SCN3A_RAT
ID SCN3A_RAT Reviewed; 1951 AA.
AC P08104;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Sodium channel protein type 3 subunit alpha;
DE AltName: Full=Sodium channel protein brain III subunit alpha;
DE AltName: Full=Sodium channel protein type III subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subtype III;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.3;
GN Name=Scn3a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=2449363; DOI=10.1016/0014-5793(88)80614-8;
RA Kayano T., Noda M., Flockerzi V., Takahashi H., Numa S.;
RT "Primary structure of rat brain sodium channel III deduced from the cDNA
RT sequence.";
RL FEBS Lett. 228:187-194(1988).
RN [2]
RP INTERACTION WITH SCORPION TOXIN BMK M1, AND MUTAGENESIS OF GLU-1559.
RX PubMed=20678086; DOI=10.1042/bj20100517;
RA He H., Liu Z., Dong B., Zhou J., Zhu H., Ji Y.;
RT "Molecular determination of selectivity of the site 3 modulator (BmK I) to
RT sodium channels in the CNS: a clue to the importance of Nav1.6 in BmK I-
RT induced neuronal hyperexcitability.";
RL Biochem. J. 431:289-298(2010).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-485 AND SER-486, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP SUBUNIT, AND INTERACTION WITH THE CONOTOXIN GVIIJ.
RX PubMed=24497506; DOI=10.1073/pnas.1324189111;
RA Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
RA Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
RA Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G., Wickenden A.D.,
RA Olivera B.M., Yoshikami D., Zhang M.M.;
RT "A disulfide tether stabilizes the block of sodium channels by the
RT conotoxin muO[section sign]-GVIIJ.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
RN [5]
RP SUBUNIT, INTERACTION WITH THE SPIDER RTX-VII TOXIN, AND MUTAGENESIS OF
RP LYS-1503; TYR-1504; MET-1505; THR-1506; LEU-1507 AND GLU-1562.
RX PubMed=25784299; DOI=10.1038/srep09241;
RA Tang C., Zhou X., Zhang Y., Xiao Z., Hu Z., Zhang C., Huang Y., Chen B.,
RA Liu Z., Liang S.;
RT "Synergetic action of domain II and IV underlies persistent current
RT generation in Nav1.3 as revealed by a tarantula toxin.";
RL Sci. Rep. 5:9241-9241(2015).
RN [6]
RP SUBUNIT, INTERACTION WITH THE SPIDER BETA/DELTA-THERAPHOTOXIN-PRE1A, AND
RP SITE SER-1510.
RX PubMed=28428547; DOI=10.1038/s41598-017-01129-0;
RA Wingerd J.S., Mozar C.A., Ussing C.A., Murali S.S., Chin Y.K.,
RA Cristofori-Armstrong B., Durek T., Gilchrist J., Vaughan C.W., Bosmans F.,
RA Adams D.J., Lewis R.J., Alewood P.F., Mobli M., Christie M.J., Rash L.D.;
RT "The tarantula toxin beta/delta-TRTX-Pre1a highlights the importance of the
RT S1-S2 voltage-sensor region for sodium channel subtype selectivity.";
RL Sci. Rep. 7:974-988(2017).
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, forms a sodium-
CC selective channel through which Na(+) ions may pass in accordance with
CC their electrochemical gradient (By similarity). May contribute to the
CC regulation of serotonin/5-hydroxytryptamine release by enterochromaffin
CC cells (By similarity). In pancreatic endocrine cells, required for both
CC glucagon and glucose-induced insulin secretion (By similarity).
CC {ECO:0000250|UniProtKB:A2ASI5, ECO:0000250|UniProtKB:Q9NY46}.
CC -!- SUBUNIT: Heterooligomer of a large alpha subunit and 2-3 smaller beta
CC subunits. Heterooligomer with SCN2B or SCN4B; disulfide-linked.
CC Interacts with NEDD4L (By similarity). Interacts with the conotoxin
CC GVIIJ (PubMed:24497506). Interacts with the spider beta/delta-
CC theraphotoxin-Pre1a (PubMed:25784299, PubMed:28428547). Interacts with
CC the spider RTX-VII toxin (AC P0DL75) (PubMed:25784299).
CC {ECO:0000250|UniProtKB:Q9NY46, ECO:0000269|PubMed:24497506,
CC ECO:0000269|PubMed:25784299, ECO:0000269|PubMed:28428547}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NY46};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000305}.
CC -!- PTM: May be ubiquitinated by NEDD4L; which would promote its
CC endocytosis. {ECO:0000250|UniProtKB:Q9NY46}.
CC -!- PTM: Phosphorylation at Ser-1452 by PKC in a highly conserved
CC cytoplasmic loop slows inactivation of the sodium channel and reduces
CC peak sodium currents. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.3/SCN3A subfamily. {ECO:0000305}.
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DR EMBL; Y00766; CAA68735.1; -; mRNA.
DR PIR; S00320; S00320.
DR RefSeq; NP_037251.1; NM_013119.1.
