GLUCL_DROME
ID GLUCL_DROME Reviewed; 456 AA.
AC Q94900; O77295; Q0Q0M3; Q2PDQ5; Q59DV9; Q8IN68; Q9GQ52; Q9GQ53; Q9VDU5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Glutamate-gated chloride channel;
DE Short=DrosGluCl;
DE Flags: Precursor;
GN Name=GluClalpha; Synonyms=GluCl {ECO:0000312|EMBL:AAC47266.1};
GN ORFNames=CG7535;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC47266.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), FUNCTION, ACTIVITY REGULATION,
RP SUBUNIT, DEVELOPMENTAL STAGE, AND RNA EDITING OF POSITIONS 27; 241 AND 345.
RC STRAIN=Oregon-R {ECO:0000312|EMBL:AAC47266.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAC47266.1};
RX PubMed=8702744; DOI=10.1074/jbc.271.33.20187;
RA Cully D.F., Paress P.S., Liu K.K., Schaeffer J.M., Arena J.P.;
RT "Identification of a Drosophila melanogaster glutamate-gated chloride
RT channel sensitive to the antiparasitic agent avermectin.";
RL J. Biol. Chem. 271:20187-20191(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA05260.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT SER-299, AND RNA EDITING OF
RP POSITIONS 27; 63; 66 AND 241.
RC TISSUE=Head {ECO:0000269|PubMed:9886055};
RX PubMed=9886055; DOI=10.1046/j.1471-4159.1999.0720066.x;
RA Semenov E.P., Pak W.L.;
RT "Diversification of Drosophila chloride channel gene by multiple
RT posttranscriptional mRNA modifications.";
RL J. Neurochem. 72:66-72(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAG40735.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), NUCLEOTIDE SEQUENCE [MRNA] OF 1-336
RP (ISOFORM B), FUNCTION, ACTIVITY REGULATION, VARIANT SER-299, AND RNA
RP EDITING OF POSITIONS 27; 63; 66; 241 AND 345.
RX PubMed=11095718; DOI=10.1073/pnas.240464697;
RA Kane N.S., Hirschberg B., Qian S., Hunt D., Thomas B., Brochu R.,
RA Ludmerer S.W., Zheng Y., Smith M., Arena J.P., Cohen C.J., Schmatz D.,
RA Warmke J., Cully D.F.;
RT "Drug-resistant Drosophila indicate glutamate-gated chloride channels are
RT targets for the antiparasitics nodulisporic acid and ivermectin.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13949-13954(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), AND RNA EDITING OF POSITIONS 27;
RP 63; 66; 241 AND 345.
RA Wang X., Xiang W., Wang X., Jiang L., Lin S., Gao A., Wang L., Sun L.,
RA Jing B., Xi D.;
RT "Cloning and functional expression of a Drosophila melanogaster glutamate-
RT gated chloride channel.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAF55695.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING OF POSITION
RP 63; 66 AND 345.
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAF55695.1}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7] {ECO:0000305}
RP RNA EDITING OF POSITIONS 27; 63; 66; 241 AND 345.
RX PubMed=10966106; DOI=10.1016/s0092-8674(00)00049-0;
RA Palladino M.J., Keegan L.P., O'Connell M.A., Reenan R.A.;
RT "A-to-I pre-mRNA editing in Drosophila is primarily involved in adult
RT nervous system function and integrity.";
RL Cell 102:437-449(2000).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF SER-278.
RX PubMed=31535971; DOI=10.7554/elife.49373;
RA Molina-Obando S., Vargas-Fique J.F., Henning M., Guer B., Schladt T.M.,
RA Akhtar J., Berger T.K., Silies M.;
RT "ON selectivity in the Drosophila visual system is a multisynaptic process
RT involving both glutamatergic and GABAergic inhibition.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Glutamate-gated chloride channel subunit (PubMed:11095718,
CC PubMed:8702744). Together with Gamma-aminobutyric acid receptor Rdl,
CC plays an important role in the visual response by regulating the
CC activity of ON/OFF-selective neurons (PubMed:31535971).
CC {ECO:0000269|PubMed:11095718, ECO:0000269|PubMed:31535971,
CC ECO:0000269|PubMed:8702744}.
CC -!- ACTIVITY REGULATION: Glutamate binding triggers a rapidly reversible
CC current, while the anti-helmintic drug ivermectin triggers a
CC permanently open channel configuration (PubMed:8702744,
CC PubMed:11095718). Inhibited by picrotoxin (PubMed:31535971).
CC {ECO:0000269|PubMed:11095718, ECO:0000269|PubMed:31535971,
CC ECO:0000269|PubMed:8702744}.
CC -!- SUBUNIT: Pentamer (By similarity). Homomultimer.
