GNAQ_MOUSE
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 03-AUG-2022, entry version 215.
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, Pancreas,
RC 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
CC SLC9A3R1. Forms a complex with PECAM1 and BDKRB2. Interacts with PECAM1
CC (By 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; 13.
DR MINT; P21279; -.
DR STRING; 10090.ENSMUSP00000025541; -.
DR iPTMnet; P21279; -.
DR PhosphoSitePlus; P21279; -.
DR SwissPalm; P21279; -.
DR EPD; P21279; -.
DR jPOST; P21279; -.
DR PaxDb; P21279; -.
DR PeptideAtlas; P21279; -.
DR PRIDE; P21279; -.
DR ProteomicsDB; 271023; -.
DR DNASU; 14682; -.
DR Ensembl; ENSMUST00000025541; ENSMUSP00000025541; ENSMUSG00000024639.
DR GeneID; 14682; -.
DR KEGG; mmu:14682; -.
DR UCSC; uc008gwt.1; mouse.
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; AVTYLWN; -.
DR OrthoDB; 754573at2759; -.
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 76 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 224 other tissues.
DR ExpressionAtlas; P21279; baseline and differential.
DR Genevisible; P21279; MM.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO: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; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; 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; 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:0007202; P:activation of phospholipase C activity; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:0042711; P:maternal behavior; IMP:MGI.
DR GO; GO:0010259; P:multicellular organism aging; 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:0006469; P:negative regulation of protein kinase activity; 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:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO: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; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00442; GPROTEINAQ.
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 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
