GNAT3_MOUSE
ID GNAT3_MOUSE Reviewed; 354 AA.
AC Q3V3I2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-3;
DE AltName: Full=Gustducin alpha-3 chain;
GN Name=Gnat3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-310.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=8657284; DOI=10.1038/381796a0;
RA Wong G.T., Gannon K.S., Margolskee R.F.;
RT "Transduction of bitter and sweet taste by gustducin.";
RL Nature 381:796-800(1996).
RN [4]
RP DISRUPTION PHENOTYPE, AND TRANSGENE.
RX PubMed=10407021; DOI=10.1523/jneurosci.19-14-05802.1999;
RA Wong G.T., Ruiz-Avila L., Margolskee R.F.;
RT "Directing gene expression to gustducin-positive taste receptor cells.";
RL J. Neurosci. 19:5802-5809(1999).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10570481; DOI=10.1038/15981;
RA Huang L., Shanker Y.G., Dubauskaite J., Zheng J.Z., Yan W., Rosenzweig S.,
RA Spielman A.I., Max M., Margolskee R.F.;
RT "Ggamma13 colocalizes with gustducin in taste receptor cells and mediates
RT IP3 responses to bitter denatonium.";
RL Nat. Neurosci. 2:1055-1062(1999).
RN [6]
RP FUNCTION.
RX PubMed=11245589; DOI=10.1152/ajpcell.2001.280.4.c742;
RA Yan W., Sunavala G., Rosenzweig S., Dasso M., Brand J.G., Spielman A.I.;
RT "Bitter taste transduced by PLC-beta(2)-dependent rise in IP(3) and alpha-
RT gustducin-dependent fall in cyclic nucleotides.";
RL Am. J. Physiol. 280:C742-C751(2001).
RN [7]
RP DISRUPTION PHENOTYPE, AND TRANSGENE.
RX PubMed=11447270; DOI=10.1073/pnas.151235798;
RA Ruiz-Avila L., Wong G.T., Damak S., Margolskee R.F.;
RT "Dominant loss of responsiveness to sweet and bitter compounds caused by a
RT single mutation in alpha-gustducin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8868-8873(2001).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=14637165; DOI=10.1016/j.bbrc.2003.10.137;
RA Kim M.-R., Kusakabe Y., Miura H., Shindo Y., Ninomiya Y., Hino A.;
RT "Regional expression patterns of taste receptors and gustducin in the mouse
RT tongue.";
RL Biochem. Biophys. Res. Commun. 312:500-506(2003).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=14586025; DOI=10.1523/jneurosci.23-30-09947.2003;
RA Caicedo A., Pereira E., Margolskee R.F., Roper S.D.;
RT "Role of the G-protein subunit alpha-gustducin in taste cell responses to
RT bitter stimuli.";
RL J. Neurosci. 23:9947-9952(2003).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=14627646; DOI=10.1523/jneurosci.23-33-10613.2003;
RA Grillet N., Dubreuil V., Dufour H.D., Brunet J.-F.;
RT "Dynamic expression of RGS4 in the developing nervous system and regulation
RT by the neural type-specific transcription factor Phox2b.";
RL J. Neurosci. 23:10613-10621(2003).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=15342734; DOI=10.1523/jneurosci.2441-04.2004;
RA He W., Yasumatsu K., Varadarajan V., Yamada A., Lem J., Ninomiya Y.,
RA Margolskee R.F., Damak S.;
RT "Umami taste responses are mediated by alpha-transducin and alpha-
RT gustducin.";
RL J. Neurosci. 24:7674-7680(2004).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=16933139; DOI=10.1007/s00429-006-0112-2;
RA Zhang G.-H., Deng S.-P., Li L.-L., Li H.-T.;
RT "Developmental change of alpha-gustducin expression in the mouse fungiform
RT papilla.";
RL Anat. Embryol. (Berl.) 211:625-630(2006).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=16740645; DOI=10.1093/chemse/bjj062;
RA Danilova V., Damak S., Margolskee R.F., Hellekant G.;
RT "Taste responses to sweet stimuli in alpha-gustducin knockout and wild-type
RT mice.";
RL Chem. Senses 31:573-580(2006).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=17290008; DOI=10.1152/ajpgi.00504.2006;
RA Sutherland K., Young R.L., Cooper N.J., Horowitz M., Blackshaw L.A.;
RT "Phenotypic characterization of taste cells of the mouse small intestine.";
RL Am. J. Physiol. 292:G1420-G1428(2007).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=17229761; DOI=10.1093/chemse/bjl053;
RA Stone L.M., Barrows J., Finger T.E., Kinnamon S.C.;
RT "Expression of T1Rs and gustducin in palatal taste buds of mice.";
RL Chem. Senses 32:255-262(2007).
