ID   GNAQ_MOUSE              Reviewed;         359 AA.
AC   P21279; Q6PFF5;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 4.
DT   27-MAR-2024, entry version 223.
DE   RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE   AltName: Full=Guanine nucleotide-binding protein alpha-q;
GN   Name=Gnaq;
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 [MRNA].
RC   TISSUE=Brain;
RX   PubMed=2123549; DOI=10.1073/pnas.87.23.9113;
RA   Strathmann M., Simon M.I.;
RT   "G protein diversity: a distinct class of alpha subunits is present in
RT   vertebrates and invertebrates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9113-9117(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-27; 61-73; 78-92; 121-133; 159-181; 184-210;
RP   283-300; 312-338 AND 346-354, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9296496; DOI=10.1038/38284;
RA   Offermanns S., Toombs C.F., Hu Y.H., Simon M.I.;
RT   "Defective platelet activation in G alpha(q)-deficient mice.";
RL   Nature 389:183-186(1997).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=9391157; DOI=10.1073/pnas.94.25.14089;
RA   Offermanns S., Hashimoto K., Watanabe M., Sun W., Kurihara H.,
RA   Thompson R.F., Inoue Y., Kano M., Simon M.I.;
RT   "Impaired motor coordination and persistent multiple climbing fiber
RT   innervation of cerebellar Purkinje cells in mice lacking Galphaq.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14089-14094(1997).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9687499; DOI=10.1093/emboj/17.15.4304;
RA   Offermanns S., Zhao L.P., Gohla A., Sarosi I., Simon M.I., Wilkie T.M.;
RT   "Embryonic cardiomyocyte hypoplasia and craniofacial defects in G alpha q/G
RT   alpha 11-mutant mice.";
RL   EMBO J. 17:4304-4312(1998).
RN   [7]
RP   PALMITOYLATION AT CYS-9 AND CYS-10, AND MUTAGENESIS OF CYS-9 AND CYS-10.
RC   TISSUE=Brain;
RX   PubMed=8227063; DOI=10.1016/s0021-9258(19)74563-3;
RA   Wedegaertner P.B., Chu D.H., Wilson P.T., Levis M.J., Bourne H.R.;
RT   "Palmitoylation is required for signaling functions and membrane attachment
RT   of Gq alpha and Gs alpha.";
RL   J. Biol. Chem. 268:25001-25008(1993).
RN   [8]
RP   FUNCTION.
RX   PubMed=17938235; DOI=10.1084/jem.20071267;
RA   Shi G., Partida-Sanchez S., Misra R.S., Tighe M., Borchers M.T., Lee J.J.,
RA   Simon M.I., Lund F.E.;
RT   "Identification of an alternative G{alpha}q-dependent chemokine receptor
RT   signal transduction pathway in dendritic cells and granulocytes.";
RL   J. Exp. Med. 204:2705-2718(2007).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18802028; DOI=10.1161/circresaha.108.176024;
RA   Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S.,
RA   O'Connell T.D.;
RT   "Nuclear alpha1-adrenergic receptors signal activated ERK localization to
RT   caveolae in adult cardiac myocytes.";
RL   Circ. Res. 103:992-1000(2008).
RN   [10]
RP   PALMITOYLATION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=19001095; DOI=10.1128/mcb.01144-08;
RA   Tsutsumi R., Fukata Y., Noritake J., Iwanaga T., Perez F., Fukata M.;
RT   "Identification of G protein alpha subunit-palmitoylating enzyme.";
RL   Mol. Cell. Biol. 29:435-447(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [12]
RP   FUNCTION.
RX   PubMed=20624888; DOI=10.1084/jem.20092735;
RA   Misra R.S., Shi G., Moreno-Garcia M.E., Thankappan A., Tighe M.,
RA   Mousseau B., Kusser K., Becker-Herman S., Hudkins K.L., Dunn R.,
RA   Kehry M.R., Migone T.S., Marshak-Rothstein A., Simon M., Randall T.D.,
RA   Alpers C.E., Liggitt D., Rawlings D.J., Lund F.E.;
RT   "G alpha q-containing G proteins regulate B cell selection and survival and
RT   are required to prevent B cell-dependent autoimmunity.";
RL   J. Exp. Med. 207:1775-1789(2010).