DR PDB; 1QG9; NMR; -; A=156-176.
DR PDBsum; 1QG9; -.
DR AlphaFoldDB; P08104; -.
DR BMRB; P08104; -.
DR SMR; P08104; -.
DR BioGRID; 269080; 4.
DR STRING; 10116.ENSRNOP00000006646; -.
DR BindingDB; P08104; -.
DR ChEMBL; CHEMBL4966; -.
DR DrugCentral; P08104; -.
DR GuidetoPHARMACOLOGY; 580; -.
DR TCDB; 1.A.1.10.1; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P08104; 8 sites.
DR iPTMnet; P08104; -.
DR PhosphoSitePlus; P08104; -.
DR SwissPalm; P08104; -.
DR PaxDb; P08104; -.
DR PRIDE; P08104; -.
DR GeneID; 497770; -.
DR KEGG; rno:497770; -.
DR CTD; 6328; -.
DR RGD; 3635; Scn3a.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; P08104; -.
DR OrthoDB; 56920at2759; -.
DR PhylomeDB; P08104; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR EvolutionaryTrace; P08104; -.
DR PRO; PR:P08104; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR GO; GO:0031402; F:sodium ion binding; IDA:RGD.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
DR GO; GO:0071236; P:cellular response to antibiotic; IDA:RGD.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEP:RGD.
DR GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0046684; P:response to pyrethroid; IDA:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 2.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..1951
FT /note="Sodium channel protein type 3 subunit alpha"
FT /id="PRO_0000048494"
FT TOPO_DOM 1..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..147
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 148..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 176..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..207
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 208..213
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 214..230
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 231..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 250..269
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 270..368
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 369..393
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 394..400
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 401..421
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 422..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 712..730
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 731..741
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 742..761
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 762..775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 776..795
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 796..797
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 798..815
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 816..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 832..850
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 851..879
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 880..900
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 901..913
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 914..934
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 935..1158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1159..1176
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1177..1189
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1190..1208
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1209..1222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1223..1241
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1242..1249
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1250..1268
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1269..1285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1286..1305
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1306..1354
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1355..1376
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1377..1393
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1394..1415
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1416..1478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1479..1496
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1497..1507
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1508..1526
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1527..1538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1539..1556
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1557..1569
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1570..1586
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1587..1605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1606..1623
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1624..1645
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1646..1668
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1669..1698
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1699..1721
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1722..1951
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 110..455
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 693..965
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1139..1450
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1459..1757
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1851..1880
FT /note="IQ"
FT REGION 28..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1898..1951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1503
FT /note="Important residue that permits the spider RTX-VII
FT toxin to inhibit fast inactivation of the channel"
FT /evidence="ECO:0000269|PubMed:25784299"
FT SITE 1506
FT /note="Important residue that permits the spider RTX-VII
FT toxin to inhibit fast inactivation of the channel"
FT /evidence="ECO:0000269|PubMed:25784299"
FT SITE 1507
FT /note="Important residue that permits the spider RTX-VII
FT toxin to inhibit fast inactivation of the channel"
FT /evidence="ECO:0000269|PubMed:25784299"
FT SITE 1510
FT /note="Key residue that permits the spider beta/delta-
FT theraphotoxin-Pre1a to inhibit fast inactivation of the
FT channel"
FT /evidence="ECO:0000269|PubMed:28428547"
FT SITE 1562
FT /note="Important residue that permits the spider RTX-VII
FT toxin to inhibit fast inactivation of the channel"
FT /evidence="ECO:0000269|PubMed:25784299"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1452
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..346
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 862
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 862
FT /note="Interchain; with the conotoxin GVIIJ (when the
FT channel is not linked to SCN2B or SCN4B; the bond to SCN2B
FT or SCN4B protects the channel from the inhibition by
FT toxin)"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 902..911
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT MUTAGEN 1503
FT /note="K->P: 6-fold decrease in activity of the spider RTX-
FT VII toxin."
FT /evidence="ECO:0000269|PubMed:25784299"
FT MUTAGEN 1504
FT /note="Y->E: 2-fold decrease in activity of the spider RTX-
FT VII toxin."
FT /evidence="ECO:0000269|PubMed:25784299"
FT MUTAGEN 1505
FT /note="M->K: 4.5-fold decrease in activity of the spider
FT RTX-VII toxin."
FT /evidence="ECO:0000269|PubMed:25784299"
FT MUTAGEN 1506
FT /note="T->I: 10-fold decrease in activity of the spider
FT RTX-VII toxin."
FT /evidence="ECO:0000269|PubMed:25784299"
FT MUTAGEN 1507
FT /note="L->N: 12-fold decrease in activity of the spider
FT RTX-VII toxin."
FT /evidence="ECO:0000269|PubMed:25784299"
FT MUTAGEN 1559
FT /note="E->D: Increase in sensitivity to the scorpion toxin
FT BMK M1."
