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 5 subunit alpha (Sodium channel protein cardiac muscle subunit alpha) (Sodium channel protein type V subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.5)

 SCN5A_RAT               Reviewed;        2019 AA.
P15389; Q925G6;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 136.
RecName: Full=Sodium channel protein type 5 subunit alpha;
AltName: Full=Sodium channel protein cardiac muscle subunit alpha;
AltName: Full=Sodium channel protein type V subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.5;
Name=Scn5a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
PubMed=2554302; DOI=10.1073/pnas.86.20.8170;
Rogart R.B., Cribbs L.L., Muglia L.K., Kephart D.D., Kaiser M.W.;
"Molecular cloning of a putative tetrodotoxin-resistant rat heart Na+
channel isoform.";
Proc. Natl. Acad. Sci. U.S.A. 86:8170-8174(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Sprague-Dawley;
Korsgaard M.P.G., Christophersen P., Ahring P.K., Olesen S.;
"Characterisation of the novel voltage-gated Na+ channel rNav1.5a
isolated from the rat hippocampal progenitor stem cell line HiB5.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[3]
MUTAGENESIS OF ASP-1612.
PubMed=9417050; DOI=10.1074/jbc.273.1.80;
Benzinger G.R., Kyle J.W., Blumenthal K.M., Hanck D.A.;
"A specific interaction between the cardiac sodium channel and site-3
toxin anthopleurin B.";
J. Biol. Chem. 273:80-84(1998).
[4]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=18386309; DOI=10.1080/01677060701672077;
Wang J., Ou S.-W., Wang Y.-J., Zong Z.-H., Lin L., Kameyama M.,
Kameyama A.;
"New variants of Nav1.5/SCN5A encode Na+ channels in the brain.";
J. Neurogenet. 22:57-75(2008).
[5]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=19376164; DOI=10.1016/j.neures.2009.04.003;
Wang J., Ou S.-W., Wang Y.-J., Kameyama M., Kameyama A., Zong Z.-H.;
"Analysis of four novel variants of Nav1.5/SCN5A cloned from the
brain.";
Neurosci. Res. 64:339-347(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-485 AND
THR-487, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[7]
MUTAGENESIS OF LEU-869.
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).
[8]
SITE CYS-374.
PubMed=26039939; DOI=10.1021/acs.biochem.5b00390;
Zhang M.M., Gajewiak J., Azam L., Bulaj G., Olivera B.M.,
Yoshikami D.;
"Probing the redox states of sodium channel cysteines at the binding
site of muO[section sign]-conotoxin GVIIJ.";
Biochemistry 54:3911-3920(2015).
-!- FUNCTION: This protein 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. It is a tetrodotoxin-resistant Na(+) channel isoform.
This channel is responsible for the initial upstroke of the action
potential. Channel inactivation is regulated by intracellular
calcium levels. {ECO:0000250|UniProtKB:Q14524,
ECO:0000250|UniProtKB:Q9JJV9}.
-!- SUBUNIT: Interacts with the PDZ domain of the syntrophin SNTA1,
SNTB1 and SNTB2. Interacts with NEDD4, NEDD4L, WWP2 and GPD1L.
Interacts with CALM. Interacts with FGF13; the interaction is
direct and may regulate SNC5A density at membranes and function.
May also interact with FGF12 and FGF14.
{ECO:0000250|UniProtKB:Q14524, ECO:0000250|UniProtKB:Q9JJV9}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14524,
ECO:0000250|UniProtKB:Q9JJV9}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:D0E0C2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P15389-1; Sequence=Displayed;
Name=2;
IsoId=P15389-2; Sequence=VSP_037482;
-!- TISSUE SPECIFICITY: Strongly expressed in the heart. Also
expressed in adult and fetal brain, spinal cord, testis, and at
moderate levels in kidney, adrenal gland, lung, skeletal muscle,
spleen, stomach and bladder. Isoform 2 is expressed in brain.
{ECO:0000269|PubMed:18386309, ECO:0000269|PubMed:19376164}.
-!- 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}.
-!- DOMAIN: The IQ domain mediates association with calmodulin.
{ECO:0000250|UniProtKB:Q14524}.
-!- PTM: Phosphorylation at Ser-1505 by PKC in a highly conserved
cytoplasmic loop slows inactivation of the sodium channel and
reduces peak sodium currents. Regulated through phosphorylation by
CaMK2D. {ECO:0000250|UniProtKB:Q14524,
ECO:0000250|UniProtKB:Q9JJV9}.
-!- PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. Does
not seem to be ubiquitinated by NEDD4 or WWP2.
{ECO:0000250|UniProtKB:Q14524}.
-!- PTM: Lacks the cysteine which covalently binds the conotoxin
GVIIJ. This cysteine (position 869) is speculated in other sodium
channel subunits alpha to be implied in covalent binding with the
sodium channel subunit beta-2 or beta-4.
