Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Sodium channel protein type 9 subunit alpha (Neuroendocrine sodium channel) (hNE-Na) (Peripheral sodium channel 1) (PN1) (Sodium channel protein type IX subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.7)

 SCN9A_HUMAN             Reviewed;        1988 AA.
Q15858; A1BUH5; Q6B4R9; Q6B4S0; Q6B4S1; Q70HX1; Q70HX2; Q8WTU1;
Q8WWN4;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 3.
27-SEP-2017, entry version 164.
RecName: Full=Sodium channel protein type 9 subunit alpha {ECO:0000305};
AltName: Full=Neuroendocrine sodium channel {ECO:0000303|PubMed:7720699};
Short=hNE-Na {ECO:0000303|PubMed:7720699};
AltName: Full=Peripheral sodium channel 1;
Short=PN1 {ECO:0000250|UniProtKB:O08562};
AltName: Full=Sodium channel protein type IX subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.7;
Name=SCN9A {ECO:0000312|HGNC:HGNC:10597}; Synonyms=NENA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION IN VOLTAGE-EVOKED
DEPOLARIZATION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND
VARIANT ARG-1161.
TISSUE=Thyroid;
PubMed=7720699;
Klugbauer N., Lacinova L., Flockerzi V., Hofmann F.;
"Structure and functional expression of a new member of the
tetrodotoxin-sensitive voltage-activated sodium channel family from
human neuroendocrine cells.";
EMBO J. 14:1084-1090(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INVOLVEMENT IN CONGENITAL
INSENSITIVITY TO PAIN, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
VARIANT ARG-1161.
PubMed=17167479; DOI=10.1038/nature05413;
Cox J.J., Reimann F., Nicholas A.K., Thornton G., Roberts E.,
Springell K., Karbani G., Jafri H., Mannan J., Raashid Y.,
Al-Gazali L., Hamamy H., Valente E.M., Gorman S., Williams R.,
McHale D.P., Wood J.N., Gribble F.M., Woods C.G.;
"An SCN9A channelopathy causes congenital inability to experience
pain.";
Nature 444:894-898(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 136-674 (ISOFORMS 1; 2; 3 AND 4), AND
TISSUE SPECIFICITY.
TISSUE=Spinal ganglion;
PubMed=15302875; DOI=10.1074/jbc.M406387200;
Raymond C.K., Castle J.C., Garrett-Engele P.W., Armour C.D., Kan Z.G.,
Tsinoremas N.T., Johnson J.M.;
"Expression of alternatively spliced sodium channel alpha-subunit
genes: unique splicing patterns are observed in dorsal root ganglia.";
J. Biol. Chem. 279:46234-46241(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 150-264 AND 1340-1400.
Diss J.K.J., Fraser S.P., Coombes R.C., Djamgoz M.B.A.;
"Upregulation of voltage-gated Na+ channel expression and metastatic
potential in human breast cancer: correlative studies on cell lines
and biopsy tissues.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 840-958, AND VARIANTS PERYTHM
THR-859 AND HIS-869.
PubMed=14985375; DOI=10.1136/jmg.2003.012153;
Yang Y., Wang Y., Li S., Xu Z., Li H., Ma L., Fan J., Bu D., Liu B.,
Fan Z., Wu G., Jin J., Ding B., Zhu X., Shen Y.;
"Mutations in SCN9A, encoding a sodium channel alpha subunit, in
patients with primary erythermalgia.";
J. Med. Genet. 41:171-174(2004).
[7]
TISSUE SPECIFICITY.
PubMed=9169448; DOI=10.1074/jbc.272.23.14805;
Sangameswaran L., Fish L.M., Koch B.D., Rabert D.K., Delgado S.G.,
Ilnicka M., Jakeman L.B., Novakovic S., Wong K., Sze P., Tzoumaka E.,
Stewart G.R., Herman R.C., Chan H., Eglen R.M., Hunter J.C.;
"A novel tetrodotoxin-sensitive, voltage-gated sodium channel
expressed in rat and human dorsal root ganglia.";
J. Biol. Chem. 272:14805-14809(1997).
[8]
FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION, AND TISSUE SPECIFICITY.
PubMed=15178348; DOI=10.1016/j.febslet.2004.04.092;
Jo T., Nagata T., Iida H., Imuta H., Iwasawa K., Ma J., Hara K.,
Omata M., Nagai R., Takizawa H., Nagase T., Nakajima T.;
"Voltage-gated sodium channel expressed in cultured human smooth
muscle cells: involvement of SCN9A.";
FEBS Lett. 567:339-343(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, PHOSPHORYLATION AT SER-1490,
AND MUTAGENESIS OF SER-1490.
PubMed=25240195; DOI=10.1016/j.febslet.2014.09.011;
Tan Z.Y., Priest B.T., Krajewski J.L., Knopp K.L., Nisenbaum E.S.,
Cummins T.R.;
"Protein kinase C enhances human sodium channel hNav1.7 resurgent
currents via a serine residue in the domain III-IV linker.";
FEBS Lett. 588:3964-3969(2014).
[10]
SUBUNIT, AND INTERACTION WITH THE CONOTOXIN GVIIJ.
PubMed=24497506; DOI=10.1073/pnas.1324189111;
Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G.,
Wickenden A.D., Olivera B.M., Yoshikami D., Zhang M.M.;
"A disulfide tether stabilizes the block of sodium channels by the
conotoxin muO[section sign]-GVIIJ.";
Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
[11]
SUBUNIT, AND INTERACTION WITH THE SPIDER
BETA/DELTA-THERAPHOTOXIN-PRE1A.
PubMed=28428547; DOI=10.1038/s41598-017-01129-0;
Wingerd J.S., Mozar C.A., Ussing C.A., Murali S.S., Chin Y.K.,
Cristofori-Armstrong B., Durek T., Gilchrist J., Vaughan C.W.,
Bosmans F., Adams D.J., Lewis R.J., Alewood P.F., Mobli M.,
Christie M.J., Rash L.D.;
"The tarantula toxin beta/delta-TRTX-Pre1a highlights the importance
of the S1-S2 voltage-sensor region for sodium channel subtype
selectivity.";
Sci. Rep. 7:974-988(2017).