CC {ECO:0000250|UniProtKB:G5EBR3, ECO:0000269|PubMed:8702744}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=F;
CC IsoId=Q94900-1; Sequence=Displayed;
CC Name=A {ECO:0000303|PubMed:10731132};
CC IsoId=Q94900-3; Sequence=VSP_051645;
CC Name=B {ECO:0000269|PubMed:9886055};
CC IsoId=Q94900-2; Sequence=VSP_051644, VSP_051646, VSP_051647;
CC Name=C;
CC IsoId=Q94900-4; Sequence=VSP_026113, VSP_051646, VSP_051647;
CC Name=D;
CC IsoId=Q94900-5; Sequence=VSP_051644, VSP_026114, VSP_051647;
CC -!- TISSUE SPECIFICITY: Expressed in the medulla layers (at protein level)
CC (PubMed:31535971). Expressed in all major ON pathway medulla neurons
CC (Mi1, Tm3, Mi4, and Mi9) and in OFF pathway neurons (Tm1, Tm2, Tm4, and
CC Tm9) (PubMed:31535971). {ECO:0000269|PubMed:31535971}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:8702744}.
CC -!- RNA EDITING: Modified_positions=27 {ECO:0000269|PubMed:10966106,
CC ECO:0000269|PubMed:11095718, ECO:0000269|PubMed:8702744,
CC ECO:0000269|PubMed:9886055, ECO:0000269|Ref.4}, 63
CC {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:10966106,
CC ECO:0000269|PubMed:11095718, ECO:0000269|PubMed:9886055,
CC ECO:0000269|Ref.4}, 66 {ECO:0000269|PubMed:10731132,
CC ECO:0000269|PubMed:10966106, ECO:0000269|PubMed:11095718,
CC ECO:0000269|PubMed:9886055, ECO:0000269|Ref.4}, 241
CC {ECO:0000269|PubMed:10966106, ECO:0000269|PubMed:11095718,
CC ECO:0000269|PubMed:8702744, ECO:0000269|PubMed:9886055,
CC ECO:0000269|Ref.4}, 345 {ECO:0000269|PubMed:10731132,
CC ECO:0000269|PubMed:10966106, ECO:0000269|PubMed:11095718,
CC ECO:0000269|PubMed:8702744, ECO:0000269|Ref.4}; Note=Partially edited.
CC Edited by Adar. {ECO:0000269|PubMed:10966106,
CC ECO:0000269|PubMed:9886055};
CC -!- DISRUPTION PHENOTYPE: Viable but with locomotor deficits
CC (PubMed:31535971). Results in loss of light response in all neuronal
CC layers part of the ON visual system (PubMed:31535971). In Mi1 neurons,
CC does not affect function of the ON visual response (PubMed:31535971).
CC RNAi-mediated knockdown in Mi1 or Tm3 neurons, does not affect function
CC of the ON visual response (PubMed:31535971).
CC {ECO:0000269|PubMed:31535971}.
CC -!- MISCELLANEOUS: Channels desensitize rapidly in the continued presence
CC of glutamate and are activated by the glutamate analog ibotenate. In
CC Xenopus oocytes, avermectins and nodulisporic acid directly activate
CC channel conductance. {ECO:0000269|PubMed:11095718,
CC ECO:0000269|PubMed:8702744}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Glutamate-gated chloride channel (TC 1.A.9.4) subfamily. {ECO:0000305}.
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DR EMBL; U58776; AAC47266.1; -; mRNA.
DR EMBL; AJ002232; CAA05260.1; -; mRNA.
DR EMBL; AF297500; AAG40735.1; -; mRNA.
DR EMBL; AF297501; AAG40736.1; -; mRNA.
DR EMBL; DQ665648; ABG57261.1; -; mRNA.
DR EMBL; AE014297; AAF55695.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13808.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52967.1; -; Genomic_DNA.
DR EMBL; AE014297; ABC66182.1; -; Genomic_DNA.
DR RefSeq; NP_001014641.2; NM_001014641.4.
DR RefSeq; NP_001034061.2; NM_001038972.4.
DR RefSeq; NP_650827.3; NM_142570.4.
DR RefSeq; NP_732447.2; NM_169873.4.
DR AlphaFoldDB; Q94900; -.
DR SMR; Q94900; -.
DR BioGRID; 67340; 2.
DR STRING; 7227.FBpp0099473; -.
DR TCDB; 1.A.9.4.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR PaxDb; Q94900; -.
DR DNASU; 42350; -.
DR GeneID; 42350; -.
DR KEGG; dme:Dmel_CG7535; -.
DR UCSC; CG7535-RA; d. melanogaster. [Q94900-1]
DR CTD; 42350; -.