{ECO:0000305|PubMed:24497506}.
-!- MISCELLANEOUS: Na(+) channels in mammalian cardiac membrane have
functional properties quite distinct from Na(+) channels in nerve
and skeletal muscle.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.5/SCN5A subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M27902; AAA42114.1; -; mRNA.
EMBL; AF353637; AAK38884.1; -; mRNA.
PIR; A33996; A33996.
RefSeq; NP_001153634.1; NM_001160162.1. [P15389-2]
RefSeq; NP_037257.1; NM_013125.2. [P15389-1]
UniGene; Rn.32074; -.
ProteinModelPortal; P15389; -.
DIP; DIP-60063N; -.
IntAct; P15389; 2.
STRING; 10116.ENSRNOP00000060180; -.
BindingDB; P15389; -.
ChEMBL; CHEMBL3866; -.
GuidetoPHARMACOLOGY; 582; -.
iPTMnet; P15389; -.
PhosphoSitePlus; P15389; -.
PaxDb; P15389; -.
PRIDE; P15389; -.
GeneID; 25665; -.
KEGG; rno:25665; -.
UCSC; RGD:3637; rat. [P15389-1]
CTD; 6331; -.
RGD; 3637; Scn5a.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOGENOM; HOG000231755; -.
HOVERGEN; HBG053100; -.
InParanoid; P15389; -.
KO; K04838; -.
PhylomeDB; P15389; -.
PRO; PR:P15389; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005901; C:caveola; ISS:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
GO; GO:0001518; C:voltage-gated sodium channel complex; ISS:BHF-UCL.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0030506; F:ankyrin binding; IDA:RGD.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0017134; F:fibroblast growth factor binding; IPI:RGD.
GO; GO:0005248; F:voltage-gated sodium channel activity; ISS:UniProtKB.
GO; GO:0086060; F:voltage-gated sodium channel activity involved in AV node cell action potential; ISS:BHF-UCL.
GO; GO:0086061; F:voltage-gated sodium channel activity involved in bundle of His cell action potential; ISS:BHF-UCL.
GO; GO:0086006; F:voltage-gated sodium channel activity involved in cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0086062; F:voltage-gated sodium channel activity involved in Purkinje myocyte action potential; ISS:BHF-UCL.
GO; GO:0086063; F:voltage-gated sodium channel activity involved in SA node cell action potential; ISS:BHF-UCL.
GO; GO:0086014; P:atrial cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0086016; P:AV node cell action potential; ISS:BHF-UCL.
GO; GO:0086067; P:AV node cell to bundle of His cell communication; ISS:BHF-UCL.
GO; GO:0003360; P:brainstem development; IEP:RGD.
GO; GO:0086043; P:bundle of His cell action potential; ISS:BHF-UCL.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISS:BHF-UCL.
GO; GO:0060048; P:cardiac muscle contraction; ISS:BHF-UCL.
GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0051899; P:membrane depolarization; ISS:BHF-UCL.
GO; GO:0086010; P:membrane depolarization during action potential; ISS:BHF-UCL.
GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISS:BHF-UCL.
GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; ISS:BHF-UCL.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; ISS:BHF-UCL.
GO; GO:0086046; P:membrane depolarization during SA node cell action potential; ISS:BHF-UCL.
GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
GO; GO:0045760; P:positive regulation of action potential; IMP:RGD.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:RGD.
GO; GO:0010460; P:positive regulation of heart rate; IMP:RGD.
GO; GO:0010765; P:positive regulation of sodium ion transport; ISS:BHF-UCL.
GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; ISS:BHF-UCL.
GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISS:BHF-UCL.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; ISS:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; ISS:BHF-UCL.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL.
GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISS:BHF-UCL.
GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; ISS:BHF-UCL.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISS:BHF-UCL.
GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IMP:RGD.
GO; GO:0086015; P:SA node cell action potential; ISS:BHF-UCL.
GO; GO:0035725; P:sodium ion transmembrane transport; IMP:RGD.
GO; GO:0006814; P:sodium ion transport; ISS:UniProtKB.
GO; GO:0021537; P:telencephalon development; IEP:RGD.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR008053; Na_channel_a5su.
InterPro; IPR001696; Na_channel_asu.
InterPro; IPR010526; Na_trans_assoc.
InterPro; IPR024583; Na_trans_cytopl.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF06512; Na_trans_assoc; 1.
Pfam; PF11933; Na_trans_cytopl; 1.
PRINTS; PR00170; NACHANNEL.
PRINTS; PR01666; NACHANNEL5.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
Ion transport; Membrane; Methylation; Phosphoprotein;
Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
Voltage-gated channel.
CHAIN 1 2019 Sodium channel protein type 5 subunit
alpha.
