ID A0A3B4WFJ2_SERLL Unreviewed; 1833 AA.
AC A0A3B4WFJ2;
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:ENSSLDP00000002655.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000002655.1}
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; ENSSLDT00000002765.1; ENSSLDP00000002655.1; ENSSLDG00000002051.1.
DR GeneTree; ENSGT00940000156263; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
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.
DR PROSITE; PS50222; EF_HAND_2; 1.
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}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1833
FT /note="Sodium channel protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017216618"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 213..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 252..279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 593..620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 632..650
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 712..740
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 802..825
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1046..1064
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1085..1104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1162..1188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1287..1311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1370..1388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1400..1422
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1434..1453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1497..1522
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1543..1562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1590..1613
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1630..1665
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 310..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1800..1833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1833 AA; 208290 MW; 6D50D57C83C56D78 CRC64;
MIIMCTILTN CIFMTFSDPP EWSKQVEYTF TGIYTFESLT KIVARGFCID GFTFLRDPWN
WLDFMVISMA YITEFVDLGN VSALRTFRVL RALKTISVIP GLKTIVGALI QSVKKLSDVM
ILTVFCLSVF ALIGLQLFMG NLRNKCVFWP INMTDQLLPN GSKGFDWATY IMNDTNFYFL
PDQLDALLCG NSSDSGRCPE GYTCMKAGRN PNYGYTSFDS FGWAFLTLFR LMTQDFWENL
YMLTLRAAGK TYMIFFVLVI FVGSFYLVNL ILAVVAMAYE EQNQATIEEA EQKEAEFKAM
LEQLRKQQEE TQAAAMATSA GTVSEAALED EGGGHLSRSS SEVSKLSSKS AKERRNRKKK
WRQKEQEKEK GDSEKVVKSE SDDGSKKSTI RFPGSRLGRK TSIMNQSLLS IPGSPFMSRH
NSRSSIFSFK GRSKDMGSEN EFADDEHSTV EESEDRRGSL FIPYRRNSYS GYSQGSSRIH
PLAPHSGGKR NSTVDCNGVV SLIGPGPGRR LLPETTDVEI KKKHSGSLMV SVDQLNSSFK
GKDRANSQMS VVTNTLIEEL EESQRKCPPC WYKFANVVLI WECCPIWLKI KHIVYLIVMD
PFVDLAITIC IVLNTLFMAM EHYPMTESFE EVLSVGNLVF TGIFAGEMFA KLIAMDPYYY
FQEGWNCFDG FIVTLSLVEL GLADVEGLSV LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV
GALGNLTLVL AIIVFIFAVV GMQLFGKSYK DCVCKIARDC ELPRWHMNDF FHSFLIVFRV
LCGEWIETMW DCMEVAGQSM CLIVFMMVMV IGNLVVLNLF LALLLSSFSA DNLAATDDDG
EPNNLQLAVA RIKTGIAWFK VNMRVFVATV LKKPIEDEQK PLDEMYEKKL NCIANHTVDI
NRELDYAKNG NGTTSGIGSS VGKYMIDEDY MSFIHNPNLT VCVPIAVGES DFENLNTEDF
SSESDVENSK DLDDTSSSEG STIDIKPDVE EVAVVEVVEE YLDPEPCWTD ECVAKYKCCD
VPITFGWGKH WWFLRKTCYL IVEHNWFETL IIFMILLSSG ALAFEDVYIE QRKTVRIILE
YADRVFTYIF ILEMLLKWVA YGFVKYFTNA WCWLDFFIVD VSIVSLIANA LGFSDLGPIK
SLRTLRALRP LRALSRFEGM RVVVNALVGA IPSIMNVLLV CLIFWLIFSI MGVNLFAGKY
YYCYNSTAEE NFLPDKVNNK TECFALINAN YTEVRWKNVK INFDNVGAGY LALLQVATFK
GWMDIMYAAI DSRKVEDQPV YEDNLYMYIY FVIFIIFGSF FTLNLFIGVI IDNFNQQKKK
FGGQDIFMTE EQKKYYNAMK KLGSKKPQKP IPRPQNNIQG MVFDFVTQQV FDISIMILIC
LNMVTMMVET DDQSEDTEVV LYWVNFIFIV IFTGEFLLKL FALRHYYFTN GWNIFDVVVV
ILSIVGMFLA DLIEKYFVSP TLFRVIRLAR IGRILRLIKG AKGIRTLLFA LMMSLPALFN
IGLLLFLVMF IFSIFGMSNF GYVKHGAGID DMYNFETFGN SMIILFMITT SAGWDGLLLP
ILNYPPDCDP LLENAGTPAT GDCGNPSVGI FFFVMYIIIS FLIVVNMYIA IILENFSVAT
EESADPLSED DFETFYEIWE KFDPDASQFI TYAKLSDFAD ALEHPLRVPK PNTIELIAMD
MPMVSGDRIH CLDILFAFTK RVLGDSGELD MLRQQMEERF VAANPSKVSY EPITTTLRRK
QEDVSARIIQ RAYRSYLARR GFVCKRKPAN NKVENGGNNQ EQEKKESTPS TASLPSYDSV
TKPDKEKQDD NNEGKGGRKE KGRNQKDIRE SKC
//