[12]
X-RAY CRYSTALLOGRAPHY (3.53 ANGSTROMS) OF 1527-1559 AND 1581-1622,
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=26680203; DOI=10.1126/science.aac5464;
Ahuja S., Mukund S., Deng L., Khakh K., Chang E., Ho H., Shriver S.,
Young C., Lin S., Johnson J.P. Jr., Wu P., Li J., Coons M., Tam C.,
Brillantes B., Sampang H., Mortara K., Bowman K.K., Clark K.R.,
Estevez A., Xie Z., Verschoof H., Grimwood M., Dehnhardt C.,
Andrez J.C., Focken T., Sutherlin D.P., Safina B.S., Starovasnik M.A.,
Ortwine D.F., Franke Y., Cohen C.J., Hackos D.H., Koth C.M.,
Payandeh J.;
"Structural basis of Nav1.7 inhibition by an isoform-selective small-
molecule antagonist.";
Science 350:0-0(2015).
[13]
CHARACTERIZATION OF VARIANTS PERYTHM THR-859 AND HIS-869, FUNCTION,
AND SUBCELLULAR LOCATION.
PubMed=15385606; DOI=10.1523/JNEUROSCI.2695-04.2004;
Cummins T.R., Dib-Hajj S.D., Waxman S.G.;
"Electrophysiological properties of mutant Nav1.7 sodium channels in a
painful inherited neuropathy.";
J. Neurosci. 24:8232-8236(2004).
[14]
VARIANT PERYTHM THR-241.
PubMed=16216943; DOI=10.1001/archneur.62.10.1587;
Michiels J.J., te Morsche R.H.M., Jansen J.B.M.J., Drenth J.P.H.;
"Autosomal dominant erythermalgia associated with a novel mutation in
the voltage-gated sodium channel alpha subunit Nav1.7.";
Arch. Neurol. 62:1587-1590(2005).
[15]
VARIANT PERYTHM VAL-1460, AND CHARACTERIZATION OF VARIANT PERYTHM
VAL-1460.
PubMed=15958509; DOI=10.1093/brain/awh514;
Dib-Hajj S.D., Rush A.M., Cummins T.R., Hisama F.M., Novella S.,
Tyrrell L., Marshall L., Waxman S.G.;
"Gain-of-function mutation in Nav1.7 in familial erythromelalgia
induces bursting of sensory neurons.";
Brain 128:1847-1854(2005).
[16]
VARIANTS PERYTHM SER-216; LYS-395; THR-859 AND PHE-869, AND VARIANT
ARG-1161.
PubMed=15955112; DOI=10.1111/j.0022-202X.2005.23737.x;
Drenth J.P., te Morsche R.H., Guillet G., Taieb A., Kirby R.L.,
Jansen J.B.;
"SCN9A mutations define primary erythermalgia as a neuropathic
disorder of voltage gated sodium channels.";
J. Invest. Dermatol. 124:1333-1338(2005).
[17]
VARIANT PERYTHM PHE-869, AND CHARACTERIZATION OF VARIANT PERYTHM
PHE-869.
PubMed=16392115; DOI=10.1002/ana.20776;
Han C., Rush A.M., Dib-Hajj S.D., Li S., Xu Z., Wang Y., Tyrrell L.,
Wang X., Yang Y., Waxman S.G.;
"Sporadic onset of erythermalgia: a gain-of-function mutation in
Nav1.7.";
Ann. Neurol. 59:553-558(2006).
[18]
CHARACTERIZATION OF VARIANT PERYTHM SER-216, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=16988069; DOI=10.1212/01.wnl.0000231514.33603.1e;
Choi J.S., Dib-Hajj S.D., Waxman S.G.;
"Inherited erythermalgia: limb pain from an S4 charge-neutral Na
channelopathy.";
Neurology 67:1563-1567(2006).
[19]
VARIANTS PEPD CYS-1007; PHE-1309; ASP-1309; PHE-1310; THR-1472;
VAL-1473; ILE-1475 AND LYS-1638, CHARACTERIZATION OF VARIANTS PEPD
THR-1472; ILE-1475 AND LYS-1638, AND FUNCTION.
PubMed=17145499; DOI=10.1016/j.neuron.2006.10.006;
Fertleman C.R., Baker M.D., Parker K.A., Moffatt S., Elmslie F.V.,
Abrahamsen B., Ostman J., Klugbauer N., Wood J.N., Gardiner R.M.,
Rees M.;
"SCN9A mutations in paroxysmal extreme pain disorder: allelic variants
underlie distinct channel defects and phenotypes.";
Neuron 52:767-774(2006).
[20]
CHARACTERIZATION OF VARIANT PERYTHM HIS-869.
PubMed=16702558; DOI=10.1073/pnas.0602813103;
Rush A.M., Dib-Hajj S.D., Liu S., Cummins T.R., Black J.A.,
Waxman S.G.;
"A single sodium channel mutation produces hyper- or hypoexcitability
in different types of neurons.";
Proc. Natl. Acad. Sci. U.S.A. 103:8245-8250(2006).
[21]
VARIANT PERYTHM GLU-1643, CHARACTERIZATION OF VARIANT PERYTHM
GLU-1643, VARIANT PEPD GLU-1643, AND CHARACTERIZATION OF VARIANT PEPD
GLU-1643.
PubMed=18945915; DOI=10.1523/JNEUROSCI.3443-08.2008;
Estacion M., Dib-Hajj S.D., Benke P.J., Te Morsche R.H., Eastman E.M.,
Macala L.J., Drenth J.P., Waxman S.G.;
"NaV1.7 gain-of-function mutations as a continuum: A1632E displays
physiological changes associated with erythromelalgia and paroxysmal
extreme pain disorder mutations and produces symptoms of both
disorders.";
J. Neurosci. 28:11079-11088(2008).
[22]
VARIANT PERYTHM ARG-10, CHARACTERIZATION OF VARIANTS PERYTHM ARG-10
AND THR-859, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19369487; DOI=10.1093/brain/awp078;
Han C., Dib-Hajj S.D., Lin Z., Li Y., Eastman E.M., Tyrrell L.,
Cao X., Yang Y., Waxman S.G.;
"Early- and late-onset inherited erythromelalgia: genotype-phenotype
correlation.";
Brain 132:1711-1722(2009).
[23]
VARIANTS GEFS+7 TYR-641 AND ARG-666, VARIANTS FEB3B VAL-62 AND
GLN-149, AND VARIANTS MET-228; ASN-490; LYS-519; MET-695; TYR-710;
VAL-750; PHE-1134; GLN-1171 AND VAL-1278.
PubMed=19763161; DOI=10.1371/journal.pgen.1000649;
Singh N.A., Pappas C., Dahle E.J., Claes L.R., Pruess T.H.,
De Jonghe P., Thompson J., Dixon M., Gurnett C., Peiffer A.,
White H.S., Filloux F., Leppert M.F.;
"A role of SCN9A in human epilepsies, as a cause of febrile seizures
and as a potential modifier of Dravet syndrome.";
PLoS Genet. 5:E1000649-E1000649(2009).
