ID G3TWG4_LOXAF Unreviewed; 1917 AA.
AC G3TWG4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN2A {ECO:0000313|Ensembl:ENSLAFP00000019922.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000019922.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000019922.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019922.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000019922.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019922.1};
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}.
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; ENSLAFT00000030237.1; ENSLAFP00000019922.1; ENSLAFG00000001625.4.
DR GeneTree; ENSGT00940000154224; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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: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 SMART; SM00015; IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
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:UP000007646};
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 125..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 224..245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 388..415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 712..736
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 748..769
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 831..859
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 921..944
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1146..1164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1185..1207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1213..1233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1262..1288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1386..1410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1469..1487
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1499..1517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1524..1549
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1586..1614
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1690..1713
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 128..421
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 509..670
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 720..951
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 958..1140
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1144..1419
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1468..1723
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 28..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 412..450
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1873..1897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1917 AA; 218199 MW; 728B3846F71B8ADD CRC64;
MAQSVLVPPG PDSFRFFTRE SLAAIEQRIA EEKAKRPKQE RKDEDDENGP KPNSDLEAGK
SLPFIYGDIP PEMVSEPLED LDPYYINKKT FIVLNKGKAI SRFSATPALY ILTPFNPIRK
LAIKILIHSL FNVLIMCTIL TNCVFMTMSN PPDWTKNVEY TFTGIYTFES LIKILARGFC
LEDFTFLRDP WNWLDFTVIT FAYVTEFVNL GNVSALRTFR VLRALKTISV IPGLKTIVGA
LIQSVKKLSD VMILTVFCLS VFALIGLQLF MGNLRNKYIT SFFSSSLDVN GTIINRTVSM
FNWDEYIEDK SHFYFLEGQN DALLCGNSSD AGQCPEGYIC VKAGRNPNYG YTSFDTFSWA
FLSLFRLMTQ DFWENLYQLT LRAAGKTYMI FFVLVIFLGS FYLINLILAV VAMAYEEQNQ
ATLEEAEQKE AEFQQMLEQL KKQQEEAQVE STFTVLKSSS VVSKLRFRKS ESEDSIRRKG
FRFSLEWLLE AKLPKDRQEN ENQGMNHISL LSIRGSLFSP RRNSRASLFS FRGRAKDIGS
ENDFADDEHS TFEDNDSRRD SLFVPHRHGE RRHSNVSQAS RASRVLPILP MNGKMHSAVD
CNGVVSLVGG PSALTSPIGQ LLPEDLLQTG ANSGTTTETE IRKRRSSSYH VSMDLLEDPT
AKQRAMSMAS ILTNTMEELE ESRQKCPPCW YKFANMCLIW DCCKPWLKVK HLVNLVVMDP
FVDLAITICI VLNTLFMAME HYPMTEQFSN VLSVGNLVFT GIFTAEMFLK IIAMDPYYYF
QEGWNIFDGF IVSLSLMELG LANVEGLSVL RSFRLLRVFK LAKSWPTLNM LIKIIGNSVG
ALGNLTLVLA IIVFIFAVVG MQLFGKSYKE CVCKISSDCE LPRWHMHDFF HSFLIVFRVL
CGEWIETMWD CMEVAGQTMC LTVFMMVMVI GNLVVLNLFL ALLLSSFSSD NLAATDDDNE
MNNLQIAVGR MQKGIDYVKR NIREFIQKAF VRKQKALDLN NKKDSCISNH TTVEISSSVE
KYVVDESDYM SFINNPSLTV TVPIAVGESD FENLNTEEFS SESDMEESKE KLNATSSSEG
STVDIGAPAE GEQPEAEPEE SLEPEACFTE DCVRKFKCCQ ISIEEGKGKL WWNVRKTCYK
IVEHNWFETF IVFMILLSSG ALAFEDIYIE QRKTIKTMLE YADKVFTYIF ILEMLLKWVA
YGFQMYFTNA WCWLDFLIVD VSLVSLTANA LGYSELGAIK SLRTLRALRP LRALSRFEGM
RVVVNALLGA IPSIMNVLLV CLIFWLIFSI MGVNLFAGKF YHCINYTTGE MFDVSVVNNY
SECKALIESN QTARWKNVKV NFDNVGLGYL SLLQVATFKG WMDIMYAAVD SRNVELQPKY
EDNLYMYLYF VIFIIFGSFF TLNLFIGVII DNFNQQKKKF GGQDIFMTEE QKKYYNAMKK
LGSKKPQKPI PRPANKFQGM VFDFVTKQVF DISIMILICL NMVTMMVETD DQSQEMTNIL
YWINLVFIVL FTGECVLKLI SLRYYYFTIG WNIFDFVVVI LSIVGMFLAE LIEKYFVSPT
LFRVIRLARI GRILRLIKGA KGIRTLLFAL MMSLPALFNI GLLLFLVMFI YAIFGMSNFA
YVKREVGIDD MFNFETFGNS MICLFQITTS AGWDGLLAPI LNSGPPDCDP EKDHPGSSVK
GDCGNPSVGI FFFVSYIIIS FLVVVNMYIA VILENFSVAT EESAEPLSED DFEMFYEVWE
KFDPDATQFI EFSKLSDFAA ALDPPLLIAK PNKVQLIAMD LPMVSGDRIH CLDILFAFTK
RVLGESGEMD ALRIQMEERF MASNPSKVSY EPITTTLKRK QEEVSAIVIQ RAYRRYLLKQ
KVKKVSCICK KDKGKEGDGT PIKEDTLIDK LHENSTPEKT DVTPSTTSPP SYDSVTK
//