ID A0A3Q4HMW7_NEOBR Unreviewed; 1796 AA.
AC A0A3Q4HMW7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN8A {ECO:0000313|Ensembl:ENSNBRP00000018537.1};
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:ENSNBRP00000018537.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000018537.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSNBRT00000019028.1; ENSNBRP00000018537.1; 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 257..277
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 358..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 397..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 739..763
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 775..793
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 854..883
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 942..968
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1126..1145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1157..1177
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1189..1209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1266..1288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1336..1354
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1366..1388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1400..1419
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1467..1488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1509..1528
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1556..1579
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 139..431
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 552..693
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 744..974
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 982..1121
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1126..1238
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1335..1589
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 25..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1796
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 505..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1740..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1796 AA; 204146 MW; 64DF8696A63A5497 CRC64;
MAAPLLAPPG PDSFRKFTPE SLAVLEQRIQ EEKNKKPPKQ DSSYRDDDDE NKPKPNSDLE
AGKSLPYIYG DLPKGMAAIP LEDLDPFYVN SQKTFIVINK GKTIFRFSAT PALYLISPFN
PVRRLAIKIL IHSYPLKCMI IMCTILTNCI FMTFSDPPEW SKQVEYTFTG IYTFESLVKI
TARGFCIDGF TFLRDPWNWL DFMVISMAYI TEFVDLGNVS ALRTFRVLRA LKTISVIPGL
KTIVGALIQS VKKLSDVMIL TVFCLSVFAL IGLQLFMGNL RHKCVQKCAE WIKFSKSRQN
ASEMTQFGSF SLLPFSPLSA NFYFLPGQLD ALLCGNSSDS GRCPEGYTCM KAGRNPNYGY
TSFDSFGWAF LALFRLMTQD FWENLYMLTL RAAGKTYMLF FVLVIFVGSF YLVNLILAVV
AMAYEEQNQA TMEEATRKEE EFKAMLEQLK KQQEDAQTAA MATSAGTVSE DAVEDDGGGR
LSCSSSEMSK LSSKSAKERR NRKKKWRQKE QEKEKGDSEK FVKSESDDGS KRSRFRFPDN
RLGRKSSIMN QSLLSIPGSP FLSRHNSKSS IFSFKGRSKD VGSENEFADD EHSTVEECEE
RRGSLFSPYR RSSYTGFHGK RNSTVDCNGV VSLIGPGPGG RLLPEVKIDK AATDESPTTE
VEVKKKLSGS LMVSVDQLNT SFGRKERANS VMSVITNTLV EELEESQRKC PPCWYKFANT
FLIWECSPKW IKIKEIVNLI VMDPFVDLAI TICIVLNTLF MAMEHYPMTP DFEDMLSVGN
LVFTGIFAGE MLFKLVAMDP YYYFQEAWNC FDGFIVTLSL VELALADVEG LSVLRSFRLL
RVFKLAKSWP TLNMLIKIIG NSVGALGNLT LVLAIIVFIF AVVGMQLFGK NYKDCVCKIS
LECELPRWHM NDFFHSFLIV FRVLCGEWIE TMWDCMEVAG QAMCLIVFMM VMVIGNLVVL
NLFLALLLSS FSADNLAATD DDGEPNNLQI SVMRIKKGIA WIKAKMRILM ASLLRKPPME
DEQKPLEDMY DKKLNCIANH TGVDINRDLD YAKNGNGTTS GIGSSVGKYM IDEDHMSFIH
NPNLTVCVPI AVGESDFENL NTEDFSSESD NENSKEVSEN SQDRTLIIFM ILLSSGALAF
EDVYIEQRKT IRIILEYADR VFTYIFILEM LLKWVAYGFV KYFTNAWCWL DFFIVDVSIV
SLVANALGYS DLGPIKSLRT LRALRPLRAL SRFEGMRATF KGWMDIMYAA VDSREVEKQP
DYEVNIYMYI YFVVFIIFGS FFTLNLFIGQ DIFMTEEQKK YYNAMKKLGS KKPQKPIPRP
QNKIQGMVFD FVTQQVFDIS IMILICLNMV TMMVETDDQS GETENVLYWV NFIFIVVFTT
EFLLKLFALR HYYFTNGWNI FDVVVVILSI VGMFLADLIE KYFVSPTLFR VIRLARIGRI
LRLIKGAKGI RTLLFALMMS LPALFNIGLL LFLVMFIFSI FGMSNFGYVK HGAGIDDLYN
FETFGNSMII LFMITTSAGW DGLLLPILNY PPDCDPNLEN PGTSVKGDCG NPSVGIFFFV
MYIIISFLIV VNMYIAIILE NFSVATEESA DPLSEDDFET FYEIWEKFDP TASQFISFAK
LPDFADALEH PLRVPKPNTI ELIAMDMPMV SGDRIHCLDI LFAFTKRVLG DSGELDMLRQ
QMEERFVAAN PSKVSYEPIT TTLRRKQEDV SARTIQNAYR AHLIRRGIIF KRVFANNKLE
NGGTNQEKKE STPSTASLPS YDSVTKPEKE KQDDNKEEWA RKEKDKNQKD EWESKC
//