[24]
VARIANTS CIP GLN-907 AND 1381-ARG--LEU-1385 DEL, AND CHARACTERIZATION
OF VARIANTS CIP GLN-907 AND 1381-ARG--LEU-1385 DEL.
PubMed=20635406; DOI=10.1002/humu.21325;
Cox J.J., Sheynin J., Shorer Z., Reimann F., Nicholas A.K.,
Zubovic L., Baralle M., Wraige E., Manor E., Levy J., Woods C.G.,
Parvari R.;
"Congenital insensitivity to pain: novel SCN9A missense and in-frame
deletion mutations.";
Hum. Mutat. 31:E1670-E1686(2010).
[25]
VARIANT PEPD PRO-1623, AND CHARACTERIZATION OF VARIANT PEPD PRO-1623.
PubMed=25285947; DOI=10.1097/ALN.0000000000000476;
Suter M.R., Bhuiyan Z.A., Laedermann C.J., Kuntzer T., Schaller M.,
Stauffacher M.W., Roulet E., Abriel H., Decosterd I., Wider C.;
"p.L1612P, a novel voltage-gated sodium channel Nav1.7 mutation
inducing a cold sensitive paroxysmal extreme pain disorder.";
Anesthesiology 122:414-423(2015).
[26]
VARIANT PERYTHM THR-1643, CHARACTERIZATION OF VARIANT PERYTHM
THR-1643, MUTAGENESIS OF ALA-1643, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24311784; DOI=10.1074/jbc.M113.502211;
Eberhardt M., Nakajima J., Klinger A.B., Neacsu C., Huhne K.,
O'Reilly A.O., Kist A.M., Lampe A.K., Fischer K., Gibson J., Nau C.,
Winterpacht A., Lampert A.;
"Inherited pain: sodium channel Nav1.7 A1632T mutation causes
erythromelalgia due to a shift of fast inactivation.";
J. Biol. Chem. 289:1971-1980(2014).
-!- FUNCTION: Mediates the voltage-dependent sodium ion permeability
of excitable membranes. Assuming opened or closed conformations in
response to the voltage difference across the membrane, the
protein forms a sodium-selective channel through which Na(+) ions
may pass in accordance with their electrochemical gradient
(PubMed:7720699, PubMed:17167479, PubMed:25240195,
PubMed:26680203, PubMed:15385606, PubMed:16988069,
PubMed:17145499, PubMed:19369487, PubMed:24311784). It is a
tetrodotoxin-sensitive Na(+) channel isoform (PubMed:7720699).
Plays a role in pain mechanisms, especially in the development of
inflammatory pain (PubMed:17167479, PubMed:17145499,
PubMed:19369487, PubMed:24311784). {ECO:0000269|PubMed:15178348,
ECO:0000269|PubMed:15385606, ECO:0000269|PubMed:16988069,
ECO:0000269|PubMed:17145499, ECO:0000269|PubMed:17167479,
ECO:0000269|PubMed:19369487, ECO:0000269|PubMed:24311784,
ECO:0000269|PubMed:25240195, ECO:0000269|PubMed:26680203,
ECO:0000269|PubMed:7720699}.
-!- SUBUNIT: The sodium channel complex consists of a large, channel-
forming alpha subunit and 2-3 smaller, ancillary beta subunits
(PubMed:7720699, PubMed:17167479, PubMed:25240195). Interacts with
NEDD4 and NEDD4L (By similarity). Interacts with the conotoxin
GVIIJ (PubMed:24497506). Interacts with the conotoxin GVIIJ
(PubMed:24497506). Interacts with the spider beta/delta-
theraphotoxin-Pre1a (PubMed:28428547).
{ECO:0000250|UniProtKB:Q62205, ECO:0000269|PubMed:17167479,
ECO:0000269|PubMed:24497506, ECO:0000269|PubMed:25240195,
ECO:0000269|PubMed:28428547, ECO:0000269|PubMed:7720699}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15385606,
ECO:0000269|PubMed:17167479, ECO:0000269|PubMed:19369487,
ECO:0000269|PubMed:24311784, ECO:0000269|PubMed:25240195,
ECO:0000269|PubMed:26680203, ECO:0000269|PubMed:7720699}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cell
projection {ECO:0000250|UniProtKB:O08562}. Note=In neurite
terminals. {ECO:0000250|UniProtKB:O08562}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q15858-1; Sequence=Displayed;
Name=2;
IsoId=Q15858-2; Sequence=VSP_012028;
Name=3;
IsoId=Q15858-3; Sequence=VSP_012029;
Name=4;
IsoId=Q15858-4; Sequence=VSP_012028, VSP_012029;
-!- TISSUE SPECIFICITY: Expressed strongly in dorsal root ganglion,
with only minor levels elsewhere in the body, smooth muscle cells,
MTC cell line and C-cell carcinoma. Isoform 1 is expressed
preferentially in the central and peripheral nervous system.
Isoform 2 is expressed preferentially in the dorsal root ganglion.
{ECO:0000269|PubMed:15178348, ECO:0000269|PubMed:15302875,
ECO:0000269|PubMed:7720699, ECO:0000269|PubMed:9169448}.
-!- DOMAIN: The sequence contains 4 internal repeats, each with 5
hydrophobic segments (S1, S2, S3, S5, S6) and one positively
charged segment (S4). Segments S4 are probably the voltage-sensors
and are characterized by a series of positively charged amino
acids at every third position. {ECO:0000305}.
-!- PTM: Phosphorylation at Ser-1490 by PKC in a highly conserved
cytoplasmic loop increases peak sodium currents.
{ECO:0000269|PubMed:25240195}.
-!- PTM: Ubiquitinated by NEDD4L; which may promote its endocytosis.
Does not seem to be ubiquitinated by NEDD4.
{ECO:0000250|UniProtKB:Q62205}.
-!- DISEASE: Primary erythermalgia (PERYTHM) [MIM:133020]: Autosomal
dominant disease characterized by recurrent episodes of severe
pain associated with redness and warmth in the feet or hands.
