RA   Akhmedov N.B., Piriev N.I., Pearce-Kelling S., Acland G.M., Aguirre G.D.,
RA   Farber D.B.;
RT   "Canine cone transducin-gamma gene and cone degeneration in the cd dog.";
RL   Invest. Ophthalmol. Vis. Sci. 39:1775-1781(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   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; AF038862; AAC98924.1; -; mRNA.
DR   RefSeq; NP_001003071.1; NM_001003071.2.
DR   RefSeq; XP_005624381.1; XM_005624324.2.
DR   RefSeq; XP_005624382.1; XM_005624325.2.
DR   RefSeq; XP_005624383.1; XM_005624326.1.
DR   RefSeq; XP_013971936.1; XM_014116461.1.
DR   RefSeq; XP_013971937.1; XM_014116462.1.
DR   AlphaFoldDB; O97564; -.
DR   SMR; O97564; -.
DR   STRING; 9615.ENSCAFP00000024872; -.
DR   PaxDb; O97564; -.
DR   Ensembl; ENSCAFT00030002649; ENSCAFP00030002360; ENSCAFG00030001482.
DR   Ensembl; ENSCAFT00040017061; ENSCAFP00040014788; ENSCAFG00040009199.
DR   GeneID; 403617; -.
DR   KEGG; cfa:403617; -.
DR   CTD; 2793; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   HOGENOM; CLU_168377_2_1_1; -.
DR   InParanoid; O97564; -.
DR   OMA; KNPFREK; -.
DR   OrthoDB; 1586104at2759; -.
DR   TreeFam; TF319909; -.
DR   Reactome; R-CFA-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-CFA-202040; G-protein activation.
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; Unplaced.
DR   Bgee; ENSCAFG00000016918; Expressed in bone marrow and 48 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   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW   Reference proteome; Transducer.
FT   CHAIN           1..66
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT                   subunit gamma-T2"
FT                   /id="PRO_0000012643"
FT   PROPEP          67..69
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012644"
FT   REGION          47..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           66
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   69 AA;  7746 MW;  210C85D9D1520314 CRC64;
     MAQELSEKEL LKMEVEQLKK EVKNPRALIS KTGKEIKDYV EAEAGNDPLL KGIPEDKNPF
     KEKGGCMIS
 
 
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