ID A0A3B4YWC2_SERLL Unreviewed; 2027 AA.
AC A0A3B4YWC2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000032683.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000032683.1}
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; 1841481.ENSSLDP00000032683; -.
DR Ensembl; ENSSLDT00000033605.1; ENSSLDP00000032683.1; ENSSLDG00000025051.1.
DR GeneTree; ENSGT00940000163423; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0045202; C:synapse; IEA:GOC.
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 GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0006110; P:regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IEA:Ensembl.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IEA:Ensembl.
DR GO; GO:0036269; P:swimming behavior; IEA:Ensembl.
DR GO; GO:0099536; P:synaptic signaling; IEA:Ensembl.
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; IPR000048; IQ_motif_EF-hand-BS.
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:SF278; SODIUM CHANNEL PROTEIN TYPE 2 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 SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50096; IQ; 1.
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 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 Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 234..255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 415..442
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 769..787
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 799..822
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 834..858
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 879..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 969..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1234..1252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1273..1292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1304..1324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1350..1376
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1470..1496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1555..1573
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1585..1603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1615..1635
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1672..1700
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1776..1799
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 140..448
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 568..718
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 768..998
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1006..1227
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1232..1505
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1554..1809
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 27..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1977..2027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1977..2001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2002..2027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2027 AA; 229604 MW; 6B9B37838DE24E8F CRC64;
MAQLLVPPGP DSFRPFVPES LAAIERRIAE EEARRPRADR RSDSDDENGP KPNSDLEAGK
SLPFIYGDTP SQLVSTPLED LDPFYSNQKT FIVLNRGKAI FRFNATPALY ILSPFNPLRR
IGFMLNKNVL LCSLTWFFTL FSMLIMFTIL TNCAFMTLSN PPEWAKNVEY TFTGIYTFES
LIKILARGFC VGKFTFLRDP WNWLDFSVIL MAYITEFVNL GNVSALRTFR VLRALKTISV
IPGLKTIVGA LIQSVKKLSD VMILTVFCLS VFALIGLQLF MGNLRQKCVR KLLFTNSSNI
TADDMMFFNG TLMESNSTFV QNATENPFNW TEYINDENNY YYLPGRRDAL LCGNASGAGL
CPEGFLCLKA GRNPDYGYTS FDTFSWAFLS LFRLMTQDYW ENLYQQTLRV AGKPYMIFFV
LVIFLGSFYL VNLILAVVAM AYDEQNQATI EEAQQKEEEF QAMLEQLKRQ QEEAQVAAAA
ATESGEYSGR GGPTSESSSG TSKLSSKSAK ERRNRRKKRK QREEEEERGA LKFHKSESED
SIKRSSFRFS IDANRLSYEK RCSSPNQSLL SIRGSLLSPR RNSRASLFSF RGRARDMGSE
NDFADDEHST FEESDSRRGS LFLPRRLERR SSAVSQTSLG APRIILPANG KMHCTVDCNG
VVSLVGGTSV TTSPVGHLLP EGTTTDTELK KRRSGFHQPS MDYLDEPGGR QRAMSVASIL
TNTMEELEES RQKCPPCWYR FANTCLIWDC CPAWLKIKEV VNMVVMDPFV DLAITICIVL
NTLFMAMEHY PMTKEFNTVL SVGNLVFTGI FTAEMCFKII ALDPYYYFQE GWNIFDGIIV
SLSLMELGLA NVEGLSVLRS FRLLRVFKLA KSWPTLNMLI KIIGNSVGAL GNLTLVLAII
VFIFAVVGMQ LFGKSYKECV CKISDECELP RWHMHDFFHS FLIVFRVLCG EWIETMWDCM
EVAGQSMCLI VFMMVMVIGN LVVLNLFLAL LLSSFSADNL AATDDDSEMN NLQIAVGRIQ
RGIAFVKATV RQFLQSLCFG GGGKGSGLAE ESKPLDELHS NGKGNCISNH TSVEISKDPG
GVYMTEGNGR PGGGLVVGVR AGGDTTVKYP VEESDYMSFI HNPSLTVTVP IAVGESDFEN
LNTEDFSSDS SDIEGSKEPQ PLSSSEGSTV DIRPPGDGVD SVELEPEESL DPEACFTEGC
VRRFQCCQIN EEGSHYKSWW TLRKTCFIIV EHNWFESFII FMILLSSGAL AFEDIYIEQR
RTIKTMLEYS DKVFTYVFIL EMLLKWVAYG FVKYFTNAWC WLDFLIVDVS LVSLVANALG
YSELSAIKSL RTLRALRPLR ALSRFEGMRV VVNALLGAIP SIMNVLLVCL IFWLIFSIMG
VNLFAGKYYH CVNTTSDEIL PISIVNNKSE CMSLVNDSAR WKNVKINFDN VGAGYLALLQ
VATFKGWMDI MYAAVDSRNL EDQPKYEVNL YMYLYFVIFI IFGSFFTLNL FIGVIIDNFN
QQKKKISCQD IFMTEEQKKY YNAMKKLGSK KPQKPIPRPT NAFQGCVFDF ITKQAFDIVI
MILICLNMVT MMVETDDQTP DMDKILYWIN LVFIVLFTGE CVLKMISLRH YYFTIGWNIF
DFVVVILSIV GMFLSELIEK YFVSPTLFRV IRLARIGRIL RLIKGAKGIR TLLFALMMSL
PALFNIGLLL FLVMFIYAIF GMSNFAYVKR EAGIDDMFNF ETFGNSMICL FQITTSGGWD
GLLAPILNKR EPDCDSQMEH PGNSYKGNCG NPSVGIFFFV SYIIICFLIV VNMYIAVILE
NFSVATEESA EPLSEDDFEM FYEVWERFDP DATQFMEYSK LSDFADALDP PLRMPKPNMI
QLISMDLPMV SGERIHCLDI LFAFTKRVLG EGGEMDVLRG QMEERFMASN PSKVSYEPIT
TTLRRKQEDM SAVIIQRAFR RYMIRLAMKK ASALYKERLK EGVRDPDKDV MVISKFTENS
TSDKTDMTPS TASPPSYNSV TKSDKDKYEK ENREKENKGK DLKERKK
//