{ECO:0000269|PubMed:14985375, ECO:0000269|PubMed:15385606,
ECO:0000269|PubMed:15955112, ECO:0000269|PubMed:15958509,
ECO:0000269|PubMed:16216943, ECO:0000269|PubMed:16392115,
ECO:0000269|PubMed:16702558, ECO:0000269|PubMed:16988069,
ECO:0000269|PubMed:18945915, ECO:0000269|PubMed:19369487,
ECO:0000269|PubMed:24311784}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Indifference to pain, congenital, autosomal recessive
(CIP) [MIM:243000]: A disorder characterized by congenital
inability to perceive any form of pain, in any part of the body.
All other sensory modalities are preserved and the peripheral and
central nervous systems are apparently intact. Patients perceive
the sensations of touch, warm and cold temperature,
proprioception, tickle and pressure, but not painful stimuli.
There is no evidence of a motor or sensory neuropathy, either
axonal or demyelinating. {ECO:0000269|PubMed:20635406}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Paroxysmal extreme pain disorder (PEPD) [MIM:167400]:
Autosomal dominant paroxysmal disorder of pain and autonomic
dysfunction. The distinctive features are paroxysmal episodes of
burning pain in the rectal, ocular, and mandibular areas
accompanied by autonomic manifestations such as skin flushing.
{ECO:0000269|PubMed:17145499, ECO:0000269|PubMed:18945915,
ECO:0000269|PubMed:25285947}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Generalized epilepsy with febrile seizures plus 7
(GEFS+7) [MIM:613863]: A rare autosomal dominant, familial
condition with incomplete penetrance and large intrafamilial
variability. Patients display febrile seizures persisting
sometimes beyond the age of 6 years and/or a variety of afebrile
seizure types. This disease combines febrile seizures, generalized
seizures often precipitated by fever at age 6 years or more, and
partial seizures, with a variable degree of severity.
{ECO:0000269|PubMed:19763161}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Febrile seizures, familial, 3B (FEB3B) [MIM:613863]:
Seizures associated with febrile episodes in childhood without any
evidence of intracranial infection or defined pathologic or
traumatic cause. It is a common condition, affecting 2-5% of
children aged 3 months to 5 years. The majority are simple febrile
seizures (generally defined as generalized onset, single seizures
with a duration of less than 30 minutes). Complex febrile seizures
are characterized by focal onset, duration greater than 30
minutes, and/or more than one seizure in a 24 hour period. The
likelihood of developing epilepsy following simple febrile
seizures is low. Complex febrile seizures are associated with a
moderately increased incidence of epilepsy.
{ECO:0000269|PubMed:19763161}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.7/SCN9A subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=SCN9A entry;
URL="https://en.wikipedia.org/wiki/SCN9A";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Silent pain - Issue 102
of February 2009;
URL="http://web.expasy.org/spotlight/back_issues/102";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X82835; CAA58042.1; -; mRNA.
EMBL; DQ857292; ABI51981.1; -; mRNA.
EMBL; AC074101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY682084; AAT85833.1; -; mRNA.
EMBL; AY682085; AAT85834.1; -; mRNA.
EMBL; AY682086; AAT85835.1; -; mRNA.
EMBL; AJ310882; CAC84550.1; -; mRNA.
EMBL; AJ310883; CAC84551.1; -; mRNA.
EMBL; AJ310897; CAC84537.1; -; mRNA.
EMBL; AJ580918; CAE45644.1; -; Genomic_DNA.
EMBL; AJ580919; CAE45645.1; -; Genomic_DNA.
CCDS; CCDS46441.1; -. [Q15858-3]
PIR; S54771; S54771.
RefSeq; NP_002968.1; NM_002977.3.
RefSeq; XP_005246814.1; XM_005246757.2. [Q15858-1]
RefSeq; XP_011509918.1; XM_011511616.2. [Q15858-1]
RefSeq; XP_011509919.1; XM_011511617.2. [Q15858-2]
RefSeq; XP_011509920.1; XM_011511618.2. [Q15858-4]
UniGene; Hs.439145; -.
PDB; 5EK0; X-ray; 3.53 A; A/B/C/D=1527-1559, A/B/C/D=1581-1622.
PDBsum; 5EK0; -.
ProteinModelPortal; Q15858; -.
IntAct; Q15858; 2.
STRING; 9606.ENSP00000386306; -.
BindingDB; Q15858; -.
ChEMBL; CHEMBL4296; -.
DrugBank; DB06218; Lacosamide.
DrugBank; DB00281; Lidocaine.
DrugBank; DB00243; Ranolazine.
DrugBank; DB06201; Rufinamide.
DrugBank; DB00313; Valproic Acid.
DrugBank; DB00909; Zonisamide.
GuidetoPHARMACOLOGY; 584; -.
TCDB; 1.A.1.10.5; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q15858; -.
PhosphoSitePlus; Q15858; -.
BioMuta; SCN9A; -.
DMDM; 327478559; -.
EPD; Q15858; -.
PaxDb; Q15858; -.
PeptideAtlas; Q15858; -.
PRIDE; Q15858; -.
Ensembl; ENST00000303354; ENSP00000304748; ENSG00000169432. [Q15858-1]
Ensembl; ENST00000409435; ENSP00000386330; ENSG00000169432. [Q15858-1]
Ensembl; ENST00000409672; ENSP00000386306; ENSG00000169432. [Q15858-3]
GeneID; 6335; -.
KEGG; hsa:6335; -.
UCSC; uc002udr.2; human. [Q15858-1]
CTD; 6335; -.
DisGeNET; 6335; -.
EuPathDB; HostDB:ENSG00000169432.14; -.
GeneCards; SCN9A; -.
GeneReviews; SCN9A; -.
HGNC; HGNC:10597; SCN9A.
HPA; CAB013679; -.
HPA; HPA061843; -.
MalaCards; SCN9A; -.
MIM; 133020; phenotype.
MIM; 167400; phenotype.
MIM; 243000; phenotype.
MIM; 603415; gene.
MIM; 613863; phenotype.
neXtProt; NX_Q15858; -.
OpenTargets; ENSG00000169432; -.
Orphanet; 88642; Channelopathy-associated congenital insensitivity to pain.
Orphanet; 33069; Dravet syndrome.
Orphanet; 1956; Erythromelalgia.
Orphanet; 36387; Generalized epilepsy with febrile seizures-plus.
Orphanet; 970; Hereditary sensory and autonomic neuropathy type 2.
Orphanet; 46348; Paroxysmal extreme pain disorder.
Orphanet; 90026; Primary erythermalgia.
Orphanet; 306577; Sodium channelopathy-related small fiber neuropathy.
PharmGKB; PA35010; -.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128242; -.
HOVERGEN; HBG053100; -.
InParanoid; Q15858; -.
KO; K04841; -.
