SCNA1_PERAM
ID SCNA1_PERAM Reviewed; 1553 AA.
AC D0E0C2;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Sodium channel protein PaFPC1 {ECO:0000303|PubMed:19800971};
DE Short=PaFPC1 {ECO:0000303|PubMed:19800971};
DE AltName: Full=NavPaS {ECO:0000303|PubMed:28183995};
OS Periplaneta americana (American cockroach) (Blatta americana).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Blattidae;
OC Blattinae; Periplaneta.
OX NCBI_TaxID=6978 {ECO:0000312|EMBL:ACX44802.1};
RN [1] {ECO:0000312|EMBL:ACX44802.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Nerve cord {ECO:0000312|EMBL:ACX44802.1};
RX PubMed=19800971; DOI=10.1016/j.ibmb.2009.09.006;
RA Moignot B., Lemaire C., Quinchard S., Lapied B., Legros C.;
RT "The discovery of a novel sodium channel in the cockroach Periplaneta
RT americana: evidence for an early duplication of the para-like gene.";
RL Insect Biochem. Mol. Biol. 39:814-823(2009).
RN [2] {ECO:0000312|PDB:5X0M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), GLYCOSYLATION AT
RP ASN-300; ASN-308; ASN-312; ASN-330; ASN-1015; ASN-1028 AND ASN-1034,
RP SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BOND, AND DOMAIN.
RX PubMed=28183995; DOI=10.1126/science.aal4326;
RA Shen H., Zhou Q., Pan X., Li Z., Wu J., Yan N.;
RT "Structure of a eukaryotic voltage-gated sodium channel at near-atomic
RT resolution.";
RL Science 355:0-0(2017).
RN [3] {ECO:0000312|PDB:6A90, ECO:0000312|PDB:6A91, ECO:0000312|PDB:6A95}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.6 ANGSTROMS) IN COMPLEX WITH SPIDER
RP MU-DIGUETOXIN-DC1A; SAXITOXIN AND TETRODOTOXIN, DISULFIDE BOND, AND
RP GLYCOSYLATION AT ASN-308; ASN-312; ASN-330; ASN-1015 AND ASN-1034.
RX PubMed=30049784; DOI=10.1126/science.aau2596;
RA Shen H., Li Z., Jiang Y., Pan X., Wu J., Cristofori-Armstrong B.,
RA Smith J.J., Chin Y.K.Y., Lei J., Zhou Q., King G.F., Yan N.;
RT "Structural basis for the modulation of voltage-gated sodium channels by
RT animal toxins.";
RL Science 362:0-0(2018).
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. {ECO:0000255|RuleBase:RU361132,
CC ECO:0000305|PubMed:28183995}.
CC -!- ACTIVITY REGULATION: Inhibited by the pore blockers saxitoxin and
CC tetrodotoxin. {ECO:0000305|PubMed:30049784}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|RuleBase:RU361132,
CC ECO:0000269|PubMed:28183995}; Multi-pass membrane protein
CC {ECO:0000255|RuleBase:RU361132, ECO:0000269|PubMed:28183995}.
CC -!- TISSUE SPECIFICITY: Detected in adult nerve cord, muscle, gut and
CC mushroom-shaped accessory glands. {ECO:0000269|PubMed:19800971}.
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|PubMed:28183995}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000255|RuleBase:RU361132}.
CC -!- WEB RESOURCE: Name=Electron Microscopy Data Bank (EMDB);
CC URL="https://www.ebi.ac.uk/pdbe/entry/emdb/EMD-6995";
CC -!- WEB RESOURCE: Name=Electron Microscopy Data Bank (EMDB);
CC URL="https://www.ebi.ac.uk/pdbe/entry/emdb/EMD-6996";
CC -!- WEB RESOURCE: Name=Electron Microscopy Data Bank (EMDB);
CC URL="https://www.ebi.ac.uk/pdbe/entry/emdb/EMD-6997";
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DR EMBL; GQ132120; ACX44802.1; -; mRNA.
