ID F6ZAN9_MACMU Unreviewed; 1842 AA.
AC F6ZAN9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN3A {ECO:0000313|Ensembl:ENSMMUP00000024795.4,
GN ECO:0000313|VGNC:VGNC:76985};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000024795.4, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000024795.4}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000024795.4};
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 SMR; F6ZAN9; -.
DR Ensembl; ENSMMUT00000026491.4; ENSMMUP00000024795.4; ENSMMUG00000018840.4.
DR VEuPathDB; HostDB:ENSMMUG00000018840; -.
DR VGNC; VGNC:76985; SCN3A.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000157130; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR TreeFam; TF323985; -.
DR Proteomes; UP000006718; Chromosome 12.
DR Bgee; ENSMMUG00000018840; Expressed in prefrontal cortex and 13 other cell types or tissues.
DR ExpressionAtlas; F6ZAN9; baseline.
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; 3.
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:UP000006718};
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 92..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 242..269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 603..621
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 633..656
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 713..741
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 803..826
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1049..1067
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1088..1110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1165..1191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1286..1310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1369..1387
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1399..1417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1429..1449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1486..1514
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1590..1613
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 49..275
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 400..552
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 602..833
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 840..1042
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1047..1319
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1368..1623
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 334..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1791..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 266..307
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 339..353
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1815..1842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1842 AA; 208421 MW; 9FDE102C58979099 CRC64;
MELAGFQCHC DGVCNRICKP RQCFSPSNFQ SLESSENYFC NSRYVTEFVD LGNVSALRTF
RVLRALKTIS VIPGLKTIVG ALIQSVKKLS DVMILTVFCL SVFALIGLQL FMGNLRNKCL
QWPPSDSAFE TNTTSYFNGT MDSNRTFVNV TMSTFNWKDY IGDDSHFYVL DGQKDPLLCG
NGSDAGQCPE GYICVKAGRN PNYGYTSFDT FSWAFLSLFR LMTQDYWENL YQLTLRAAGK
TYMIFFVLVI FLGSFYLVNL ILAVVAMAYE EQNQATLEEA EQKEAEFQQM LEQLKKQQEE
AQAVAAASAA SRDFSGIGGL GELLESSSEA SKLSSKSAKE WRNRRKKRRQ REHHGGNNKG
EKDSFPKSES EDSVKRSSFL FSMDGNRLTS DKKFCSPHQS LLSIRGSLFS PRRNSKTSIF
SFRGRAKDVG SENDFADDEH STFEDSESRR DSLFVPHRHG ERRNSNVSQA SMSSRMVPGL
PANGKMHSTV DCNGVVSLVG GPSALTSPTG QLLPEGTTTE TEIRKRRLSS YQISMEMLED
SSGRQRAMSI ASILTNTMEE LEESRQKCPP CWYRFANVFL IWDCCDAWLK VKHLVNLIVM
DPFVDLAITI CIVLNTLFMA MEHYPMTEQF SSVLTVGNLV FTGIFTAEMV LKIIAMDPYY
YFQEGWNIFD GIIVSLSLME LGLSNVEGLS VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS
VGALGNLTLV LAIIVFIFAV VGMQLFGKSY KECVCKINDD CTLPRWHMND FFHSFLIVFR
VLCGEWIETM WDCMEVAGQT MCLIVFMLVM VIGNLVVLNL FLALLLSSFS SDNLAATDDD
NEMNNLQIAV GRMQKGIDYV KNKIRECFRK AFFRKPKVIE IHEGNKIDSC MSNNTGIEIS
KELNYLRDGN GTTSGVGTGS SVEKYVIDEN DYMSFINNPS LTVTVPIAVG ESDFENLNTE
EFSSESELEE SKEKLNATSS SEGSTVDVAL PREGEQAEIE PEEDLKPEAC FTEGCIKKFP
FCQVSTEEGK GKIWWNLRKT CYSIVEHNWF ETFIVFMILL SSGALAFEDI YIEQRKTIKT
MLEYADKVFT YIFILEMLLK WVAYGFQTYF TNAWCWLDFL IVDVSLVSLV ANALGYSELG
AIKSLRTLRA LRPLRALSRF EGMRVVVNAL VGAIPSIMNV LLVCLIFWLI FSIMGVNLFA
GKFYHCVNMT TGNMFDVSDV NNLSDCQALG KQARWKNVKV NFDNVGAGYL ALLQVATFKG
WMDIMYAAVD SRDVTLQPMY EENLYMYLYF VIFIIFGSFF TLNLFIGVII DNFNQQKKKF
GGQDIFMTEE QKKYYNAMKK LGSKKPQKPI PRPANKFQGM VFDFVTRQVF DISIMILICL
NMVTMMVETD DQGKYMTLVL SRINLVFIVL FTGEFVLKLV SLRHYYFTIG WNIFDFVVVI
LSIVGMFLAE MIEKYFVSPT LFRVIRLARI GRILRLIKGA KGIRTLLFAL MMSLPALFNI
GLLLFLVMFI YAIFGMSNFA YVKKEAGIDD MFNFETFGNS MICLFQITTS AGWDGLLAPI
LNSAPPDCDP DTIHPGSSVK GDCGNPSVGI FFFVSYIIIS FLVVVNMYIA VILENFSVAT
EESAEPLSED DFEMFYEVWE KFDPDATQFI EFSKLSDFAA ALDPPLLIAK PNKVQLIAMD
LPMVSGDRIH CLDILFAFTK RVLGESGEMD ALRIQMEDRF MSSNPSKVSY EPITTTLKRK
QEEVSAAIIQ RNFRCYLLKQ RLKNISNNYN KEAIKGRIDL PIKQDMIIDK LNGNSTPEKS
DGSSSTTSPP SYDSVTKPDK EKFEKDKPEK ESKVKEVREN QK
//