OMA; RQKCPPW; -.
OrthoDB; EOG091G00FK; -.
PhylomeDB; Q15858; -.
TreeFam; TF323985; -.
Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
SIGNOR; Q15858; -.
GeneWiki; Nav1.7; -.
GenomeRNAi; 6335; -.
PRO; PR:Q15858; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000169432; -.
CleanEx; HS_SCN9A; -.
ExpressionAtlas; Q15858; baseline and differential.
Genevisible; Q15858; HS.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:Ensembl.
GO; GO:0031402; F:sodium ion binding; IEA:Ensembl.
GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:UniProtKB.
GO; GO:0048266; P:behavioral response to pain; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006814; P:sodium ion transport; TAS:ProtInc.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR001696; Na_channel_asu.
InterPro; IPR010526; Na_trans_assoc.
InterPro; IPR024583; Na_trans_cytopl.
InterPro; IPR028803; SCN9A.
PANTHER; PTHR10037:SF235; PTHR10037:SF235; 1.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF06512; Na_trans_assoc; 1.
Pfam; PF11933; Na_trans_cytopl; 1.
PRINTS; PR00170; NACHANNEL.
SMART; SM00015; IQ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Disease mutation; Disulfide bond; Epilepsy;
Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Sodium; Sodium channel;
Sodium transport; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation; Voltage-gated channel.
CHAIN 1 1988 Sodium channel protein type 9 subunit
alpha.
/FTId=PRO_0000048502.
TOPO_DOM 1 126 Cytoplasmic. {ECO:0000305}.
TRANSMEM 127 145 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 146 152 Extracellular. {ECO:0000305}.
TRANSMEM 153 173 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 174 187 Cytoplasmic. {ECO:0000305}.
TRANSMEM 188 205 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 206 211 Extracellular. {ECO:0000305}.
TRANSMEM 212 228 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 229 247 Cytoplasmic. {ECO:0000305}.
TRANSMEM 248 267 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 268 346 Extracellular. {ECO:0000305}.
INTRAMEM 347 371 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 372 378 Extracellular. {ECO:0000305}.
TRANSMEM 379 399 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 400 744 Cytoplasmic. {ECO:0000305}.
TRANSMEM 745 763 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 764 774 Extracellular. {ECO:0000305}.
TRANSMEM 775 794 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 795 808 Cytoplasmic. {ECO:0000305}.
TRANSMEM 809 828 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 829 830 Extracellular. {ECO:0000305}.
TRANSMEM 831 848 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 849 864 Cytoplasmic. {ECO:0000305}.
TRANSMEM 865 883 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 884 912 Extracellular. {ECO:0000305}.
INTRAMEM 913 933 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 934 946 Extracellular. {ECO:0000305}.
TRANSMEM 947 967 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 968 1193 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1194 1211 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1212 1224 Extracellular. {ECO:0000305}.
TRANSMEM 1225 1243 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1244 1257 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1258 1276 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1277 1284 Extracellular. {ECO:0000305}.
TRANSMEM 1285 1303 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1304 1320 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1321 1340 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1341 1392 Extracellular. {ECO:0000305}.
INTRAMEM 1393 1414 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1415 1431 Extracellular. {ECO:0000305}.
TRANSMEM 1432 1453 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1454 1516 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1517 1534 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1535 1545 Extracellular. {ECO:0000305}.
TRANSMEM 1546 1564 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1565 1576 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1577 1594 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1595 1607 Extracellular. {ECO:0000305}.
TRANSMEM 1608 1624 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1625 1643 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1644 1661 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1662 1683 Extracellular. {ECO:0000305}.
INTRAMEM 1684 1706 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1707 1736 Extracellular. {ECO:0000305}.
TRANSMEM 1737 1759 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1760 1988 Cytoplasmic. {ECO:0000305}.
REPEAT 112 410 I. {ECO:0000305}.
REPEAT 726 989 II. {ECO:0000305}.
REPEAT 1180 1488 III. {ECO:0000305}.
REPEAT 1497 1795 IV. {ECO:0000305}.
DOMAIN 1889 1918 IQ.
MOD_RES 503 503 Phosphoserine.
{ECO:0000250|UniProtKB:O88420}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000250|UniProtKB:O88420}.
MOD_RES 1490 1490 Phosphoserine; by PKC.
{ECO:0000269|PubMed:25240195}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1352 1352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1366 1366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1375 1375 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 275 324 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 895 895 Interchain; with SCN2B or SCN4B.
{ECO:0000250|UniProtKB:P04775}.
DISULFID 895 895 Interchain; with the conotoxin GVIIJ
(when the channel is not linked to SCN2B
or SCN4B; the bond to SCN2B or SCN4B
protects the channel from the inhibition
by toxin).
{ECO:0000250|UniProtKB:P04775}.
DISULFID 935 944 {ECO:0000250|UniProtKB:D0E0C2}.
VAR_SEQ 200 229 YLTEFVNLGNVSALRTFRVLRALKTISVIP -> YVTEFVD
LGNVSALRTFRVLRALKTISVIP (in isoform 2 and
isoform 4).
{ECO:0000303|PubMed:15302875}.
/FTId=VSP_012028.
VAR_SEQ 648 658 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15302875,
ECO:0000303|PubMed:17167479,
ECO:0000303|PubMed:7720699}.
/FTId=VSP_012029.
VARIANT 10 10 Q -> R (in PERYTHM; causes a
hyperpolarizing shift of -5.3 mV for the
midpoint of activation which is smaller
than that seen in other mutations causing
early-onset erythromelalgia mutations;
also causes a faster rate of activation
and slower deactivation compared to wild-
type; expression of the mutant protein
induced hyperexcitability in dorsal root
ganglion neurons but the increase is
smaller than that produced by Thr-859;
dbSNP:rs267607030).
{ECO:0000269|PubMed:19369487}.
/FTId=VAR_064595.
VARIANT 62 62 I -> V (in FEB3B; dbSNP:rs121908920).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064596.
VARIANT 149 149 P -> Q (in FEB3B; dbSNP:rs121908921).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064597.
VARIANT 216 216 F -> S (in PERYTHM; hyperpolarizes the
voltage dependence of activation by 11
mV, accelerates activation, slows
deactivation and enhances the response to
slow, small depolarizations;
dbSNP:rs80356469).
{ECO:0000269|PubMed:15955112,
ECO:0000269|PubMed:16988069}.
/FTId=VAR_064598.
VARIANT 228 228 I -> M (in dbSNP:rs71428908).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064599.