DR PDB; 5X0M; EM; 3.80 A; A=1-1553.
DR PDB; 6A90; EM; 2.80 A; A=1-1553.
DR PDB; 6A91; EM; 3.20 A; A=1-1553.
DR PDB; 6A95; EM; 2.60 A; A=1-1553.
DR PDB; 6NT3; EM; 3.40 A; A=1-269, A=289-1155, A=1287-1505.
DR PDB; 6NT4; EM; 3.50 A; A=1-269, A=289-1155, A=1287-1505.
DR PDBsum; 5X0M; -.
DR PDBsum; 6A90; -.
DR PDBsum; 6A91; -.
DR PDBsum; 6A95; -.
DR PDBsum; 6NT3; -.
DR PDBsum; 6NT4; -.
DR AlphaFoldDB; D0E0C2; -.
DR SMR; D0E0C2; -.
DR IntAct; D0E0C2; 1.
DR TCDB; 1.A.1.10.20; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; D0E0C2; -.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 3.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00170; NACHANNEL.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Repeat; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1553
FT /note="Sodium channel protein PaFPC1"
FT /id="PRO_0000439762"
FT TOPO_DOM 1..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 141..159
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 160..165
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 166..186
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 187..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 201..218
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 219..224
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 225..241
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 242..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 261..280
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 281..360
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT INTRAMEM 361..385
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 386..392
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 393..413
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 414..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 520..538
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 539..549
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 550..569
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 570..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 584..603
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 604..605
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 606..623
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 624..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 640..658
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 659..686
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT INTRAMEM 687..707
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 708..719
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 720..740
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 741..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 858..875
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 876..888
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 889..907
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 908..921
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 922..940
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 941..945
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 946..964
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 965..981
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 982..1001
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1002..1047
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT INTRAMEM 1048..1069
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1070..1086
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 1087..1108
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1109..1171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 1172..1189
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1190..1200
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 1201..1219
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1220..1231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 1232..1249
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1250..1262
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 1263..1279
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1280..1298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 1299..1316
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1317..1338
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT INTRAMEM 1339..1361
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1362..1387
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TRANSMEM 1388..1410
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT TOPO_DOM 1411..1553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1146
FT /note="Linker region that may regulate channel
FT inactivation"
FT /evidence="ECO:0000303|PubMed:28183995"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378
FT /ligand="saxitoxin"
FT /ligand_id="ChEBI:CHEBI:180458"
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A91"
FT BINDING 701
FT /ligand="tetrodotoxin"
FT /ligand_id="ChEBI:CHEBI:180459"
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A95"
FT BINDING 704
FT /ligand="saxitoxin"
FT /ligand_id="ChEBI:CHEBI:180458"
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A91"
FT BINDING 704
FT /ligand="tetrodotoxin"
FT /ligand_id="ChEBI:CHEBI:180459"
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A95"
FT BINDING 1062