/FTId=PRO_0000048498.
TOPO_DOM 1 132 Cytoplasmic. {ECO:0000305}.
TRANSMEM 133 151 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 152 158 Extracellular. {ECO:0000305}.
TRANSMEM 159 179 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 180 193 Cytoplasmic. {ECO:0000305}.
TRANSMEM 194 211 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 212 217 Extracellular. {ECO:0000305}.
TRANSMEM 218 234 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 235 253 Cytoplasmic. {ECO:0000305}.
TRANSMEM 254 273 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 274 358 Extracellular. {ECO:0000305}.
INTRAMEM 359 383 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 384 390 Extracellular. {ECO:0000305}.
TRANSMEM 391 411 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 412 718 Cytoplasmic. {ECO:0000305}.
TRANSMEM 719 737 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 738 748 Extracellular. {ECO:0000305}.
TRANSMEM 749 768 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 769 782 Cytoplasmic. {ECO:0000305}.
TRANSMEM 783 802 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 803 804 Extracellular. {ECO:0000305}.
TRANSMEM 805 822 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 823 838 Cytoplasmic. {ECO:0000305}.
TRANSMEM 839 857 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 858 886 Extracellular. {ECO:0000305}.
INTRAMEM 887 907 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 908 920 Extracellular. {ECO:0000305}.
TRANSMEM 921 941 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 942 1208 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1209 1226 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1227 1239 Extracellular. {ECO:0000305}.
TRANSMEM 1240 1258 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1259 1272 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1273 1291 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1292 1299 Extracellular. {ECO:0000305}.
TRANSMEM 1300 1318 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1319 1335 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1336 1355 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1356 1407 Extracellular. {ECO:0000305}.
INTRAMEM 1408 1429 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1430 1446 Extracellular. {ECO:0000305}.
TRANSMEM 1447 1468 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1469 1531 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1532 1549 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1550 1560 Extracellular. {ECO:0000305}.
TRANSMEM 1561 1579 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1580 1591 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1592 1609 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1610 1622 Extracellular. {ECO:0000305}.
TRANSMEM 1623 1639 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1640 1658 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1659 1676 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1677 1698 Extracellular. {ECO:0000305}.
INTRAMEM 1699 1721 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1722 1750 Extracellular. {ECO:0000305}.
TRANSMEM 1751 1773 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1774 2019 Cytoplasmic. {ECO:0000305}.
REPEAT 114 421 I. {ECO:0000305}.
REPEAT 700 972 II. {ECO:0000305}.
REPEAT 1189 1503 III. {ECO:0000305}.
REPEAT 1512 1809 IV. {ECO:0000305}.
DOMAIN 1903 1932 IQ.
REGION 1841 1903 Interaction with FGF13.
{ECO:0000250|UniProtKB:Q14524}.
REGION 1977 1980 Interaction with NEDD4, NEDD4L and WWP2.
{ECO:0000250|UniProtKB:Q14524}.
SITE 374 374 Cys residue near the selectivity filter,
which has a free thiol that is
susceptible to reaction with
methanethiosulfonate (MTSET); Sodium
current is irreversibly blocked by MTSET.
{ECO:0000250|UniProtKB:P04775,
ECO:0000269|PubMed:26039939}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 39 39 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 461 461 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 487 487 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 527 527 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 527 527 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JJV9}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 665 665 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 668 668 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 1505 1505 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q14524}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 284 284 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 741 741 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 804 804 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 865 865 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1367 1367 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1376 1376 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1382 1382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1390 1390 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 281 336 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 909 918 {ECO:0000250|UniProtKB:D0E0C2}.
VAR_SEQ 1080 1132 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_037482.
MUTAGEN 869 869 L->C: >1000-fold increase of sensitivity
to the conotoxin GVIIJ(SSG).
{ECO:0000269|PubMed:24497506}.
MUTAGEN 1612 1612 D->N,R: Little change in voltage-
dependence of conductance and decrease in
affinity to the sea anemone toxin
anthopleurin-B (residue Lys-37).
{ECO:0000269|PubMed:9417050}.