RN   [13]
RP   HISTAMINYLATION AT GLN-209.
RX   PubMed=23022564; DOI=10.1016/j.febslet.2012.09.027;
RA   Vowinckel J., Stahlberg S., Paulmann N., Bluemlein K., Grohmann M.,
RA   Ralser M., Walther D.J.;
RT   "Histaminylation of glutamine residues is a novel posttranslational
RT   modification implicated in G-protein signaling.";
RL   FEBS Lett. 586:3819-3824(2012).
RN   [14]
RP   INTERACTION WITH GAS2L2.
RX   PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA   Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT   "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT   of the A2A adenosine receptor.";
RL   Biochim. Biophys. Acta 1833:3145-3154(2013).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling systems
CC       (PubMed:9687499). Required for platelet activation (PubMed:9296496).
CC       Regulates B-cell selection and survival and is required to prevent B-
CC       cell-dependent autoimmunity (PubMed:20624888). Regulates chemotaxis of
CC       BM-derived neutrophils and dendritic cells (in vitro)
CC       (PubMed:17938235). Transduces FFAR4 signaling in response to long-chain
CC       fatty acids (LCFAs) (By similarity). Together with GNA11, required for
CC       heart development (PubMed:9687499). {ECO:0000250|UniProtKB:P50148,
CC       ECO:0000269|PubMed:17938235, ECO:0000269|PubMed:20624888,
CC       ECO:0000269|PubMed:9296496, ECO:0000269|PubMed:9687499}.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC       alpha chain contains the guanine nucleotide binding site. Binds NHERF1.
CC       Forms a complex with PECAM1 and BDKRB2. Interacts with PECAM1 (By
CC       similarity). Interacts with GAS2L2 (PubMed:23994616).
CC       {ECO:0000250|UniProtKB:P50148, ECO:0000269|PubMed:23994616}.
CC   -!- INTERACTION:
CC       P21279; O08915: Aip; NbExp=2; IntAct=EBI-771975, EBI-6935014;
CC       P21279; Q01970: PLCB3; Xeno; NbExp=6; IntAct=EBI-771975, EBI-4289548;
CC       P21279; P41220-1: RGS2; Xeno; NbExp=3; IntAct=EBI-771975, EBI-16037474;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19001095};
CC       Lipid-anchor {ECO:0000269|PubMed:19001095}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:P50148}. Nucleus {ECO:0000269|PubMed:18802028}.
CC       Nucleus membrane {ECO:0000269|PubMed:18802028}. Note=Colocalizes with
CC       the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane
CC       of cardiac myocytes. {ECO:0000269|PubMed:18802028}.
CC   -!- PTM: Palmitoylated by ZDHHC3 and ZDHHC7 (PubMed:19001095).
CC       Palmitoylation occurs in the Golgi and participates in the localization
CC       of GNAQ to the plasma membrane (PubMed:19001095).
CC       {ECO:0000269|PubMed:19001095}.
CC   -!- PTM: Histaminylated at Gln-209 residues by TGM2.
CC       {ECO:0000269|PubMed:23022564}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable but suffer from cerebellar ataxia
CC       and display deficiencies in primary hemostasis due to a defect in
CC       platelet activation (PubMed:9296496, PubMed:9391157). Mice lacking Gnaq
CC       and Gna11 are embryonic lethal due to cardiomyocyte hypoplasia
CC       (PubMed:9687499). Mice lacking Gnaq and with one single intact copy of
CC       Gna11, as well as mice lacking Gna11 and with one single intact copy of
CC       Gnaq die shortly after birth; lethality is caused by heart
CC       malformations (PubMed:9687499). Newborns display craniofacial defects
CC       (PubMed:9687499). {ECO:0000269|PubMed:9296496,
CC       ECO:0000269|PubMed:9391157, ECO:0000269|PubMed:9687499}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M55412; AAA63306.1; -; mRNA.
