ID A0A3Q4MSC3_NEOBR Unreviewed; 1999 AA.
AC A0A3Q4MSC3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN8A {ECO:0000313|Ensembl:ENSNBRP00000018229.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000018229.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000018229.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|RuleBase:RU361132}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361132}.
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DR STRING; 32507.ENSNBRP00000018229; -.
DR Ensembl; ENSNBRT00000018718.1; ENSNBRP00000018229.1; ENSNBRG00000012055.1.
DR GeneTree; ENSGT00940000156263; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000012055; Expressed in brain and 2 other cell types or tissues.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR008054; Na_channel_a8su.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc_dom.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF23; SODIUM CHANNEL PROTEIN TYPE 8 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PRINTS; PR01667; NACHANNEL8.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion channel {ECO:0000256|RuleBase:RU361132};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|RuleBase:RU361132};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW ECO:0000256|RuleBase:RU361132};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361132};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361132};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 345..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 384..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 714..738
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 750..768
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 829..858
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 917..943
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1216..1234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1255..1274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1332..1358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1455..1481
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1540..1558
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1570..1588
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1600..1619
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1656..1684
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1759..1782
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 135..418
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 539..669
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 719..949
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 957..1091
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1214..1490
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1539..1792
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1943..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1943..1965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1967..1999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1999 AA; 227583 MW; 5703E674454B4E75 CRC64;
MAAPLLAPPG PDSFRKFTPE SLAVLEQRIQ EEKNKKPPKQ DSSYRDDDDE NKPKPNSDLE
AGKSLPYIYG DLPKGMAAIP LEDLDPFYVN SQKTFIVINK GKTIFRFSAT PALYLISPFN
PVRRLAIKIL IHSYPLKMII MCTILTNCIF MTFSDPPEWS KQVYTFTGIY TFESLVKITA
RGFCIDGFTF LRDPWNWLDF MVISMYITEF VDLGNVSALR TFRVLRALKT ISVIPLKTIV
GALIQSVKKL SDVMILTVFC LSVFALIGLQ LFMGNLRHKC VFWPINTNES YLANGSKGFD
WDEYITNDNF YFLPGQLDAL LCGNSSDSRC PEGYTCMKAG RNPNYGYTSF DSFGWAFLAL
FRLMTQDFWE NLYMLTLRAA GKTYMLFFVL VIFVGSFYLV NLILAVVAMA YEEQNQATME
EATRKEEEFK AMLEQLKKQQ EDAQTAAMAT SAGTVSEDAV EDDGGGRLSC SSSEMSKLSS
KSAKERRNRK KKWRQKEQEK EKGDSEKFVK SESDDGSKRS RFRFPDNRLG RKSSIMNQSL
LSIPGSPFLS RHNSKSSIFS FKGRSKDVGS ENEFADDEHS TVEECEERRG SLFSPYRRSS
YTGFHGKRNS TVDCNGVVSL IGPGPGGRLL PEPTTEVEVK KKLSGSLMVS VDQLNTSFGR
KERANSVMSV ITNTLVELEE SQRKCPPCWY KFANTFLIWE CSPKWIKIKE IVNLIVMDPF
VDLAITICIV LNTLFMAMEH YPMTPDFEDM LSVGNLVFTG IFAGEMLFKL VAMDPYYYFQ
EAWNCFDGFI VTLSLVELAL ADVEGLSVLR SFRLLRVFKL AKSWPTLNML IKIIGNSVGA
LGNLTLVLAI IVFIFAVVGM QLFGKNYKDC VCKISLECEL PRWHMNDFFH SFLIVFRVLC
GEWIETMWDC MEVAGQAMCL IVFMMVMVIG NLVVLNLFLA LLLSSFSADN LAATDDDGEP
NNLQISVMRI KKGIAWIKAK MRILMASLLR KPPMEDEQKP LEDMYDKKLN CIANHTGVDI
NRDLDYAKNG NGTTSGIGSS VGKYMIDEDH MSFIHNPNLT VCVPIAVGES DFENLNTEDF
SSESDNENSK EXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXXXYL IVEHNWFETL IIFMILLSSG ALAFEDVYIE QRKTIRIILE YADRVFTYIF
ILEMLLKWVA YGFVKYFTNA WCWLDFFIVD VSIVSLVANA LGYSDLGPIK SLRTLRALRP
LRALSRFEGM RVVVNALVGA IPSIMNVLLV CLIFWLIFSI MGVNLFAGKY YYCFNETSEE
YFPTSVVDNK TQCFELINLN YSEVRWKNVK INFDNVGAGY LALLQVATFK GWMDIMYAAV
DSREVEKQPD YEVNIYMYIY FVVFIIFGSF FTLNLFIGVI IDNFNQQKKK FGGQDIFMTE
EQKKYYNAMK KLGSKKPQKP IPRPQNKIQG MVFDFVTQQV FDISIMILIC LNMVTMMVET
DDQSGETENV LYWVNFIFIV VFTTEFLLKL FALRHYYFTN GWNIFDVVVV ILSIVMFLAD
LIEKYFVSPT LFRVIRLARI GRILRLIKGA KGIRTLLFAL MMSLPALFNI GLLLFLVMFI
FSIFGMSNFG YVKHGAGIDD LYNFETFGNS MIILFMITTS AGWDGLLLPI LNYPPDCDPN
LENPGTSVKG DCGNPSVGIF FFVMYIIISF LIVVNMYIAI ILENFSVATE ESADPLSEDD
FETFYEIWEK FDPTASQFIS FAKLPDFADA LEHPLRVPKP NTIELIAMDM PMVSGDRIHC
LDILFAFTKR VLGDSGELDM LRQQMEERFV AANPSKVSYE PITTTLRRKQ EDVSARTIQN
AYRAHLIRRG IIFKRVFANN KLENGGTNQE KKESTPSTAS LPSYDSVTKP EKEKQDDNKE
EWARKEKDKN QKDEWESKC
//