FT /ligand="tetrodotoxin"
FT /ligand_id="ChEBI:CHEBI:180459"
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A95"
FT BINDING 1063
FT /ligand="saxitoxin"
FT /ligand_id="ChEBI:CHEBI:180458"
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A91"
FT BINDING 1354
FT /ligand="tetrodotoxin"
FT /ligand_id="ChEBI:CHEBI:180459"
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A95"
FT BINDING 1356
FT /ligand="saxitoxin"
FT /ligand_id="ChEBI:CHEBI:180458"
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A91"
FT BINDING 1356
FT /ligand="tetrodotoxin"
FT /ligand_id="ChEBI:CHEBI:180459"
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A95"
FT SITE 539
FT /note="Interacts with the spider Mu-diguetoxin-Dc1a"
FT /evidence="ECO:0000269|PubMed:30049784"
FT SITE 542..543
FT /note="Interacts with the spider Mu-diguetoxin-Dc1a"
FT /evidence="ECO:0000269|PubMed:30049784"
FT SITE 549
FT /note="Interacts with the spider Mu-diguetoxin-Dc1a"
FT /evidence="ECO:0000269|PubMed:30049784"
FT SITE 613
FT /note="Interacts with the spider Mu-diguetoxin-Dc1a"
FT /evidence="ECO:0000269|PubMed:30049784"
FT SITE 1002
FT /note="Interacts with the spider Mu-diguetoxin-Dc1a"
FT /evidence="ECO:0000269|PubMed:30049784"
FT SITE 1027
FT /note="Interacts with the spider Mu-diguetoxin-Dc1a"
FT /evidence="ECO:0000269|PubMed:30049784"
FT SITE 1032
FT /note="Interacts with the spider Mu-diguetoxin-Dc1a"
FT /evidence="ECO:0000269|PubMed:30049784"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M,
FT ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91,
FT ECO:0007744|PDB:6A95"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M,
FT ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91,
FT ECO:0007744|PDB:6A95"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M,
FT ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91,
FT ECO:0007744|PDB:6A95"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M,
FT ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91,
FT ECO:0007744|PDB:6A95"
FT CARBOHYD 1028
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0007744|PDB:5X0M"
FT CARBOHYD 1034
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M,
FT ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91,
FT ECO:0007744|PDB:6A95"
FT DISULFID 288..337
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M,
FT ECO:0007744|PDB:6A91, ECO:0007744|PDB:6A95"
FT DISULFID 328..343
FT /evidence="ECO:0000269|PubMed:30049784,
FT ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91,
FT ECO:0007744|PDB:6A95"
FT DISULFID 709..717
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M,
FT ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91,
FT ECO:0007744|PDB:6A95"
FT DISULFID 1011..1030
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M,
FT ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91,
FT ECO:0007744|PDB:6A95"
FT DISULFID 1368..1381
FT /evidence="ECO:0000269|PubMed:28183995,
FT ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M,
FT ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91,
FT ECO:0007744|PDB:6A95"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 56..60
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6A91"
FT TURN 97..108
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6NT4"
FT HELIX 163..185
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6NT3"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 259..280
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:6A90"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6NT4"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:6A91"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 361..372
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 393..403
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 407..434
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 511..516
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 519..537
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 546..568
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 584..599
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:6A90"
FT TURN 606..608
FT /evidence="ECO:0007829|PDB:6A90"
FT HELIX 609..622
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 625..634
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 638..663
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 687..698
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 703..712
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 715..717
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 718..728
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 729..731
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 732..741
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 835..837
FT /evidence="ECO:0007829|PDB:6A91"
FT HELIX 841..854
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 856..874
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 884..911
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 915..919
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 921..940
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 942..944
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 948..951
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 952..959
