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Database: UniProt
Entry: GNAT3_BOVIN
LinkDB: GNAT3_BOVIN
Original site: GNAT3_BOVIN 
ID   GNAT3_BOVIN             Reviewed;         354 AA.
AC   P0C7Q4;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-3;
DE   AltName: Full=Gustducin alpha-3 chain;
GN   Name=GNAT3;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   MUTAGENESIS OF GLY-352, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=9671782; DOI=10.1073/pnas.95.15.8933;
RA   Ming D., Ruiz-Avila L., Margolskee R.F.;
RT   "Characterization and solubilization of bitter-responsive receptors that
RT   couple to gustducin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8933-8938(1998).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16928202; DOI=10.1111/j.1469-7580.2006.00617.x;
RA   Tizzano M., Merigo F., Sbarbati A.;
RT   "Evidence of solitary chemosensory cells in a large mammal: the diffuse
RT   chemosensory system in Bos taurus airways.";
RL   J. Anat. 209:333-337(2006).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17021831; DOI=10.1007/s00359-006-0168-8;
RA   Fehr J., Meyer D., Widmayer P., Borth H.C., Ackermann F., Wilhelm B.,
RA   Gudermann T., Boekhoff I.;
RT   "Expression of the G-protein alpha-subunit gustducin in mammalian
RT   spermatozoa.";
RL   J. Comp. Physiol. A 193:21-34(2007).
CC   -!- FUNCTION: Guanine nucleotide-binding protein (G protein) alpha subunit
CC       playing a prominent role in bitter and sweet taste transduction as well
CC       as in umami (monosodium glutamate, monopotassium glutamate, and inosine
CC       monophosphate) taste transduction.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma,
CC       respectively GNAT3, GNB1 and GNG13 for Gustducin heterotrimer for
CC       bitter taste transduction. The alpha chain contains the guanine
CC       nucleotide binding site. Gustducin heterotrimer may also be composed of
CC       GNAT3, GNB3 and GNG13.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in epithelial cells of taste buds of the
CC       circumvallate, foliate and fungiform. Detected in various region of the
CC       respiratory track. Expressed also in spermatozoa.
CC       {ECO:0000269|PubMed:16928202, ECO:0000269|PubMed:17021831,
CC       ECO:0000269|PubMed:9671782}.
CC   -!- INDUCTION: By bitter compounds denatonium, quinine, strychnine,
CC       nicotine, atropine, quinacrine and caffeic acid in presence of taste
CC       membranes. {ECO:0000269|PubMed:9671782}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFC03016846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03016847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001103452.1; NM_001109982.1.
DR   PDB; 4A4M; X-ray; 3.30 A; B=344-354.
DR   PDB; 5EN0; X-ray; 2.81 A; B=344-354.
DR   PDBsum; 4A4M; -.
DR   PDBsum; 5EN0; -.
DR   AlphaFoldDB; P0C7Q4; -.
DR   SMR; P0C7Q4; -.
DR   STRING; 9913.ENSBTAP00000011395; -.
DR   PaxDb; 9913-ENSBTAP00000011395; -.
DR   Ensembl; ENSBTAT00000011395.6; ENSBTAP00000011395.6; ENSBTAG00000008641.6.
DR   GeneID; 516262; -.
DR   KEGG; bta:516262; -.
DR   CTD; 346562; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008641; -.
DR   VGNC; VGNC:29456; GNAT3.
DR   eggNOG; KOG0082; Eukaryota.
DR   GeneTree; ENSGT00940000161422; -.
DR   InParanoid; P0C7Q4; -.
DR   OMA; EDQRQLC; -.
DR   OrthoDB; 2897309at2759; -.
DR   Reactome; R-BTA-170670; Adenylate cyclase inhibitory pathway.
DR   Reactome; R-BTA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR   Reactome; R-BTA-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-BTA-418594; G alpha (i) signalling events.
DR   Reactome; R-BTA-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-BTA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000008641; Expressed in oocyte and 8 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0001917; C:photoreceptor inner segment; IBA:GO_Central.
DR   GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IBA:GO_Central.
DR   GO; GO:0050916; P:sensory perception of sweet taste; IBA:GO_Central.
DR   GO; GO:0050917; P:sensory perception of umami taste; IEA:Ensembl.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR10218:SF66; GUANINE NUCLEOTIDE-BINDING PROTEIN G(T) SUBUNIT ALPHA-3; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; GTP-binding; Lipoprotein; Magnesium;
KW   Metal-binding; Myristate; Nucleotide-binding; Reference proteome;
KW   Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..354
FT                   /note="Guanine nucleotide-binding protein G(t) subunit
FT                   alpha-3"
FT                   /id="PRO_0000342670"
FT   DOMAIN          32..354
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          35..48
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          173..181
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          196..205
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          265..272
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          324..329
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   COMPBIAS        10..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40..47
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         200..204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         269..272
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         352
FT                   /note="G->P: Loss of in vitro activation by denatonium due
FT                   to disruption of interaction with taste receptors."
FT                   /evidence="ECO:0000269|PubMed:9671782"
FT   HELIX           345..350
FT                   /evidence="ECO:0007829|PDB:5EN0"
SQ   SEQUENCE   354 AA;  40332 MW;  E5A707336B6941A9 CRC64;
     MGIGISSESK ESAKRSKELE KKLQEDAERD ARTVKLLLLG AGESGKSTIV KQMKIIHKNG
     YSEQECMEFK AVIYSNTLQS ILAIVKAMAT LEIDYVNPRS AEDQQQLCAM ANTLEDGSMT
     PELAEIIKRL WRDPGVQACF ERASEYQLND SAAYYLNDLD RIAAPGYVPN EQDVLHSRVK
     TTGIIETQFS FKDLHFRMFD VGGQRSERKK WIHCFEGVTC IIFCAALSAY DMVLVEDEEV
     NRMHESLHLF NSICNHKYFA TTSIVLFLNK KDLFQEKVTK VHLSICFPEY TGPNTFEDAG
     NYIKNQFLDL NLKKEDKEIY SHMTCATDTQ NVKFVFDAVT DIIIKENLKD CGLF
//
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