ID F7ISP2_CALJA Unreviewed; 1993 AA.
AC F7ISP2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN3A {ECO:0000313|Ensembl:ENSCJAP00000011222.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000011222.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000011222.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000011222.4}
RP IDENTIFICATION.
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 Ensembl; ENSCJAT00000011842.4; ENSCJAP00000011222.4; ENSCJAG00000006101.5.
DR GeneTree; ENSGT00940000157130; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR OMA; CDAWLKI; -.
DR Proteomes; UP000008225; Chromosome 6.
DR Bgee; ENSCJAG00000006101; Expressed in frontal cortex and 3 other cell types or tissues.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
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 GO; GO:0048266; P:behavioral response to pain; IEA:Ensembl.
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:SF237; SODIUM CHANNEL PROTEIN TYPE 3 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; 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:UP000008225};
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 244..264
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 394..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 755..773
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 785..808
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 865..893
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 955..978
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1201..1219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1240..1262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1268..1288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1317..1343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1438..1462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1520..1538
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1550..1568
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1580..1600
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1637..1665
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1741..1764
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 149..427
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 552..704
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 754..985
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 992..1194
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1199..1471
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1519..1774
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1942..1993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 418..459
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 19..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1942..1965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1966..1993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1993 AA; 225997 MW; 11DE6743C7061E62 CRC64;
MAQALLVPPG PESFRLFTRE SLAKPKKEQD NDDENKPKPN SDLEAGKNLP FIYGDIPPEM
VSEPLEDLDP YYINKKTFIV MNKGKAIFRF SATSALYILS PLNPVRKIAI KILEKYFNEL
KTHKRIGFAM IENIYFNSSN RIVNFGLNVF LRYTFTGIYT FESLIKILAR GFCLEDFTFL
RDPWNWLDFS VIVMAYVTEF VDLGNVSALR TFRVLRALKT ISVIPGLKTI VGALIQSVKK
LSDVMILTVF CLSVFALIGL QLFMGNLRNK CLQWPPSDSA FEINTTSYFN GTMDSNGTFV
NVTMSTFNWK DYIGDDSHFY VLDGQKDPLL CGNGSDAGQC PEGYICVKAG RNPNYGYTSF
DTFSWAFLSL FRLMTQDYWE NLYQLTLRAA GKTYMIFFVL VIFLGSFYLV NLILAVVAMA
YEEQNQATLE EAEQKEAEFQ QMLEQLKKQQ EEAQAVAAAS AASRDFSGIG GLGELLESSS
EASKLSSKSA KEWRNRRKKR RQREHLEGNN KGERDSFPKS ESEDSVKRSS FLFSMDGNRL
TSDKKFCSPH QSLLSIRGSL FSPRRNSKTS IFSFRGRAKD VGSENDFADD EHSTFEDSES
RRDSLFVPHR HGERRNSNVS QASMSSRMVP GLPANGKMHS TVDCNGVVSL VGGPSALTSP
TGQPLPEGTT TETEVRKRRL SSYQISMEML EDSSGRQRAM SIASILTNTM EELEESRQKC
PPCWYRFANM FLIWDCCDAW LKVKHLVNLI VMDPFVDLAI TICIVLNTLF MAMEHYPMTE
QFSSVLTVGN LVFTGIFTAE MVLKIIAMDP YYYFQEGWNI FDGIIVSLSL MELGLSNVEG
LSVLRSFRLL RVFKLAKSWP TLNMLIKIIG NSVGALGNLT LVLAIIVFIF AVVGMQLFGK
SYKECVCKIN DDCTLPRWHM NDFFHSFLIV FRVLCGEWIE TMWDCMEVAG QTMCLIVFML
VMVIGNLVVL NLFLALLLSS FSSDNLAATD DDNEMNNLQI AVGRMQKGID YVKNKIRECF
RKAFFRKPKV IEIHEGNKID SCMSNNTGIE ISKEFNYLRD GNGTTSGVGT GSSVEKYVID
ENDYMSFINN PSLTVTVPIA VGESDFENLN TEEFSSESEL EESKEKLNAT SSSEGSTVDV
ALPREGEQAE IEPEEDLKPE ACFTEGCIKK FPFCQVSTEE GKGKIWWNLR KTCYSIVEHN
WFETFIVFMI LLSSGALAFE DIYIEQRKTI KTMLEYADKV FTYIFILEML LKWVAYGFQT
YFTNAWCWLD FLIVDVSLVS LVANALGYSE LGAIKSLRTL RALRPLRALS RFEGMRVVVN
ALVGAIPSIM NVLLVCLIFW LIFSIMGVNL FAGKFYHCVN MTTGNMFNVS EVNNFSDCQA
LGKQARWKNV KVNFDNVGAG YLALLQVATF KGWMDIMYAA VDSRDVKLQP LYEDNLYMYL
YFVIFIIFGS FFTLNLFIGV IIDNFNQQKK KISQDIFMTE EQKKYYNAMK KLGSKKPQKP
IPRPANKFQG MVFDFVTRQV FDISIMILIC LNMVTMMVET DDQGKYMTLV LSRINLVFIV
LFTGEFVLKL VSLRHYYFTI GWNIFDFVVV ILSIVGMFLA EMIEKYFVSP TLFRVIRLAR
IGRILRLIKG AKGIRTLLFA LMMSLPALFN IGLLLFLVMF IYAIFGMSNF AYVKKEAGID
DMFNFETFGN SMICLFQITT SAGWDGLLAP ILNSAPPDCD PDTIHPGSSV KGDCGNPSVG
IFFFVSYIII SFLVVVNMYI AVILENFSVA TEESAEPLSE DDFEMFYEVW EKFDPDATQF
IEFSKLSDFA AALDPPLLIA KPNKVQLIAM DLPMVSGDRI HCLDILFAFT KRVLGESGEM
DALRIQMEDR FMASNPSKVS YEPITTTLKR KQEEVSAAII QRNFRCYLLK QRLKNISSNY
NKEAIKGRID LPIKQDMIID KLNGNSTPEK TDGSSSTTSP PSYDSVTKPD KEKFEKDKPE
KESKGKEVRE NQK
//