RN [16]
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).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17724330; DOI=10.1073/pnas.0706890104;
RA Jang H.-J., Kokrashvili Z., Theodorakis M.J., Carlson O.D., Kim B.-J.,
RA Zhou J., Kim H.H., Xu X., Chan S.L., Juhaszova M., Bernier M., Mosinger B.,
RA Margolskee R.F., Egan J.M.;
RT "Gut-expressed gustducin and taste receptors regulate secretion of
RT glucagon-like peptide-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15069-15074(2007).
RN [18]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17724332; DOI=10.1073/pnas.0706678104;
RA Margolskee R.F., Dyer J., Kokrashvili Z., Salmon K.S., Ilegems E., Daly K.,
RA Maillet E.L., Ninomiya Y., Mosinger B., Shirazi-Beechey S.P.;
RT "T1R3 and gustducin in gut sense sugars to regulate expression of Na+-
RT glucose cotransporter 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15075-15080(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. Transduction by this alpha subunit
CC involves coupling of specific cell-surface receptors with a cGMP-
CC phosphodiesterase; Activation of phosphodiesterase lowers intracellular
CC levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible
CC cation channel leading to influx of calcium, ultimately leading to
CC release of neurotransmitter. Indeed, denatonium and strychnine induce
CC transient reduction in cAMP and cGMP in taste tissue, whereas this
CC decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer
CC transduces response to bitter and sweet compounds via regulation of
CC phosphodiesterase for alpha subunit, as well as via activation of
CC phospholipase C for beta and gamma subunits, with ultimate increase
CC inositol trisphosphate and increase of intracellular Calcium. GNAT3 can
CC functionally couple to taste receptors to transmit intracellular
CC signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and
CC TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act
CC as bitter sensors. Functions also as lumenal sugar sensors in the gut
CC to control the expression of the Na+-glucose transporter SGLT1 in
CC response to dietaty sugar, as well as the secretion of Glucagon-like
CC peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP.
CC Thus, may modulate the gut capacity to absorb sugars, with implications
CC in malabsorption syndromes and diet-related disorders including
CC diabetes and obesity. {ECO:0000269|PubMed:10570481,
CC ECO:0000269|PubMed:11245589, ECO:0000269|PubMed:17724330,
CC ECO:0000269|PubMed:17724332}.
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. {ECO:0000269|PubMed:10570481}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in taste buds (sensory organs of
CC clustered epithelial cells) of the circumvallate and fungiform papillae
CC of the tongue as well as in palatal taste buds at protein level.
CC Expressed in enteroendocrine cells of the gut, such as in subsets of
CC enteroendocrine cells in the midjejunum and brush cells. Detected also
CC in spermatozoa. {ECO:0000269|PubMed:14637165,
CC ECO:0000269|PubMed:17021831, ECO:0000269|PubMed:17229761,
CC ECO:0000269|PubMed:17290008, ECO:0000269|PubMed:17724332}.
CC -!- DEVELOPMENTAL STAGE: From week 1 to 7, the number of cells expressing
CC GNAT3 in single taste buds increases within fungiform papilla; by week
CC 7, the number reached the value found in adults. Expressed in cell
CC bodies and axons of facial motor neurons at 10.5 dpc.
CC {ECO:0000269|PubMed:14627646, ECO:0000269|PubMed:16933139}.
CC -!- PTM: Potential N-myristoylation may anchor alpha-subunit to the inner
CC surface of plasma membrane. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are not affected in their tasting ability
CC for salty (NaCl) and sour (HCl) stimuli, which are known not to be
CC mediated by G proteins; but, they exhibit a significant reduction in
CC the ability to taste the bitter compounds denatonium and quinine as
CC well as the sweet compounds sucrose and SC45647, a guanidine sweetener.
CC The incidence of cells responding to bitter stimulus is also reduced by
CC seventy per cent. The residual behavioral response to bitter and sweet
CC taste in these deficient mice suggests that there is alternative
CC mechanism to compensate. However, transgenic expression of Gnat3 in
CC these deficient mice restores responsiveness to both bitter and sweet
CC compounds, whereas expression of mutated 'Gly-352' transgene do not.
