SCNA_ELEEL
ID SCNA_ELEEL Reviewed; 1820 AA.
AC P02719;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Sodium channel protein;
DE AltName: Full=Na(+) channel;
OS Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=8005;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6209577; DOI=10.1038/312121a0;
RA Noda M., Shimizu S., Tanabe T., Takai T., Kayano T., Ikeda T.,
RA Takahashi H., Nakayama H., Kanaoka Y., Minamino N., Kangawa K., Matsuo H.,
RA Raftery M.A., Hirose T., Inayama S., Hayashida H., Miyata T., Numa S.;
RT "Primary structure of Electrophorus electricus sodium channel deduced from
RT cDNA sequence.";
RL Nature 312:121-127(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2442385; DOI=10.3109/10799898709054998;
RA Noda M., Numa S.;
RT "Structure and function of sodium channel.";
RL J. Recept. Res. 7:467-497(1987).
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, the protein
CC forms a sodium-selective channel through which Na(+) ions may pass in
CC accordance with their electrochemical gradient.
CC {ECO:0000269|PubMed:2442385}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2442385};
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|PubMed:2442385}.
CC -!- MISCELLANEOUS: Available data suggest that activation and inactivation
CC gates are located near the cytoplasmic surface of the membrane. It is
CC hypothesized that residues 802-806, 847-857, 894-910, and 942-955
CC might, in conjunction with the positively charged residues of S4, act
CC as a voltage sensor involved with the activation gate.
CC {ECO:0000305|PubMed:2442385}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000305}.
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DR EMBL; X01119; CAA25587.1; -; mRNA.
DR EMBL; M22252; AAA79960.1; -; mRNA.
DR PIR; A03178; CHEE.
DR PDB; 5XSY; EM; 4.00 A; A=1-1820.
DR PDBsum; 5XSY; -.
DR AlphaFoldDB; P02719; -.
DR BMRB; P02719; -.
DR SMR; P02719; -.
DR STRING; 8005.ENSEEEP00000026793; -.
DR TCDB; 1.A.1.10.19; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; P02719; -.
DR PRIDE; P02719; -.
DR Proteomes; UP000314983; Unassembled WGS sequence.
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 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; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 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; Reference proteome; Repeat; Sodium;
KW Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT CHAIN 1..1820
FT /note="Sodium channel protein"
FT /id="PRO_0000048513"
FT TOPO_DOM 1..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..138
FT /note="Helical; Name=S1 of repeat I"
FT TOPO_DOM 139..149
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 150..171
FT /note="Helical; Name=S2 of repeat I"
FT TOPO_DOM 172..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..197
FT /note="Helical; Name=S3 of repeat I"
FT TOPO_DOM 198..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT TOPO_DOM 225..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 244..264
FT /note="Helical; Name=S5 of repeat I"
FT TOPO_DOM 265..346
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 347..371
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 372..378
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 379..402
FT /note="Helical; Name=S6 of repeat I"
FT TOPO_DOM 403..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 558..578
FT /note="Helical; Name=S1 of repeat II"
FT TOPO_DOM 579..599
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 600..620
FT /note="Helical; Name=S2 of repeat II"
FT TOPO_DOM 621..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 626..643
FT /note="Helical; Name=S3 of repeat II"
FT TOPO_DOM 644..650
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 651..671
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT TOPO_DOM 672..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 691..711
FT /note="Helical; Name=S5 of repeat II"
FT TOPO_DOM 712..734
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 735..755
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 756..766
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 767..790
FT /note="Helical; Name=S6 of repeat II"
FT TOPO_DOM 791..1004
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1005..1025
FT /note="Helical; Name=S1 of repeat III"
FT TOPO_DOM 1026..1037
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1038..1058
FT /note="Helical; Name=S2 of repeat III"
FT TOPO_DOM 1059..1065
