ID I6NKP6_TRIAD Unreviewed; 1947 AA.
AC I6NKP6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:AEX00065.1};
RN [1] {ECO:0000313|EMBL:AEX00065.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22854023;
RA Gur Barzilai M., Reitzel A.M., Kraus J.E., Gordon D., Technau U.,
RA Gurevitz M., Moran Y.;
RT "Convergent evolution of sodium ion selectivity in metazoan neuronal
RT signaling.";
RL Cell Rep. 2:242-248(2012).
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; HQ877452; AEX00065.1; -; mRNA.
DR SMR; I6NKP6; -.
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; 1.20.120.350; 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; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF62; SODIUM CHANNEL PROTEIN 60E; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00170; NACHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50096; IQ; 1.
PE 2: Evidence at transcript level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion channel {ECO:0000256|RuleBase:RU361132, ECO:0000313|EMBL:AEX00065.1};
KW Ion transport {ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
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}; Transport {ECO:0000256|RuleBase:RU361132};
KW Voltage-gated channel {ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 96..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 160..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 215..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 346..372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 643..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 681..703
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 842..865
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1210..1228
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1248..1271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1277..1301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1322..1347
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1440..1469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1529..1549
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1561..1580
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1592..1610
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1651..1676
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1747..1772
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 95..376
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 643..872
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1208..1473
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1529..1782
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 502..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1947 AA; 221089 MW; 888451283F6C1A8B CRC64;
MDQGYGHVIS VNTPDYEDWK DFNQNRKCIN EQIKKNHLTG KLVKDFDQQQ TDTVCLLTKR
MNSYYVYRYN TSNSLHLFPP NNPIRLITMR ITSNQFFDLF IFIAIFINCV LMAFPNGIDP
SIEITFNTIY TVEMLLKIMA RGFIFHTYAY LRDPWNWLDF IVVIVGYLTM IPALSVLPGA
SVIRVLRALR MITALEGLKA IVNALFKSFR MLADVFCLAL FILIIFALIG VQLFMGILTQ
KCCRPFNSTG DIVEPFTMTK FKNYVNVSSN WYFENGDPVI CGNESSARHC PVDYLCYQYA
YPNPNDGFTS FDNFPVSLLV SFQLITLDNW EDIYNKVNDA IDSWCIIYFI PVVLLGAFYV
MNLVIAIVAM AYNKEDKILQ DQKCDIRHMR ESYRNSTVFI FFENEIPKLW IPKIGSNPYG
NGHVLKIRNQ KGVLSSRSEG DIEMNLMKGR NGYNEENFKK LGKNIGKPEQ IPKGNHIDQG
SLKNKEGKIN IISLKISAAI DDPAKMQPHE GNSSSTKIEN TALDNPINEN RKTSRSARHS
ALSRSDGEID RIKPNVVSVS HTFTSKLSAA NKIGNNGEIN GKSPSTLMKK REKVIRLVPE
GGQSSGSATV TTVSIVLNAE TTSTKSTIWR QIRVLVGRIV DDSLFELFIT GCIILNTVLM
SMYQPLEEYN SKVPAQNIDN YVFTCIFTTE MTLKLIAFGF TGYIQSKWNV FDGIVVIISL
VDLLLEFISI SSNSLSVLRT LRLLRVFKLA RSWTTMRRLL STIVSGAKAL LYILLILILT
IYVFAVLGMK IFRDAYRKHF ENLPRWNFDD FIDSFMMIFR ILCGEWIEPL YDAIQATNIS
SILFFLAAYV VGKLLVLHLF LALLLSSFEN QSFQEAYSDN SGSQKNNGNL YDALRYLIVT
LRLNKLWNYT FARILPQKKT KPKCPKLESA GNVNLASSNY NPQILQHTEI LKDENNRNGL
DEINTLSRSI TEEKISTSAN NGKGQSSSKG PKLLVEYNES ALVSDQPQRK KSANHREVRN
TLSDGDAHSA CDYNYNQEKK QRSLNQTQED DSDYLDLQRT LGLLVPDQID DESDSGQIID
KRNYLSVRRA SSRRKSMTQS TSSIFDSNSR DVSSDYIYCE TPNVSRQDSV RSDSQCTDTE
ANNSVGMKAM SNTSCNGGLQ YSERSISQPI DCFPKVCMKR IPYCIQGETS LCQAWMTVRS
HVKNVVEHRF FEGIILLLIV ASSISLTFED IHLHKNPTLI QVLYVSNIFF AAAFSIEMIL
KLIGIGVHGY ICSPWNILDA AIVVVSIITL VLENVSAFRS LRVLRALRPL RAISHWEGMR
AVVNALFGCI PHITNVIIVC AFFWLVFCVG GVNFFGGKFY KCLDLDNNLI PASIISNKTD
CLANNYIWKN SQINFDSVPQ AFLALFEVAT FEGWIQVMGD AVDAREIDQQ PIPLNNKSAY
IYFVAFIIIG SFFSLNLIVS VIIDCFYALK QKSESGSLGI PTDLFMTESQ KRWYNVMKTM
SKSKPVRRIP LPKRDSQKRL LAIVQSNKFE LAIILVIVAN TAAMMVVHFD QSQEVTRVLD
TLNYIFTAIY VLEAILKIIA MRQHYFKNLW NLFDFIIVLV AIIGIILDVM DNSNASIPIN
PSMLRTLRLF RIVRILRVLE FAKGIRKLLT AFAMSMPALF NVALLVFLVM FIYAIVGMSS
FAYVKHQTAI TKNMNFETFP NGLLLLFRLS TSAGWNDVLH DLMVQPPDCN NSATAFSWNG
DCGNPPVAIT FLITYIFITT FVLINMYVAI ILNNYQEVEE EEEGSVITAE DINVFYETWA
KYDPEASQFI SFRYLSPLVA ELKPPLRIPQ PNKYPLIALD LALYDSRLVH CLDVLEALVE
RVIGQPNADE AGDVVEEIKR QIQKKFSETF PSSGIPKQYD KSKRLKQLAV QEIKAAVIIQ
RAYRHYRLRK ACKEHSQRMR RQSAIHL
//