VARIANT 241 241 S -> T (in PERYTHM; dbSNP:rs80356470).
{ECO:0000269|PubMed:16216943}.
/FTId=VAR_032014.
VARIANT 395 395 N -> K (in PERYTHM; dbSNP:rs80356471).
{ECO:0000269|PubMed:15955112}.
/FTId=VAR_064600.
VARIANT 406 406 E -> K (in PERYTHM).
/FTId=VAR_064601.
VARIANT 490 490 S -> N (in dbSNP:rs58022607).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064602.
VARIANT 519 519 E -> K (in dbSNP:rs187453572).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064603.
VARIANT 641 641 N -> Y (in GEFS+7; dbSNP:rs121908918).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064604.
VARIANT 666 666 K -> R (in GEFS+7; also found in a
patient with severe myoclonic epilepsy in
infancy; dbSNP:rs121908919).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064605.
VARIANT 695 695 I -> M (in dbSNP:rs199588089).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064606.
VARIANT 710 710 C -> Y (found in a patient with severe
myoclonic epilepsy in infancy;
dbSNP:rs201709980).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064607.
VARIANT 750 750 I -> V (in dbSNP:rs182650126).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064608.
VARIANT 859 859 I -> T (in PERYTHM; sporadic; activated
at more negative potentials; slower
inactivation kinetics than wild-type
channels; dbSNP:rs80356474).
{ECO:0000269|PubMed:14985375,
ECO:0000269|PubMed:15385606,
ECO:0000269|PubMed:15955112,
ECO:0000269|PubMed:19369487}.
/FTId=VAR_019947.
VARIANT 869 869 L -> F (in PERYTHM; causes a
hyperpolarizing shift in channel
activation, a depolarizing shift of
inactivation and an 18-fold increase in
deactivation time compared to wild-type;
the mean ramp current amplitude in
response to slow depolarization is higher
in the mutant channels;
dbSNP:rs80356476).
{ECO:0000269|PubMed:15955112,
ECO:0000269|PubMed:16392115}.
/FTId=VAR_064609.
VARIANT 869 869 L -> H (in PERYTHM; activated at more
negative potentials; slower inactivation
kinetics than wild-type channels;
dbSNP:rs80356475).
{ECO:0000269|PubMed:14985375,
ECO:0000269|PubMed:15385606,
ECO:0000269|PubMed:16702558}.
/FTId=VAR_019948.
VARIANT 907 907 R -> Q (in CIP; significant reduction in
membrane localization of the mutant
protein compared to the wild-type;
complete loss of function of the sodium
channel). {ECO:0000269|PubMed:20635406}.
/FTId=VAR_064610.
VARIANT 932 932 M -> L (in dbSNP:rs12478318).
/FTId=VAR_030444.
VARIANT 943 943 M -> L (in dbSNP:rs12478318).
/FTId=VAR_055646.
VARIANT 1007 1007 R -> C (in PEPD; dbSNP:rs121908910).
{ECO:0000269|PubMed:17145499}.
/FTId=VAR_032015.
VARIANT 1134 1134 L -> F (in dbSNP:rs200160858).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064611.
VARIANT 1161 1161 W -> R (in dbSNP:rs6746030).
{ECO:0000269|PubMed:15955112,
ECO:0000269|PubMed:17167479,
ECO:0000269|PubMed:7720699}.
/FTId=VAR_019949.
VARIANT 1171 1171 E -> Q (found in a patient with severe
myoclonic epilepsy in infancy).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064612.
VARIANT 1278 1278 L -> V (in dbSNP:rs180922748).
{ECO:0000269|PubMed:19763161}.
/FTId=VAR_064613.
VARIANT 1309 1309 V -> D (in PEPD; dbSNP:rs121908911).
{ECO:0000269|PubMed:17145499}.
/FTId=VAR_032016.
VARIANT 1309 1309 V -> F (in PEPD; dbSNP:rs121908912).
{ECO:0000269|PubMed:17145499}.
/FTId=VAR_032017.
VARIANT 1310 1310 V -> F (in PEPD; dbSNP:rs121908913).
{ECO:0000269|PubMed:17145499}.
/FTId=VAR_032018.
VARIANT 1381 1385 Missing (in CIP; significant reduction in
membrane localization of the mutant
protein compared to the wild-type;
complete loss of function of the sodium
channel). {ECO:0000269|PubMed:20635406}.
/FTId=VAR_064614.
VARIANT 1460 1460 F -> V (in PERYTHM; produces a
hyperpolarizing shift in channel
activation and a depolarizing shift in
steady-state activation;
dbSNP:rs80356478).
{ECO:0000269|PubMed:15958509}.
/FTId=VAR_032019.
VARIANT 1472 1472 I -> T (in PEPD; reduction in fast
inactivation leading to persistent sodium
current; dbSNP:rs121908914).
{ECO:0000269|PubMed:17145499}.
/FTId=VAR_032020.
VARIANT 1473 1473 F -> V (in PEPD).
{ECO:0000269|PubMed:17145499}.
/FTId=VAR_032021.
VARIANT 1475 1475 T -> I (in PEPD; reduction in fast
inactivation leading to persistent sodium
current; dbSNP:rs121908915).
{ECO:0000269|PubMed:17145499}.
/FTId=VAR_032022.
VARIANT 1623 1623 L -> P (in PEPD; depolarizes the voltage-
dependence of channel activation and
steady-state fast inactivation; increases
ramp current).
{ECO:0000269|PubMed:25285947}.
/FTId=VAR_072279.
VARIANT 1638 1638 M -> K (in PEPD; reduction in fast
inactivation leading to persistent sodium
current). {ECO:0000269|PubMed:17145499}.
/FTId=VAR_032023.
VARIANT 1643 1643 A -> E (in PERYTHM and PEPD;
hyperpolarizes voltage-dependence of
channel activation; depolarizes the
voltage-dependence of steady-state fast
inactivation; slows channel deactivation;
enhances persistent and resurgent
current; enhances neuronal
hyperexcitability in dorsal root ganglion
neurons; dbSNP:rs879253994).
{ECO:0000269|PubMed:18945915,
ECO:0000269|PubMed:24311784}.
/FTId=VAR_072280.
VARIANT 1643 1643 A -> T (in PERYTHM; no effect on voltage-
dependence of channel activation;
depolarizes the voltage dependence of
steady-state fast inactivation;
accelerates channel deactivation; no
increase in persistent and resurgent
currents; enhances neuronal
hyperexcitability in dorsal root ganglion
neurons). {ECO:0000269|PubMed:24311784}.