FT /evidence="ECO:0000269|PubMed:20678086"
FT MUTAGEN 1562
FT /note="E->Q: 5.5-fold decrease in activity of the spider
FT RTX-VII toxin."
FT /evidence="ECO:0000269|PubMed:25784299"
FT MUTAGEN 1562
FT /note="E->R: 20-fold decrease in activity of the spider
FT RTX-VII toxin."
FT /evidence="ECO:0000269|PubMed:25784299"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:1QG9"
SQ SEQUENCE 1951 AA; 221387 MW; 74E5E851524BD10E CRC64;
MAQALLVPPG PESFRLFTRE SLAAIEKRAA EEKAKKPKKE QDIDDENKPK PNSDLEAGKN
LPFIYGDIPP EMVSEPLEDL DPYYVSKKTF VVLNKGKAIF RFSATSALYI LTPLNPVRKI
AIKILVHSLF SMLIMCTILT NCVFMTLSNP PDWTKNVEYT FTGIYTFESL IKILARGFCL
EDFTFLRDPW NWLDFSVIVM AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCSQW PPSDSAFETN TTSYFNGTMD
SNGTFVNVTM STFNWKDYIA DDSHFYVLDG QKDPLLCGNG SDAGQCPEGY ICVKAGRNPN
YGYTSFDTFS WAFLSLFRLM TQDYWENLYQ LTLRAAGKTY MIFFVLVIFL GSFYLVNLIL
AVVAMAYEEQ NQATLEEAEQ KEAEFQQMLE QLKKQQEEAQ AVAAASAASR DFSGIGGLGE
LLESSSEASK LSSKSAKEWR NRRKKRRQRE HLEGNHRADG DRFPKSESED SVKRRSFLLS
LDGNPLTGDK KLCSPHQSLL SIRGSLFSPR RNSKTSIFSF RGRAKDVGSE NDFADDEHST
FEDSESRRDS LFVPHRPGER RNSNGTTTET EVRKRRLSSY QISMEMLEDS SGRQRSMSIA
SILTNTMEEL EESRQKCPPC WYRFANVFLI WDCCDAWLKV KHLVNLIVMD PFVDLAITIC
IVLNTLFMAM EHYPMTQQFS SVLTVGNLVF TGIFTAEMVL KIIAMDPYYY FQEGWNIFDG
IIVSLSLMEL GLANVEGLSV LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL
AIIVFIFAVV GMQLFGKSYK ECVCKINVDC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW
DCMEVAGQTM CLIVFMLVMV IGNLVVLNLF LALLLSSFSS DNLAATDDDN EMNNLQIAVG
RMQKGIDFVK NKIRECFRKA FFRKPKVIEI QEGNKIDSCM SNNTGIEISK ELNYLKDGNG
TTSGVGTGSS VEKYVIDEND YMSFINNPSL TVTVPIAVGE SDFENLNTEE FSSESELEES
KEKLNATSSS EGSTVDVAPP REGEQAEIEP EEDLKPEACF TEGCIKKFPF CQVSTEEGKG
KIWWNLRKTC YSIVEHNWFE TFIVFMILLS SGALAFEDIY IEQRKTIKTM LEYADKVFTY
IFILEMLLKW VAYGFQTYFT NAWCWLDFLI VDVSLVSLVA NALGYSELGA IKSLRTLRAL
RPLRALSRFE GMRVVVNALV GAIPSIMNVL LVCLIFWLIF SIMGVNLFAG KFYHCVNTTT
GNMFEIKEVN NFSDCQALGK QARWKNVKVN FDNVGAGYLA LLQVATFKGW MDIMYAAVDS
RDVKLQPIYE ENLYMYLYFV IFIIFGSFFT LNLFIGVIID NFNQQKKKFG GQDIFMTEEQ
KKYYNAMKKL GSKKPQKPIP RPANKFQGMV FDFVTRQVFD ISIMILICLN MVTMMVETDD
QSKYMTLVLS RINLVFIVLF TGEFLLKLIS LRYYYFTIGW NIFDFVVVIL SIVGMFLAEL
IEKYFVSPTL FRVIRLARIG RILRLIKGAK GIRTLLFALM MSLPALFNIG LLLFLVMFIY
AIFGMSNFAY VKKEAGIDDM FNFETFGNSM ICLFQITTSA GWDGLLAPIL NSAPPDCDPD
AIHPGSSVKG DCGNPSVGIF FFVSYIIISF LVVVNMYIAV ILENFSVATE ESAEPLSEDD
FEMFYEVWEK FDPDATQFIE FCKLSDFAAA LDPPLLIAKP NKVQLIAMDL PMVSGDRIHC
LDILFAFTKR VLGESGEMDA LRIQMEDRFM ASNPSKVSYE PITTTLKRKQ EEVSAAIIQR
NYRCYLLKQR LKNISSKYDK ETIKGRIDLP IKGDMVIDKL NGNSTPEKTD GSSSTTSPPS
YDSVTKPDKE KFEKDKPEKE IKGKEVRENQ K