DR   EMBL; BC057583; AAH57583.1; -; mRNA.
DR   CCDS; CCDS29684.1; -.
DR   PIR; A38414; RGMSQ.
DR   RefSeq; NP_032165.3; NM_008139.5.
DR   PDB; 2BCJ; X-ray; 3.06 A; Q=37-359.
DR   PDB; 2RGN; X-ray; 3.50 A; A/D=37-359.
DR   PDB; 3AH8; X-ray; 2.90 A; A=37-359.
DR   PDB; 4EKC; X-ray; 7.40 A; A/C=18-359.
DR   PDB; 4EKD; X-ray; 2.71 A; A=18-359.
DR   PDB; 4GNK; X-ray; 4.00 A; A/C=7-359.
DR   PDB; 4QJ3; X-ray; 3.00 A; A=7-359.
DR   PDB; 4QJ4; X-ray; 3.30 A; A=7-359.
DR   PDB; 4QJ5; X-ray; 3.41 A; A=7-359.
DR   PDB; 5DO9; X-ray; 2.60 A; A/C/E=37-350.
DR   PDB; 7SQ2; X-ray; 2.60 A; A=35-359.
DR   PDBsum; 2BCJ; -.
DR   PDBsum; 2RGN; -.
DR   PDBsum; 3AH8; -.
DR   PDBsum; 4EKC; -.
DR   PDBsum; 4EKD; -.
DR   PDBsum; 4GNK; -.
DR   PDBsum; 4QJ3; -.
DR   PDBsum; 4QJ4; -.
DR   PDBsum; 4QJ5; -.
DR   PDBsum; 5DO9; -.
DR   PDBsum; 7SQ2; -.
DR   AlphaFoldDB; P21279; -.
DR   SMR; P21279; -.
DR   BioGRID; 199971; 22.
DR   CORUM; P21279; -.
DR   DIP; DIP-606N; -.
DR   IntAct; P21279; 14.
DR   MINT; P21279; -.
DR   STRING; 10090.ENSMUSP00000025541; -.
DR   GlyGen; P21279; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P21279; -.
DR   PhosphoSitePlus; P21279; -.
DR   SwissPalm; P21279; -.
DR   EPD; P21279; -.
DR   jPOST; P21279; -.
DR   PaxDb; 10090-ENSMUSP00000025541; -.
DR   PeptideAtlas; P21279; -.
DR   ProteomicsDB; 271023; -.
DR   Pumba; P21279; -.
DR   DNASU; 14682; -.
DR   Ensembl; ENSMUST00000025541.6; ENSMUSP00000025541.6; ENSMUSG00000024639.6.
DR   GeneID; 14682; -.
DR   KEGG; mmu:14682; -.
DR   UCSC; uc008gwt.1; mouse.
DR   AGR; MGI:95776; -.
DR   CTD; 2776; -.
DR   MGI; MGI:95776; Gnaq.
DR   VEuPathDB; HostDB:ENSMUSG00000024639; -.
DR   eggNOG; KOG0085; Eukaryota.
DR   GeneTree; ENSGT00940000162569; -.
DR   HOGENOM; CLU_014184_6_0_1; -.
DR   InParanoid; P21279; -.
DR   OMA; EHQSEFY; -.
DR   OrthoDB; 2897309at2759; -.
DR   PhylomeDB; P21279; -.
DR   TreeFam; TF300673; -.
DR   Reactome; R-MMU-112043; PLC beta mediated events.
DR   Reactome; R-MMU-202040; G-protein activation.
DR   Reactome; R-MMU-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-MMU-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   BioGRID-ORCS; 14682; 1 hit in 81 CRISPR screens.
DR   ChiTaRS; Gnaq; mouse.
DR   EvolutionaryTrace; P21279; -.