/FTId=VAR_072281.
VARIANT 1919 1919 D -> G (in dbSNP:rs3750904).
/FTId=VAR_019950.
MUTAGEN 1490 1490 S->A: Abolishes stimulation by agents
that stimulate PKC activity.
{ECO:0000269|PubMed:25240195}.
MUTAGEN 1490 1490 S->D,E: Increases current amplitude.
{ECO:0000269|PubMed:25240195}.
MUTAGEN 1643 1643 A->D: Depolarizes the voltage-dependence
of steady-state fast inactivation;
enhances persistent current.
{ECO:0000269|PubMed:24311784}.
MUTAGEN 1643 1643 A->K: No effect on voltage-dependence of
steady-state fast inactivation.
{ECO:0000269|PubMed:24311784}.
MUTAGEN 1643 1643 A->V: No effect on voltage-dependence of
steady-state fast inactivation.
{ECO:0000269|PubMed:24311784}.
CONFLICT 267 267 F -> S (in Ref. 4; AAT85834).
{ECO:0000305}.
CONFLICT 301 301 K -> R (in Ref. 4; AAT85835).
{ECO:0000305}.
CONFLICT 309 309 S -> P (in Ref. 4; AAT85834).
{ECO:0000305}.
CONFLICT 420 420 E -> G (in Ref. 4; AAT85834).
{ECO:0000305}.
CONFLICT 430 430 L -> P (in Ref. 4; AAT85834).
{ECO:0000305}.
CONFLICT 501 501 S -> P (in Ref. 4; AAT85835).
{ECO:0000305}.
CONFLICT 610 610 P -> T (in Ref. 4; AAT85835).
{ECO:0000305}.
CONFLICT 642 642 G -> R (in Ref. 4; AAT85835).
{ECO:0000305}.
SEQUENCE 1988 AA; 226372 MW; 1BAEB8F32EBF5438 CRC64;
MAMLPPPGPQ SFVHFTKQSL ALIEQRIAER KSKEPKEEKK DDDEEAPKPS SDLEAGKQLP
FIYGDIPPGM VSEPLEDLDP YYADKKTFIV LNKGKTIFRF NATPALYMLS PFSPLRRISI
KILVHSLFSM LIMCTILTNC IFMTMNNPPD WTKNVEYTFT GIYTFESLVK ILARGFCVGE
FTFLRDPWNW LDFVVIVFAY LTEFVNLGNV SALRTFRVLR ALKTISVIPG LKTIVGALIQ
SVKKLSDVMI LTVFCLSVFA LIGLQLFMGN LKHKCFRNSL ENNETLESIM NTLESEEDFR
KYFYYLEGSK DALLCGFSTD SGQCPEGYTC VKIGRNPDYG YTSFDTFSWA FLALFRLMTQ
DYWENLYQQT LRAAGKTYMI FFVVVIFLGS FYLINLILAV VAMAYEEQNQ ANIEEAKQKE
LEFQQMLDRL KKEQEEAEAI AAAAAEYTSI RRSRIMGLSE SSSETSKLSS KSAKERRNRR
KKKNQKKLSS GEEKGDAEKL SKSESEDSIR RKSFHLGVEG HRRAHEKRLS TPNQSPLSIR
GSLFSARRSS RTSLFSFKGR GRDIGSETEF ADDEHSIFGD NESRRGSLFV PHRPQERRSS
NISQASRSPP MLPVNGKMHS AVDCNGVVSL VDGRSALMLP NGQLLPEVII DKATSDDSGT
TNQIHKKRRC SSYLLSEDML NDPNLRQRAM SRASILTNTV EELEESRQKC PPWWYRFAHK
FLIWNCSPYW IKFKKCIYFI VMDPFVDLAI TICIVLNTLF MAMEHHPMTE EFKNVLAIGN
LVFTGIFAAE MVLKLIAMDP YEYFQVGWNI FDSLIVTLSL VELFLADVEG LSVLRSFRLL
RVFKLAKSWP TLNMLIKIIG NSVGALGNLT LVLAIIVFIF AVVGMQLFGK SYKECVCKIN
DDCTLPRWHM NDFFHSFLIV FRVLCGEWIE TMWDCMEVAG QAMCLIVYMM VMVIGNLVVL
NLFLALLLSS FSSDNLTAIE EDPDANNLQI AVTRIKKGIN YVKQTLREFI LKAFSKKPKI
SREIRQAEDL NTKKENYISN HTLAEMSKGH NFLKEKDKIS GFGSSVDKHL MEDSDGQSFI
HNPSLTVTVP IAPGESDLEN MNAEELSSDS DSEYSKVRLN RSSSSECSTV DNPLPGEGEE
AEAEPMNSDE PEACFTDGCV WRFSCCQVNI ESGKGKIWWN IRKTCYKIVE HSWFESFIVL
MILLSSGALA FEDIYIERKK TIKIILEYAD KIFTYIFILE MLLKWIAYGY KTYFTNAWCW
LDFLIVDVSL VTLVANTLGY SDLGPIKSLR TLRALRPLRA LSRFEGMRVV VNALIGAIPS
IMNVLLVCLI FWLIFSIMGV NLFAGKFYEC INTTDGSRFP ASQVPNRSEC FALMNVSQNV
RWKNLKVNFD NVGLGYLSLL QVATFKGWTI IMYAAVDSVN VDKQPKYEYS LYMYIYFVVF
IIFGSFFTLN LFIGVIIDNF NQQKKKLGGQ DIFMTEEQKK YYNAMKKLGS KKPQKPIPRP
GNKIQGCIFD LVTNQAFDIS IMVLICLNMV TMMVEKEGQS QHMTEVLYWI NVVFIILFTG
ECVLKLISLR HYYFTVGWNI FDFVVVIISI VGMFLADLIE TYFVSPTLFR VIRLARIGRI
LRLVKGAKGI RTLLFALMMS LPALFNIGLL LFLVMFIYAI FGMSNFAYVK KEDGINDMFN
FETFGNSMIC LFQITTSAGW DGLLAPILNS KPPDCDPKKV HPGSSVEGDC GNPSVGIFYF
VSYIIISFLV VVNMYIAVIL ENFSVATEES TEPLSEDDFE MFYEVWEKFD PDATQFIEFS
KLSDFAAALD PPLLIAKPNK VQLIAMDLPM VSGDRIHCLD ILFAFTKRVL GESGEMDSLR
SQMEERFMSA NPSKVSYEPI TTTLKRKQED VSATVIQRAY RRYRLRQNVK NISSIYIKDG
DRDDDLLNKK DMAFDNVNEN SSPEKTDATS STTSPPSYDS VTKPDKEKYE QDRTEKEDKG
KDSKESKK


Related products :

Catalog number Product name Quantity
EIAAB37609 Peripheral sodium channel 1,PN1,Rat,Rattus norvegicus,Scn9a,Sodium channel protein type 9 subunit alpha,Sodium channel protein type IX subunit alpha,Voltage-gated sodium channel subunit alpha Nav1.7
EIAAB37616 Homo sapiens,hPN3,Human,Peripheral nerve sodium channel 3,PN3,SCN10A,Sodium channel protein type 10 subunit alpha,Sodium channel protein type X subunit alpha,Voltage-gated sodium channel subunit alpha
EIAAB37611 hNE-Na,Homo sapiens,Human,NENA,Neuroendocrine sodium channel,Peripheral sodium channel 1,PN1,SCN9A,Sodium channel protein type 9 subunit alpha,Sodium channel protein type IX subunit alpha,Voltage-gate
EIAAB37615 Mouse,Mus musculus,Peripheral nerve sodium channel 3,PN3,Scn10a,Sensory neuron sodium channel,Sns,Sodium channel protein type 10 subunit alpha,Sodium channel protein type X subunit alpha,Voltage-gated
