ID M3ZJ55_XIPMA Unreviewed; 1728 AA.
AC M3ZJ55;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000002247.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000002247.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000002247.2};
RG Ensembl;
RL Submitted (NOV-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; 8083.ENSXMAP00000002247; -.
DR Ensembl; ENSXMAT00000002252.2; ENSXMAP00000002247.2; ENSXMAG00000002228.2.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000156263; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR InParanoid; M3ZJ55; -.
DR OMA; YNDSNFY; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000002852};
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 134..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 233..254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 393..420
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 527..553
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 565..583
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 645..670
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 729..755
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 942..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 981..1000
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1058..1084
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1183..1207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1269..1287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1299..1321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1333..1352
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1396..1421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1442..1461
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1489..1512
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1529..1564
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 417..455
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 21..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1728 AA; 197454 MW; 8180ABA051F64A3A CRC64;
MAAPLLAPPG PDSFKKFTPE SLANIEKRIQ EEKNKKPPKP RSDSSHRDTS DDNEPKPNSD
LEAGKSLPFI YGDIPDGMAA TPLEDLDPYY LNQKTFIVLN KGKTIFRFSA TPSLYIISPF
NPFRRIAIKI LIHSYPFTSL IMIIMCTILT NCIFMTFSDP PEWSKQVEYT FTGIYTFESL
TKIVARGFAI DGFTFLRDPW NWLDFMVISM AYITEFVDLG NVSALRTFRV LRALKTISVI
PGLKTIVGAL IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCVFW PINMTEQYLE
NGSRGFDWNK YIYNDSNFYF LPGALDALLC GNSSDSGRCP EGFTCMKAGR NPNYGYTSFD
SFGWAFLTLF RLMTQDFWEN LYMLTLRAAG KTYMVFFVLV IFVGSFYLVN LILAVVAMAY
EEQNQATMEE AEQKEAEFKA MLEQLKKQQE ETQVRKRNST VDCNGVVSLI GPGPGRRLLP
EVKIDKAATD DKLEESQRKC PPCWYKFANI FLIWECCPIW LKIKHIVYLI VMDPFVDLAI
TICIVLNTLF MAMEHYPMTP HFEEVLSVGN LVFTGIFAGE MFAKLIAMDP YYYFQEGWNC
FDGFIVTLSL VELGLADVEG LSVLRNMRLF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL
AIIVFIFAVV GMQLFGKSYK DCVCKIALDC ELPRWHMNDF FHSFLIVFRV LCGEWIETMW
DCMEVAGQAM CIIVFMMVMV IGNLVVLNLF LALLLSSFSA DNLAATDDDG EPNNLQLAVA
RIKIGIAWFK ANMRILQPIE DEQKPLDYEE KLNCIANHPA EINRELDYPK NGNGTTSGIG
SSVGKYMIDD DYMSFIHNPN LTVCVPIAVG ESDFENLNTE DFSSESDVEN SKDVSRNGCR
VFINHAECVA KYKCCDVPIT HGWGKHWWFL RKTCYLIVEH NWFETLIIFM ILLSSGALAF
EDVYIEQRKT VRIILDYADR VFTYIFILEM LLKWVAYGFV KYFTNAWCWL DFFIVDVSIV
SLIANALGFS DLGPIKSLRT LRALRPLRAL SRFEGMRVVV NALVGAIPSI MNVLLVCLIF
WLIFSIMGVN LFAGKYYYCF NETAEEYFLP DDVNNKTECF ELINSNHTEV RWKNVKINFD
NVGAGYLALL QVATFKGWMD IMYAAIDSRK VEDQPVYEDN LYMYIYFVIF IIFGSFFTLN
LFIGVIIDNF NQQKKKIRTI FFTFTFSEKE QKKYYNAMKK LGSKKPQKPI PRPQNPIQGM
VFDFVTQQVF DISIMILICL NMVTMMVETD DQSEETEVVL YWVNFVFIVV FTGEFLLKLF
ALRHYYFTNG WNIFDVVVVI LSIVGMFLAD LIEKYFVSPT LFRVIRLARI GRILRLIKGA
KGIRTLLFAL MMSLPALFNI GLLLFLVMFI FSIFGMSNFG YVKHGAGIDD MYNFETFGNS
MIILFMITTS AGWDGLLLPI LNYPPDCDPL LENAGTPATG NCGNPSVGIF FFVMYIIISF
LIVVNMYIAI ILENFSVATE ESADPLSEDD FETFYEIWEK FDPDASQFIT YAKLSDFADA
LEHPLRVPKP NTIELIAMDM PMVSGDRIHC LDILFAFTKR VLGDSGELDM LRQQMEERFV
AANPSKVSYE PITTTLRRKQ EDVSARIIQR AYRSHLARRG FVCKRKPANN KAENQEQEKK
EGTPSTASLP SYDSVTKPEK EKQDDNNEGK GERKEKGRNQ KDIRESQC
//
