ID A0A2U9CYI8_SCOMX Unreviewed; 1975 AA.
AC A0A2U9CYI8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN ORFNames=SMAX5B_009684 {ECO:0000313|EMBL:AWP21110.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP21110.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP21110.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CP026263; AWP21110.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000015217; -.
DR Proteomes; UP000246464; Chromosome 21.
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; 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:SF295; SODIUM CHANNEL PROTEIN; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR SMART; SM00015; IQ; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion channel {ECO:0000256|RuleBase:RU361132, ECO:0000313|EMBL:AWP21110.1};
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:UP000246464};
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 112..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 220..237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 344..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 383..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 712..730
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 762..780
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 816..839
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 894..919
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1144..1162
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1183..1201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1260..1286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1383..1406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1465..1483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1495..1513
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1520..1545
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1582..1610
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1686..1709
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 125..416
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 509..661
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 711..926
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 933..1138
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1142..1415
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1464..1719
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1010..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 407..441
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1029..1069
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1975 AA; 223847 MW; 63DB43E8BF0CB41E CRC64;
MAGCVFPMGP ESFQRFTPDS LAAIEQRIAQ ERARRSKHYQ EDLGDVELLR RRPDLEAGKQ
LPRIFADIPS HLVGVPLEDI DPYYFKKKRV GHSARLCVCV CVCVCVCVHV CAYVSVCVCV
CVCVLFIMCT ILTNCCFMAM SEPAYWAKYL EYTFTGIYTF ESLIKILARG FCVGPFTFLR
DPWNWLDFSV IVMAYVTEFV DLGNVSALRT FRVLRALKTI SVIPGLKTIV GALIQSVKKL
ADVMILTVFC LSVFALIGLQ LFMGNLRQKC VRSAAHCVND SLPANTSFYC NNKTWASMKD
FVNDEDNFYK AEGAKDALIC GNSSDAGKCP DGFECLKAGK NPNYGYTSFD TFGWAFLSLF
RLMTQDYWEN LYHQTLRSAG KTYMVFFVVV IFLGSFYLVN LILAVVAMAY EEQNQATIAE
ASQKEREFHQ AMERLKKEQQ VAAQKDSLVS PDLSPFGPPL DTLEERRRSQ ALVGVADVES
NLSEEKLLQV DMADGGKPLH PLLARSFSSR TRRSSQVSSI FNFRLRSRGS DGEMADDEYS
VPGDVVDGVG GRTYSGGTFS GILPHPWPKR RPSTYSTTSR SSQVFYPTLN INGKLFVAMD
QNGVSPPPIP PLQGQLPACT MEKVKEESVP TSSTELSTML LPRPSSTHDP ERRGRALSAA
SYLTDAMEEL EEAHKRCHPC WYTFAHRYLV WQCSAPWLRA KQLVNVMVMD PFLDLAITVC
IVLNTLFMAM EHYPMTDEFN GMLSIGNLVL LEEKHTSVFD SLLFFFHSSV CVLISFKLLL
GKSRLSLSSQ LRVFKLARSW PTLNTLIKII GNSMGALGNL TLVLAIIVFI FAVVGMQLFG
KNYQDCVCKI SKDCALPRWH MKDFFHSFLI VFRVLCGEWI ETMWDCMEVA GQPLCILVFM
LVMVIGNLVL LNLFLALLLS SFSSDNLSAP DDDGEMNNLH IALHRITRGL AWCRRQVVDF
FNGNLKRRRQ KRKEAKAMMK LKRLSTIHTE VNGAVIGRHV EKYVVPEDDS YMTNPNLTIS
VPIAPGESDV EFPEEEDEEE EEEDEEDEEE EEEEQNEGSE EEEEREEQKD DVSLSEGSTV
DLRKPGEEED EYSEMAEEAM DPDNCFPDMC VSRFRCCDVD TTGRLGQTWW RLRKTCYQIV
EHSWFESFII FMILLSSGAL AFEDIYIEKR KVVKVVLEYA DKIFTYIFIL EMLLKWLAYG
FKKYFTNYWC WLDFLIVDVS LVSLVANTLG YSDFAAIKSL RTLRALRPLR ALSRFEGMRV
VVNALIGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFGR CVNRTGHIYD AAFINNKSEC
EALNDTSLYY WTKVKVNFDN VGAGYLALLQ VATFKGWMEI MYAAVDSRAV EEQPIKEINL
YMYLYFVIFI IFGSFFTLNL FIGVIIDNFN QQKRKMRGQD IFMTEEQKKY YNAMKKLGSK
KPQKPIPRPL NPLHGFFFDL AGKQAFDIII MVLILFNMIT MMVETDEQSP QMEYILNNIN
LAFIIVFTAE CLVKIVALRC YFFTVGWNIF DFVVVILSVV GIVLADIIEK YFVSPTLFRV
IRLARIGRIL RLIRGAKGIR TLLFALMMSL PALFNIGLLL FLVMFIYAIF GMANFAYVKR
QAGIDDMFNF ETFGNSMICL FQITTSAGWD GLLSPILNNS PEECNPNIPH TGTTVRGNCG
NPSVGITFFV TYIIISFLIV VNMYIAIILE NFSVATEEST EPLSEDDFEM FYEVWEKFDP
EATQFIEYAK LSDFADSLSE PLRIAKPNKI KLITMDLPMV SGDKIHCLDI LFAFTKRVLG
ESGEMDALKQ QMEEKFMMAN PSKISYEPIT TTLRRKQEEV SATVIQRCYR RHLVRRQMKA
ASYLYRQITT PRHAGGVSEE GGEGMFGEDA PEKEGLIAAM MKENYGSSLV EMEQSETISS
TSSPPSYDSV TRATSEVFHP LAANXGTVVV DTAESEASEQ SPAAADRDRR QETVP
//