DR   PRO; PR:P21279; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P21279; Protein.
DR   Bgee; ENSMUSG00000024639; Expressed in ventromedial nucleus of hypothalamus and 227 other cell types or tissues.
DR   ExpressionAtlas; P21279; baseline and differential.
DR   GO; GO:0005901; C:caveola; ISO:MGI.
DR   GO; GO:0044297; C:cell body; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO:MGI.
DR   GO; GO:0030234; F:enzyme regulator activity; IMP:MGI.
DR   GO; GO:0003925; F:G protein activity; IMP: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; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0001508; P:action potential; IMP:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:1904888; P:cranial skeletal system development; IGI:MGI.
DR   GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; IGI:MGI.
DR   GO; GO:0021884; P:forebrain neuron development; IMP:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007215; P:glutamate receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; IGI:MGI.
DR   GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IMP:MGI.
DR   GO; GO:0042711; P:maternal behavior; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0043267; P:negative regulation of potassium ion transport; ISO:MGI.
DR   GO; GO:0016322; P:neuron remodeling; IMP:MGI.
DR   GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR   GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:MGI.
DR   GO; GO:0045634; P:regulation of melanocyte differentiation; IMP:MGI.
DR   GO; GO:0010543; P:regulation of platelet activation; IMP:UniProtKB.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
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; IPR000654; Gprotein_alpha_Q.
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:SF316; GUANINE NUCLEOTIDE-BINDING PROTEIN G(Q) SUBUNIT ALPHA; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00442; GPROTEINAQ.
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.
DR   Genevisible; P21279; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Direct protein sequencing; Golgi apparatus;
KW   GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Nucleus; Palmitate; Reference proteome; Transducer.
FT   CHAIN           1..359
FT                   /note="Guanine nucleotide-binding protein G(q) subunit
FT                   alpha"
FT                   /id="PRO_0000203761"
FT   DOMAIN          38..359
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          41..54
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          178..186
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          201..210
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          270..277
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          329..334
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         46..53
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P29992"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         180..183
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         274..277
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         331
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   MOD_RES         209
FT                   /note="5-glutamyl histamine"
FT                   /evidence="ECO:0000269|PubMed:23022564"
FT   LIPID           9
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:8227063"
FT   LIPID           10
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:8227063"
FT   MUTAGEN         9
FT                   /note="C->S: Abolishes palmitoylation."
FT                   /evidence="ECO:0000269|PubMed:8227063"
FT   MUTAGEN         10
FT                   /note="C->S: Abolishes palmitoylation."
FT                   /evidence="ECO:0000269|PubMed:8227063"
FT   CONFLICT        28..29
FT                   /note="QL -> HV (in Ref. 1; AAA63306)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="Missing (in Ref. 2; AAH57583)"
FT                   /evidence="ECO:0000305"
FT   STRAND          39..45
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   STRAND          47..51
FT                   /evidence="ECO:0007829|PDB:4QJ4"
FT   HELIX           52..63
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           69..73
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           76..96
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           105..114
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           139..146
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           147..150
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           157..161
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           164..168
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           176..181
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   STRAND          188..195
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   STRAND          197..206
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           210..213
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           214..219
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   STRAND          224..231
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           232..236
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           247..260
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           262..264
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   STRAND          267..274
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           276..282
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   TURN            283..285
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           288..290
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           302..314
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   STRAND          324..328
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   HELIX           334..346
FT                   /evidence="ECO:0007829|PDB:5DO9"
FT   TURN            347..349
FT                   /evidence="ECO:0007829|PDB:5DO9"
SQ   SEQUENCE   359 AA;  42158 MW;  3BCBA4EE7DADADBF CRC64;
     MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
     IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP YKYEHNKAHA QLVREVDVEK
     VSAFENPYVD AIKSLWNDPG IQECYDRRRE YQLSDSTKYY LNDLDRVADP SYLPTQQDVL
     RVRVPTTGII EYPFDLQSVI FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
     ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR
     DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
//