EIAAB37612 Kiaa4197,Mouse,Mus musculus,Peripheral sodium channel 1,PN1,Scn9a,Sodium channel protein type 9 subunit alpha,Sodium channel protein type IX subunit alpha,Voltage-gated sodium channel subunit alpha Na
EIAAB37610 Nas,Oryctolagus cuniculus,Rabbit,Schwann cell sodium channel,SCN9A,Sodium channel protein type 9 subunit alpha,Sodium channel protein type IX subunit alpha,Voltage-gated sodium channel subunit alpha N
EIAAB37575 Homo sapiens,Human,NAC1,SCN1,SCN1A,Sodium channel protein brain I subunit alpha,Sodium channel protein type 1 subunit alpha,Sodium channel protein type I subunit alpha,Voltage-gated sodium channel sub
EIAAB37596 Homo sapiens,Human,SCN4A,SkM1,Sodium channel protein skeletal muscle subunit alpha,Sodium channel protein type 4 subunit alpha,Sodium channel protein type IV subunit alpha,Voltage-gated sodium channel
EIAAB37606 Homo sapiens,Human,MED,SCN8A,Sodium channel protein type 8 subunit alpha,Sodium channel protein type VIII subunit alpha,Voltage-gated sodium channel subunit alpha Nav1.6
EIAAB37607 Mouse,Mus musculus,Nbna1,Scn8a,Sodium channel protein type 8 subunit alpha,Sodium channel protein type VIII subunit alpha,Voltage-gated sodium channel subunit alpha Nav1.6
EIAAB37618 NaN,Nan,Rat,Rattus norvegicus,Scn11a,Sensory neuron sodium channel 2,Sns2,Sodium channel protein type 11 subunit alpha,Sodium channel protein type XI subunit alpha,Voltage-gated sodium channel subunit
EIAAB37617 Mouse,Mus musculus,NaN,Nan,Nat,Scn11a,Sensory neuron sodium channel 2,Sns2,Sodium channel protein type 11 subunit alpha,Sodium channel protein type XI subunit alpha,Voltage-gated sodium channel subuni
EIAAB37614 Peripheral nerve sodium channel 3,PN3,Rat,Rattus norvegicus,Scn10a,Sensory neuron sodium channel,Sns,Sodium channel protein type 10 subunit alpha,Sodium channel protein type X subunit alpha,Voltage-ga
EIAAB37608 NaCh6,Peripheral nerve protein type 4,PN4,Rat,Rattus norvegicus,Scn8a,Sodium channel 6,Sodium channel protein type 8 subunit alpha,Sodium channel protein type VIII subunit alpha,Voltage-gated sodium c
EIAAB37595 Mouse,Mus musculus,Scn4a,Sodium channel protein skeletal muscle subunit alpha,Sodium channel protein type 4 subunit alpha,Sodium channel protein type IV subunit alpha,Voltage-gated sodium channel subu
EIAAB37604 HH1,Homo sapiens,Human,SCN5A,Sodium channel protein cardiac muscle subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type V subunit alpha,Voltage-gated sodium channel su
EIAAB37605 Homo sapiens,Human,Putative voltage-gated sodium channel subunit alpha Nax,SCN6A,SCN7A,Sodium channel protein cardiac and skeletal muscle subunit alpha,Sodium channel protein type 7 subunit alpha,Sodi
EIAAB37589 Rat,Rattus norvegicus,Scn3a,Sodium channel protein brain III subunit alpha,Sodium channel protein type 3 subunit alpha,Sodium channel protein type III subunit alpha,Voltage-gated sodium channel subtyp
EIAAB37603 Rat,Rattus norvegicus,Scn5a,Sodium channel protein cardiac muscle subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type V subunit alpha,Voltage-gated sodium channel sub
EIAAB37602 mH1,Mouse,Mus musculus,Scn5a,Sodium channel protein cardiac muscle subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type V subunit alpha,Voltage-gated sodium channel su
EIAAB37583 Rat,Rattus norvegicus,Scn2a,Scn2a1,Sodium channel protein brain II subunit alpha,Sodium channel protein type 2 subunit alpha,Sodium channel protein type II subunit alpha,Voltage-gated sodium channel s
EIAAB37590 Homo sapiens,Human,KIAA1356,NAC3,SCN3A,Sodium channel protein brain III subunit alpha,Sodium channel protein type 3 subunit alpha,Sodium channel protein type III subunit alpha,Voltage-gated sodium cha
EIAAB37619 hNaN,Homo sapiens,Human,Peripheral nerve sodium channel 5,PN5,SCN11A,SCN12A,Sensory neuron sodium channel 2,SNS2,Sodium channel protein type 11 subunit alpha,Sodium channel protein type XI subunit alp
EIAAB37576 Rat,Rattus norvegicus,Scn1a,Sodium channel protein brain I subunit alpha,Sodium channel protein type 1 subunit alpha,Sodium channel protein type I subunit alpha,Voltage-gated sodium channel subunit al
EIAAB37597 Mu-1,Rat,Rattus norvegicus,Scn4a,SkM1,Sodium channel protein skeletal muscle subunit alpha,Sodium channel protein type 4 subunit alpha,Sodium channel protein type IV subunit alpha,Voltage-gated sodium


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur