SCN1_HETBL
ID SCN1_HETBL Reviewed; 1522 AA.
AC Q05973;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Sodium channel protein 1 brain;
DE AltName: Full=Sodium channel protein I brain;
OS Heterololigo bleekeri (Spear squid) (Loligo bleekeri).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Heterololigo.
OX NCBI_TaxID=1423826;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Optic lobe;
RX PubMed=1339273; DOI=10.1016/s0006-291x(05)80775-2;
RA Sato C., Matsumoto G.;
RT "Primary structure of squid sodium channel deduced from the complementary
RT DNA sequence.";
RL Biochem. Biophys. Res. Commun. 186:61-68(1992).
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC 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 -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000305}.
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DR EMBL; D14525; BAA03398.1; -; mRNA.
DR PIR; JC1101; JC1101.
DR AlphaFoldDB; Q05973; -.
DR SMR; Q05973; -.
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; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 2.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00170; NACHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Repeat; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1522
FT /note="Sodium channel protein 1 brain"
FT /id="PRO_0000048514"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..70
FT /note="Helical; Name=S1 of repeat I"
FT TOPO_DOM 71..77
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 78..99
FT /note="Helical; Name=S2 of repeat I"
FT TOPO_DOM 100..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 113..134
FT /note="Helical; Name=S3 of repeat I"
FT TOPO_DOM 135..143
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..167
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT TOPO_DOM 168..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 180..201
FT /note="Helical; Name=S5 of repeat I"
FT TOPO_DOM 202..278
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 279..303
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 304..308
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 309..331
FT /note="Helical; Name=S6 of repeat I"
FT TOPO_DOM 332..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 407..426
FT /note="Helical; Name=S1 of repeat II"
FT TOPO_DOM 427..442
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 443..464
FT /note="Helical; Name=S2 of repeat II"
FT TOPO_DOM 465..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..491
FT /note="Helical; Name=S3 of repeat II"
FT TOPO_DOM 492..498
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 499..522
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT TOPO_DOM 523..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 532..553
FT /note="Helical; Name=S5 of repeat II"
FT TOPO_DOM 554..575
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 576..596
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 597..607
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 608..628
FT /note="Helical; Name=S6 of repeat II"
FT TOPO_DOM 629..777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 778..797
FT /note="Helical; Name=S1 of repeat III"
FT TOPO_DOM 798..815
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 816..837
FT /note="Helical; Name=S2 of repeat III"
FT TOPO_DOM 838..846
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 847..868
FT /note="Helical; Name=S3 of repeat III"
FT TOPO_DOM 869..874
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 875..898
FT /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT TOPO_DOM 899..915
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 916..937
FT /note="Helical; Name=S5 of repeat III"
FT TOPO_DOM 938..976
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 977..998
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 999..1009
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1010..1022
FT /note="Helical; Name=S6 of repeat III"
FT TOPO_DOM 1023..1100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1101..1120
FT /note="Helical; Name=S1 of repeat IV"
FT TOPO_DOM 1121..1132
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1133..1154
FT /note="Helical; Name=S2 of repeat IV"
FT TOPO_DOM 1155..1162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1163..1184
FT /note="Helical; Name=S3 of repeat IV"
FT TOPO_DOM 1185..1194
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1195..1218
FT /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT TOPO_DOM 1219..1236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1237..1258
FT /note="Helical; Name=S5 of repeat IV"
FT TOPO_DOM 1259..1270
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1271..1293
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1294..1323
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1324..1346
FT /note="Helical; Name=S6 of repeat IV"
FT TOPO_DOM 1347..1522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 41..342
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 393..647
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 770..1074
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1083..1386
FT /note="IV"
FT /evidence="ECO:0000305"
FT MOD_RES 1076
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 963
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 207..255
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 598..606
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
SQ SEQUENCE 1522 AA; 174114 MW; 4CFDDB83E5436626 CRC64;
MDEKYTAKNR DKTFVVIEKR FKKNIIHRFS AKRSLFLFTP RNPIRRLAVC IATNVCFDYF
LMFTIMINCV FLAMPDISEF AEYIFLGIYT MEMAIKLVAG GFFIDKYTYL RDAWNCLDFT
VIMISYITLL LQTINDKVIS DITGLRTFRV LRALRTLSII PGLKTMVNAL LRALRMLISV
LILILFCLWI FSQAGVQLFG GALRHKCVLQ IHGSPAFGKT YDEFYAEHIE NSDNWLAKGN
GEYVLCGNAT GAGPCPTNYT CLPDIGENPN YGYTNFDSIG WSMLISFQLL TQDYWEDVYN
KVIRAHSPWT VIYFIVINFF GSLYLMNLML AVVATAYELE VKNTGKKLQQ TAATAREQSL
KEQERRNTLT VSEADSHVDD RNCTCCEQCC GCCYNPWLRV QSFAHCIITD SFTEVFIIFI
IVLNTVFLAM EHHGMSMELK NVLKVANYVF TTVFVLEAIL KLLAFNKQYF KSGWNICDLV
VVVASLIDLG VEGLKGVSVF RSFRLLRVFH LAQSWTTMRL LLCIILNTLG SLGYLTIILI
IVIYIFAVTG LQLFHTEYTP DKFRGEPVPR WNFNDFLHSF MMVFRILCGE WIEPMYDCMR
ACNGLCFLIF IPVTVFGKTL FFLFIGLVLG AFGSDTVEQE VEVSSFALPG PESKPCSVRE
RGISATDDNV KDDGQDEVQQ NSEETKIDLR NNDKQSKDGM ILENNCNNDS LASLGSLGSI
PDIMDGSSVE DDISSCQQKD IQPCLPLFIS SRFKCLREFD DTSHGKKWNN FRRQLMMVCE
NKYFETGVLV IIFASSILLA FEDIYLNEKP RLKLAIFYLD ITFCLLFFLE MVLKLVALGF
VHYYTHFWTI LDFTIVIITV ISLAASGLGM EQITAFRSLR TLRALRPLRA VSRWQGMKII
VNALMLSIPS IFNVLLVCVV FWLIFAIMGV QLFAGKFYKC VNETNMRIPP TEVANKIECY
NKNYTWVNSN VNFDNVGGAF LALFQVATFE GWMEIMADAV DVTEVDEQPK FEATVYYYFY
FVLFIIFGSF FVLNLVIGVI IDKFSFLKKK YDGTYLDMFL TPTQQNYYNT LKKLGTKKPQ
KTVKRPKNKC QAVVYDLVMS NQFEIFITTI IITNMIFMAF EHYNQSEVVT EVLATANIAF
TILYAVEAII KIIGLRIHYL RNLWNVFDFL VVTLSVMDAF LNDIFGDGIF MNPSLLRVAR
MFRIGRIIRL IKWAKGMRKL LFALVISLPA LFNIGALLML VMFIYTIIGM SSFGQIKLSG
ALNDQVNFQT FGKTFLLLVR LATSAGWNDI LGPLLIQPPN CDPNYITTST GEKIKVVNGD
CGMPWLAISY MVSYIIIVFM IVFNMYIAVI LENFNQAHAQ EEVGITEDDL DMFYGVWEQY
DPLATQFIKH EQLSDFIQDL DPPLKVKKPN NVAIATFDLP IVKGGHIHCL DILLALVKFA
LGGNLEETEA FKRVRTQMEA RFDEIFPTRE KSEIRTSTLQ MRREEMAART LQRAWKRRKI
MRSFPSPEMI RYFIISAPET AV