DR FlyBase; FBgn0024963; GluClalpha.
DR VEuPathDB; VectorBase:FBgn0024963; -.
DR eggNOG; KOG3644; Eukaryota.
DR InParanoid; Q94900; -.
DR PhylomeDB; Q94900; -.
DR Reactome; R-DME-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR BioGRID-ORCS; 42350; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42350; -.
DR PRO; PR:Q94900; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR ExpressionAtlas; Q94900; baseline and differential.
DR Genevisible; Q94900; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0008068; F:extracellularly glutamate-gated chloride channel activity; IDA:FlyBase.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd19062; LGIC_TM_GluCl; 1.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR015680; Glu_Cl_Channel.
DR InterPro; IPR044721; GluCl_TM.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR PANTHER; PTHR18945:SF754; PTHR18945:SF754; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Chloride; Chloride channel;
KW Disulfide bond; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Postsynaptic cell membrane; Receptor; Reference proteome;
KW RNA editing; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..456
FT /note="Glutamate-gated chloride channel"
FT /evidence="ECO:0000255"
FT /id="PRO_0000000497"
FT TOPO_DOM 23..245
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 246..268
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 269..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 274..295
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 296..302
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 303..323
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 324..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 427..450
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 451..456
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 71
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 90
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 154
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 183
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT DISULFID 163..177
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT DISULFID 222..233
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT VAR_SEQ 60..79
FT /note="GPAIVRINLFVRSIMTISDI -> NKATNVSVNMFLRSISKIDDY (in
FT isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_026113"
FT VAR_SEQ 68..80
FT /note="LFVRSIMTISDIK -> IFVRSISKIDDVT (in isoform B and
FT isoform D)"
FT /evidence="ECO:0000303|PubMed:11095718,
FT ECO:0000303|PubMed:9886055, ECO:0000303|Ref.4"
FT /id="VSP_051644"
FT VAR_SEQ 230..232
FT /note="EYS -> T (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_051645"
FT VAR_SEQ 335..341
FT /note="GSNKANM -> DV (in isoform D)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_026114"
FT VAR_SEQ 417..420
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:11095718,
FT ECO:0000303|PubMed:9886055"
FT /id="VSP_051646"
FT VAR_SEQ 456
FT /note="E -> ETF (in isoform B, isoform C and isoform D)"
FT /evidence="ECO:0000303|PubMed:11095718,
FT ECO:0000303|PubMed:9886055, ECO:0000303|Ref.4"
FT /id="VSP_051647"
FT VARIANT 27
FT /note="I -> V (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:10966106,
FT ECO:0000269|PubMed:9886055"
FT VARIANT 63
FT /note="I -> V (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:10966106"
FT VARIANT 66
FT /note="I -> V (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:10966106"
FT VARIANT 241
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:10966106,
FT ECO:0000269|PubMed:9886055"
FT VARIANT 299
FT /note="P -> S (resistant to nodulisporic acid)"
FT /evidence="ECO:0000269|PubMed:11095718,
FT ECO:0000269|PubMed:9886055"
FT VARIANT 345
FT /note="S -> N (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:10966106,
FT ECO:0000269|PubMed:9886055"
FT MUTAGEN 278
FT /note="S->T: Shows resistance to picrotoxin-induced
FT activity inhibition."
FT /evidence="ECO:0000269|PubMed:31535971"
FT CONFLICT 50
FT /note="I -> V (in Ref. 4; ABG57261)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="P -> S (in Ref. 3; AAG40736)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="V -> A (in Ref. 4; ABG57261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 52307 MW; AE892B338B79A060 CRC64;
MGSGHYFWAI LYFASLCSAS LANNAKINFR EKEKKVLDQI LGAGKYDARI RPSGINGTDG
PAIVRINLFV RSIMTISDIK MEYSVQLTFR EQWTDERLKF DDIQGRLKYL TLTEANRVWM
PDLFFSNEKE GHFHNIIMPN VYIRIFPNGS VLYSIRISLT LACPMNLKLY PLDRQICSLR
MASYGWTTND LVFLWKEGDP VQVVKNLHLP RFTLEKFLTD YCNSKTNTGE YSCLKVDLLF
KREFSYYLIQ IYIPCCMLVI VSWVSFWLDQ GAVPARVSLG VTTLLTMATQ TSGINASLPP
VSYTKAIDVW TGVCLTFVFG ALLEFALVNY ASRSGSNKAN MHKESMKKKR RDLEQASLDA
ASDLLDTDSN ATFAMKPLVR HPGDPLALEK RLQCEVHMQA PKRPNCCKTW LSKFPTRQCS
RSKRIDVISR ITFPLVFALF NLVYWSTYLF REEEDE