SEQUENCE 2019 AA; 227367 MW; CFC3B03CEAE708AD CRC64;
MANLLLPRGT SSFRRFTRES LAAIEKRMAE KQARGGSATS QESREGLQEE EAPRPQLDLQ
ASKKLPDLYG NPPRELIGEP LEDLDPFYST QKTFIVLNKG KTIFRFSATN ALYVLSPFHP
VRRAAVKILV HSLFSMLIMC TILTNCVFMA QHDPPPWTKY VEYTFTAIYT FESLVKILAR
GFCLHAFTFL RDPWNWLDFS VIVMAYTTEF VDLGNVSALR TFRVLRALKT ISVISGLKTI
VGALIQSVKK LADVMVLTVF CLSVFALIGL QLFMGNLRHK CVRNFTELNG TNGSVEADGL
VWNSLDVYLN DPANYLLKNG TTDVLLCGNS SDAGTCPEGY RCLKAGENPD HGYTSFDSFA
WAFLALFRLM TQDCWERLYQ QTLRSAGKIY MIFFMLVIFL GSFYLVNLIL AVVAMAYEEQ
NQATIAETEE KEKRFQEAME MLKKEHEALT IRGVDTVSRS SLEMSPLAPV TNHERKSKRR
KRLSSGTEDG GDDRLPKSDS EDGPRALNQL SLTHGLSRTS MRPRSSRGSI FTFRRRDQGS
EADFADDENS TAGESESHRT SLLVPWPLRH PSAQGQPGPG ASAPGYVLNG KRNSTVDCNG
VVSLLGAGDA EATSPGSYLL RPMVLDRPPD TTTPSEEPGG PQMLTPQAPC ADGFEEPGAR
QRALSAVSVL TSALEELEES HRKCPPCWNR FAQHYLIWEC CPLWMSIKQK VKFVVMDPFA
DLTITMCIVL NTLFMALEHY NMTAEFEEML QVGNLVFTGI FTAEMTFKII ALDPYYYFQQ
GWNIFDSIIV ILSLMELGLS RMGNLSVLRS FRLLRVFKLA KSWPTLNTLI KIIGNSVGAL
GNLTLVLAII VFIFAVVGMQ LFGKNYSELR HRISDSGLLP RWHMMDFFHA FLIIFRILCG
EWIETMWDCM EVSGQSLCLL VFLLVMVIGN LVVLNLFLAL LLSSFSADNL TAPDEDGEMN
NLQLALARIQ RGLRFVKRTT WDFCCGILRR RPKKPAALAT HSQLPSCITA PRSPPPPEVE
KVPPARKETR FEEDKRPGQG TPGDSEPVCV PIAVAESDTE DQEEDEENSL GTEEESSKQE
SQVVSGGHEP YQEPRAWSQV SETTSSEAGA STSQADWQQE QKTEPQAPGC GETPEDSYSE
GSTADMTNTA DLLEQIPDLG EDVKDPEDCF TEGCVRRCPC CMVDTTQSPG KVWWRLRKTC
YRIVEHSWFE TFIIFMILLS SGALAFEDIY LEERKTIKVL LEYADKMFTY VFVLEMLLKW
VAYGFKKYFT NAWCWLDFLI VDVSLVSLVA NTLGFAEMGP IKSLRTLRAL RPLRALSRFE
GMRVVVNALV GAIPSIMNVL LVCLIFWLIF SIMGVNLFAG KFGRCINQTE GDLPLNYTIV
NNKSECESFN VTGELYWTKV KVNFDNVGAG YLALLQVATF KGWMDIMYAA VDSRGYEEQP
QWEDNLYMYI YFVVFIIFGS FFTLNLFIGV IIDNFNQQKK KLGGQDIFMT EEQKKYYNAM
KKLGSKKPQK PIPRPLNKYQ GFIFDIVTKQ AFDVTIMFLI CLNMVTMMVE TDDQSPEKVN
ILAKINLLFV AIFTGECIVK MAALRHYYFT NSWNIFDFVV VILSIVGTVL SDIIQKYFFS
PTLFRVIRLA RIGRILRLIR GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIYSIFGMAN
FAYVKWEAGI DDMFNFQTFA NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLPNSNGS
RGNCGSPAVG ILFFTTYIII SFLIVVNMYI AIILENFSVA TEESTEPLSE DDFDMFYEIW
EKFDPEATQF IEYLALSDFA DALSEPLRIA KPNQISLINM DLPMVSGDRI HCMDILFAFT
KRVLGESGEM DALKIQMEEK FMAANPSKIS YEPITTTLRR KHEEVSATVI QRAFRRHLLQ
RSVKHASFLF RQQAGGSGLS DEDAPEREGL IAYMMNGNFS RRSAPLSSSS ISSTSFPPSY
DSVTRATSDN LPVRASDYSR SEDLADFPPS PDRDRESIV


Related products :

Catalog number Product name Quantity
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
EIAAB37584 HBSC II,Homo sapiens,Human,NAC2,SCN2A,SCN2A1,SCN2A2,Sodium channel protein brain II subunit alpha,Sodium channel protein type 2 subunit alpha,Sodium channel protein type II subunit alpha,Voltage-gated
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
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
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
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
EIAAB37613 Canis familiaris,Canis lupus familiaris,Dog,NaNG,SCN10A,Sodium channel protein type 10 subunit alpha,Sodium channel protein type X subunit alpha,Voltage-gated sodium channel subunit alpha Nav1.8
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


 

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