CC Furthermore, in wild-type mice, this mutated transgene acts as
CC dominant-negative by inhibition of endogenous Gnat3 interactions with
CC taste receptors. Mice show less preference for acesulfame-K, dulcin,
CC fructose, D-phenylalanine, L-proline, D-tryptophan, saccharin,
CC sweetener SC45647 and sucrose; Furthermore, in their gut, sugar or
CC sweeteners do not increase SGLT1 expression and glucose-absorptive
CC capacity compared to wild-type mice and the ingestion of glucose
CC reveals deficiencies in secretion of GLP-1 and regulation of plasma
CC insulin and glucose. Mice lacking GNAT3 show less preference for umami
CC compounds such as monosodium glutamate (MSG) and no preference for
CC inosine monophosphate (IMP) whereas wild-type mice strongly prefer IMP.
CC The response to umami signals implicates the anteriorly placed taste
CC buds of the tongue, and not the posterior part.
CC {ECO:0000269|PubMed:10407021, ECO:0000269|PubMed:11447270,
CC ECO:0000269|PubMed:14586025, ECO:0000269|PubMed:15342734,
CC ECO:0000269|PubMed:16740645, ECO:0000269|PubMed:17724330,
CC ECO:0000269|PubMed:17724332, ECO:0000269|PubMed:8657284}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {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; AC129572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK040065; BAE20568.1; -; mRNA.
DR CCDS; CCDS39017.1; -.
DR RefSeq; NP_001074612.1; NM_001081143.1.
DR AlphaFoldDB; Q3V3I2; -.
DR SMR; Q3V3I2; -.
DR BioGRID; 232466; 2.
DR STRING; 10090.ENSMUSP00000030561; -.
DR iPTMnet; Q3V3I2; -.
DR PhosphoSitePlus; Q3V3I2; -.
DR jPOST; Q3V3I2; -.
DR MaxQB; Q3V3I2; -.
DR PaxDb; Q3V3I2; -.
DR PRIDE; Q3V3I2; -.
DR ProteomicsDB; 263381; -.
DR Antibodypedia; 29521; 153 antibodies from 28 providers.
DR Ensembl; ENSMUST00000030561; ENSMUSP00000030561; ENSMUSG00000028777.
DR GeneID; 242851; -.
DR KEGG; mmu:242851; -.
DR UCSC; uc008wnr.1; mouse.
DR CTD; 346562; -.
DR MGI; MGI:3588268; Gnat3.
DR VEuPathDB; HostDB:ENSMUSG00000028777; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000161422; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q3V3I2; -.
DR OMA; EDQRQLC; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q3V3I2; -.
DR TreeFam; TF300673; -.
DR Reactome; R-MMU-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-MMU-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-MMU-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR BioGRID-ORCS; 242851; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q3V3I2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3V3I2; protein.
DR Bgee; ENSMUSG00000028777; Expressed in mucosa of large intestine and 22 other tissues.
DR ExpressionAtlas; Q3V3I2; baseline and differential.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IPI:MGI.
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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
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:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0050913; P:sensory perception of bitter taste; IMP:MGI.
DR GO; GO:0050916; P:sensory perception of sweet taste; IMP:MGI.
DR GO; GO:0050909; P:sensory perception of taste; IDA:MGI.
DR GO; GO:0050917; P:sensory perception of umami taste; IMP:MGI.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Reference proteome; 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_0000342672"
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"
SQ SEQUENCE 354 AA; 40316 MW; 05DBC95DAC356CEF CRC64;
MGSGISSESK ESARRSKELE KKLQEDAERD ARTVKLLLLG AGESGKSTIV KQMKIIHKNG
YSKQECMEFK AVIYSNTLQS ILAIVKAMAT LGIDYVNPRS REDQEQLHSM ANTLEDGDMT
PQLAEIIKRL WGDPGIQACF ERASEYQLND SAAYYLNDLD RLTAPGYVPN EQDVLHSRVK
TTGIIETQFS FKDLNFRMFD VGGQRSERKK WIHCFEGVTC IIFCAALSAY DMVLVEDEEV
NRMHESLHLF NSICNHKYFA TTSIVLFLNK KDLFQEKVAK VHLSICFPEY TGPNTFEDAG
NYIKNQFLDL NLKKEDKEIY SHMTCATDTQ NVKFVFDAVT DIIIKENLKD CGLF