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 962..964
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 965..967
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 968..976
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 979..1004
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 1009..1012
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 1014..1016
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 1021..1023
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1027..1032
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 1036..1039
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1047..1058
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1063..1072
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1086..1088
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1089..1099
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 1100..1105
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1106..1122
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 1127..1129
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1131..1143
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1158..1165
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 1166..1168
FT /evidence="ECO:0007829|PDB:6A90"
FT HELIX 1170..1185
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1187..1189
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1196..1204
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1207..1222
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1226..1230
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1232..1248
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 1252..1254
FT /evidence="ECO:0007829|PDB:6A91"
FT STRAND 1256..1259
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1261..1270
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1271..1274
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1275..1278
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1283..1294
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1296..1320
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 1321..1323
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 1332..1338
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1339..1348
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1349..1351
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 1352..1354
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1355..1362
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 1373..1376
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1384..1398
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 1399..1402
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1404..1422
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1428..1436
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 1438..1440
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 1446..1449
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1450..1452
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1453..1458
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 1462..1464
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1470..1474
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1483..1485
FT /evidence="ECO:0007829|PDB:6A95"
FT STRAND 1486..1488
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1489..1503
FT /evidence="ECO:0007829|PDB:6A95"
FT TURN 1509..1512
FT /evidence="ECO:0007829|PDB:6A95"
FT HELIX 1514..1519
FT /evidence="ECO:0007829|PDB:6A95"
SQ SEQUENCE 1553 AA; 179116 MW; 62CBCDA0A59D61D5 CRC64;
MADNSPLIRE ERQRLFRPYT RAMLTAPSAQ PAKENGKTEE NKDNSRDKGR GANKDRDGSA
HPDQALEQGS RLPARMRNIF PAELASTPLE DFDPFYKNKK TFVVVTKAGD IFRFSGEKSL
WMLDPFTPIR RVAISTMVQP IFSYFIMITI LIHCIFMIMP ATQTTYILEL VFLSIYTIEV
VVKVLARGFI LHPFAYLRDP WNWLDFLVTL IGYITLVVDL GHLYALRAFR VLRSWRTVTI
VPGWRTIVDA LSLSITSLKD LVLLLLFSLF VFAVLGLQIY MGVLTQKCVK HFPADGSWGN
FTDERWFNYT SNSSHWYIPD DWIEYPLCGN SSGAGMCPPG YTCLQGYGGN PNYGYTSFDT
FGWAFLSVFR LVTLDYWEDL YQLALRSAGP WHILFFIIVV FYGTFCFLNF ILAVVVMSYT
HMVKRADEEK AAERELKKEK KAASVANNTA NGQEQTTIEM NGDEAVVIDN NDQAARQQSD
PETPAPSVTQ RLTDFLCVWD CCVPWQKLQG AIGAVVLSPF FELFIAVIIV LNITFMALDH
HDMNIEFERI LRTGNYIFTS IYIVEAVLKI IALSPKFYFK DSWNVFDFII VVFAILELGL
EGVQGLSVFR SFRLLRVFRL AKFWPTLNNF MSVMTKSYGA FVNVMYVMFL LLFIFAIIGM
QLFGMNYIDN MERFPDGDLP RWNFTDFLHS FMIVFRALCG EWIESMWDCM LVGDWSCIPF
FVAVFFVGNL VILNLLIALL LNNYGSFCTS PTSDEEDSKD EDALAQIVRI FKRFKPNLNA
VKLSPMKPDS EDIVESQEIQ GNNIADAEDV LAGEFPPDCC CNAFYKCFPS RPARDSSVQR
MWSNIRRVCF LLAKNKYFQK FVTAVLVITS VLLALEDIYL PQRPVLVNIT LYVDYVLTAF
FVIEMIIMLF AVGFKKYFTS KWYWLDFIVV VAYLLNFVLM CAGIEALQTL RLLRVFRLFR
PLSKVNGMQV VTSTLVEAVP HIFNVILVGI FFWLVFAIMG VQLFAGKFYK CVDENSTVLS
HEITMDRNDC LHENYTWENS PMNFDHVGNA YLSLLQVATF KGWLQIMNDA IDSREVHKQP
IRETNIYMYL YFIFFIVFGS FFILKLFVCI LIDIFRQQRR KAEGLSATDS RTQLIYRRAV
MRTMSAKPVK RIPKPTCHPQ SLMYDISVNR KFEYTMMILI ILNVAVMAID HYGQSMEFSE
VLDYLNLIFI IIFFVECVIK VSGLRHHYFK DPWNIIDFLY VVLAIAGLML SDVIEKYFIS
PTLLRILRIL RVGRLLRYFQ SARGMRLLLL ALRKALRTLF NVSFLLFVIM FVYAVFGMEF
FMHIRDAGAI DDVYNFKTFG QSIILLFQLA TSAGWDGVYF AIANEEDCRA PDHELGYPGN
CGSRALGIAY LVSYLIITCL VVINMYAAVI LDYVLEVYED SKEGLTDDDY DMFFEVWQQF
DPEATQYIRY DQLSELLEAL QPPLQVQKPN KYKILSMNIP ICKDDHIFYK DVLEALVKDV
FSRRGSPVEA GDVQAPNVDE AEYKPVSSTL QRQREEYCVR LIQNAWRKHK QQN