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1066..1086
FT /note="Helical; Name=S3 of repeat III"
FT TOPO_DOM 1087..1091
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1092..1112
FT /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT TOPO_DOM 1113..1131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1132..1152
FT /note="Helical; Name=S5 of repeat III"
FT TOPO_DOM 1153..1199
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1200..1221
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1222..1243
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1244..1264
FT /note="Helical; Name=S6 of repeat III"
FT TOPO_DOM 1265..1320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1321..1341
FT /note="Helical; Name=S1 of repeat IV"
FT TOPO_DOM 1342..1352
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1353..1376
FT /note="Helical; Name=S2 of repeat IV"
FT TOPO_DOM 1377..1380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1381..1398
FT /note="Helical; Name=S3 of repeat IV"
FT TOPO_DOM 1399..1416
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1417..1437
FT /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT TOPO_DOM 1438..1453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1454..1474
FT /note="Helical; Name=S5 of repeat IV"
FT TOPO_DOM 1475..1490
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1491..1513
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1514..1543
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1544..1567
FT /note="Helical; Name=S6 of repeat IV"
FT TOPO_DOM 1568..1820
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 108..410
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 548..811
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 988..1295
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1304..1602
FT /note="IV"
FT /evidence="ECO:0000305"
FT REGION 285..342
FT /note="Non-homologous region of repeat I"
FT REGION 483..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1194
FT /note="Non-homologous region of repeat III"
FT REGION 1490..1505
FT /note="Non-homologous region of repeat IV"
FT COMPBIAS 485..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..956
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 271..324
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 757..766
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
SQ SEQUENCE 1820 AA; 208332 MW; 1B271F626E057864 CRC64;
MARKFSSARP EMFRRFTPDS LEEIEAFTEL KKSCTLEKKE PESTPRIDLE AGKPLPMIYG
DPPEDLLNIP LEDLDPFYKT QKTFIVISKG NIINRFNAER ALYIFSPFNP IRRGAIRVFV
NSAFNFFIMF TIFSNCIFMT ISNPPAWSKI VEYTFTGIYT FEVIVKVLSR GFCIGHFTFL
RDPWNWLDFS VVTMTYITEF IDLRNVSALR TFRVLRALKT ITIFPGLKTI VRALIESMKQ
MGDVVILTVF SLAVFTLAGM QLFMGNLRHK CIRWPISNVT LDYESAYNTT FDFTAYIENE
ENQYFLDGAL DALLCGNNSD AGKCPEGYTC MKAGRNPNYG YTNYDNFAWT FLCLFRLMLQ
DYWENLYQMT LRAAGKSYMV FFIMVIFLGS FYLINLILAV VAMAYEEQNQ ATLAEAQEKE
AEFQRAVEQL RIQQEQINDE RKASLASQLT QNQEAEITDD GDDAIKECNG KAFPLANIRE
PSSVKLSTEE QRSDSKSMDS KHSVDKPSLK HKAASTMSVF TLEDLEAARR PCPPVWYKFA
GFVFKWNCCG PWVFLKKWVH FVMMDPFTDL FITLCIILNT LFMSIEHHPM NESFQSLLSA
GNLVFTTIFA AEMVLKIIAL DPYYYFQQTW NIFDSIIVSL SLLELGLSNM QGMSVLRSLR
LLRIFKLAKS WPTLNILIKI ICNSVGALGN LTIVLAIIVF IFALVGFQLF GKNYKEYVCK
ISDDCELPRW HMNDFFHSFL IVFRALCGEW IETMWDCMEV GGVPMCLAVY MMVIIIGNLV
MLNLFLALLL SSFSSDNLSS IEEDDEVNSL QVASERISRA KNWVKIFITG TVQALVLWIQ
GKKPPSDDVV GEEGDNEGKK DTLPLNYLDG EKIVDGITNC VESPTLNLPI VKGESEIEEE
GLVDSSDEED TNKKKHALND EDSSVCSTVD YSPSEQDPLA KEEEEEEEEE PEELESKDPE
ACFTEKCIWR FPFLDVDITQ GKGKIWWNLR RTCYTIVEHD YFETFIIFMI LLSSGVLAFE
DIYIWRRRVI KVILEYADKV FTYVFIVEML LKWVAYGFKR YFTDAWCWLD FVIVGASIMG
ITSSLLGYEE LGAIKNLRTI RALRPLRALS RFEGMKVVVR ALLGAIPSIM NVLLVCLMFW
LIFSIMGVNL FAGKFYRCIN TTTDEILPVE EVNNRSDCMA LMYTNEVRWV NLKVNYDNAG
MGYLSLLQVS TFKGWMDIMY AAVDSREVED QPIYEINVYM YLYFVIFIVF GAFFTLNLFI
GVIIDNFNRQ KQKLGGEDLF MTEEQKKYYN AMKKLGSKKA AKCIPRPSNV VQGVVYDIVT
QPFTDIFIMA LICINMVAMM VESEDQSQVK KDILSQINVI FVIIFTVECL LKLLALRQYF
FTVGWNVFDF AVVVISIIGL LLSDIIEKYF VSPTLFRVIR LARIARVLRL IRAAKGIRTL
LFALMMSLPA LFNIGLLLFL IMFIFSIFGM SNFAYVKKQG GVDDIFNFET FGNSMICLFE
ITTSAGWDGL LLPTLNTGPP DCDPDVENPG TDVRGNCGNP GKGITFFCSY IILSFLVVVN
MYIAIILENF GVAQEESSDL LCEDDFVMFD ETWHKFDVHG TQFLDYNDLP RFVNALQEPM
RIPNPNRHKL AKMDMYVVME DKISYLDVLL AVTQEVLGDT TEMEAMRLSI QAKFKKDNPS
PTFFEPVVTT LRRKEEEWAS VVIQRAFRQY LLMRAVSHAS FLSQIKHMNE GPKDGVGSQD
SLITQKMNAL YRGNPELTMP LEQQIKPMLD KPRMPSLSVP ETYPIQIPKE VTNEVILHSA
PMVRQNYSYS GAIVVRESIV
