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Protein

Sodium channel protein type 10 subunit alpha

Gene

Scn10a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tetrodotoxin-resistant channel that 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 sodium ions may pass in accordance with their electrochemical gradient. Plays a role in neuropathic pain mechanisms.1 Publication

GO - Molecular functioni

  • ion channel binding Source: MGI
  • voltage-gated sodium channel activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Sodium transport, Transport

Keywords - Ligandi

Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium channel protein type 10 subunit alpha
Alternative name(s):
Peripheral nerve sodium channel 3
Short name:
PN3
Sensory neuron sodium channel
Sodium channel protein type X subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.8
Gene namesi
Name:Scn10a
Synonyms:Sns
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:108029. Scn10a.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 125CytoplasmicSequence analysisAdd BLAST125
Transmembranei126 – 149Helical; Name=S1 of repeat ISequence analysisAdd BLAST24
Topological domaini150 – 154ExtracellularSequence analysis5
Transmembranei155 – 174Helical; Name=S2 of repeat ISequence analysisAdd BLAST20
Topological domaini175 – 187CytoplasmicSequence analysisAdd BLAST13
Transmembranei188 – 206Helical; Name=S3 of repeat ISequence analysisAdd BLAST19
Topological domaini207 – 212ExtracellularSequence analysis6
Transmembranei213 – 232Helical; Voltage-sensor; Name=S4 of repeat ISequence analysisAdd BLAST20
Topological domaini233 – 248CytoplasmicSequence analysisAdd BLAST16
Transmembranei249 – 272Helical; Name=S5 of repeat ISequence analysisAdd BLAST24
Topological domaini273 – 372ExtracellularSequence analysisAdd BLAST100
Transmembranei373 – 398Helical; Name=S6 of repeat ISequence analysisAdd BLAST26
Topological domaini399 – 658CytoplasmicSequence analysisAdd BLAST260
Transmembranei659 – 683Helical; Name=S1 of repeat IISequence analysisAdd BLAST25
Topological domaini684 – 694ExtracellularSequence analysisAdd BLAST11
Transmembranei695 – 718Helical; Name=S2 of repeat IISequence analysisAdd BLAST24
Topological domaini719 – 726CytoplasmicSequence analysis8
Transmembranei727 – 746Helical; Name=S3 of repeat IISequence analysisAdd BLAST20
Topological domaini747 – 752ExtracellularSequence analysis6
Transmembranei753 – 772Helical; Voltage-sensor; Name=S4 of repeat IISequence analysisAdd BLAST20
Topological domaini773 – 788CytoplasmicSequence analysisAdd BLAST16
Transmembranei789 – 809Helical; Name=S5 of repeat IISequence analysisAdd BLAST21
Topological domaini810 – 863ExtracellularSequence analysisAdd BLAST54
Transmembranei864 – 889Helical; Name=S6 of repeat IISequence analysisAdd BLAST26
Topological domaini890 – 1148CytoplasmicSequence analysisAdd BLAST259
Transmembranei1149 – 1172Helical; Name=S1 of repeat IIISequence analysisAdd BLAST24
Topological domaini1173 – 1185ExtracellularSequence analysisAdd BLAST13
Transmembranei1186 – 1211Helical; Name=S2 of repeat IIISequence analysisAdd BLAST26
Topological domaini1212 – 1217CytoplasmicSequence analysis6
Transmembranei1218 – 1239Helical; Name=S3 of repeat IIISequence analysisAdd BLAST22
Topological domaini1240 – 1243ExtracellularSequence analysis4
Transmembranei1244 – 1265Helical; Voltage-sensor; Name=S4 of repeat IIISequence analysisAdd BLAST22
Topological domaini1266 – 1284CytoplasmicSequence analysisAdd BLAST19
Transmembranei1285 – 1312Helical; Name=S5 of repeat IIISequence analysisAdd BLAST28
Topological domaini1313 – 1392ExtracellularSequence analysisAdd BLAST80
Transmembranei1393 – 1419Helical; Name=S6 of repeat IIISequence analysisAdd BLAST27
Topological domaini1420 – 1472CytoplasmicSequence analysisAdd BLAST53
Transmembranei1473 – 1496Helical; Name=S1 of repeat IVSequence analysisAdd BLAST24
Topological domaini1497 – 1507ExtracellularSequence analysisAdd BLAST11
Transmembranei1508 – 1531Helical; Name=S2 of repeat IVSequence analysisAdd BLAST24
Topological domaini1532 – 1537CytoplasmicSequence analysis6
Transmembranei1538 – 1561Helical; Name=S3 of repeat IVSequence analysisAdd BLAST24
Topological domaini1562 – 1573ExtracellularSequence analysisAdd BLAST12
Transmembranei1574 – 1595Helical; Voltage-sensor; Name=S4 of repeat IVSequence analysisAdd BLAST22
Topological domaini1596 – 1610CytoplasmicSequence analysisAdd BLAST15
Transmembranei1611 – 1633Helical; Name=S5 of repeat IVSequence analysisAdd BLAST23
Topological domaini1634 – 1698ExtracellularSequence analysisAdd BLAST65
Transmembranei1699 – 1723Helical; Name=S6 of repeat IVSequence analysisAdd BLAST25
Topological domaini1724 – 1958CytoplasmicSequence analysisAdd BLAST235

GO - Cellular componenti

  • axon Source: MGI
  • C-fiber Source: MGI
  • extracellular exosome Source: MGI
  • plasma membrane Source: MGI
  • voltage-gated sodium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi861Q → E: Sensitive to inhibition by some components of the venom of Centruroides sculpturatus. 1 Publication1
Mutagenesisi1922Y → A: No regulation by NEDD4L. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5158.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000485081 – 1958Sodium channel protein type 10 subunit alphaAdd BLAST1958

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi279N-linked (GlcNAc...)Sequence analysis1
Glycosylationi288N-linked (GlcNAc...)Sequence analysis1
Glycosylationi311N-linked (GlcNAc...)Sequence analysis1
Glycosylationi334N-linked (GlcNAc...)Sequence analysis1
Modified residuei440PhosphoserineBy similarity1
Modified residuei443PhosphoserineBy similarity1
Modified residuei466PhosphoserineBy similarity1
Modified residuei478PhosphoserineBy similarity1
Modified residuei611PhosphoserineBy similarity1
Modified residuei614PhosphoserineBy similarity1
Glycosylationi1323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1329N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1337N-linked (GlcNAc...)Sequence analysis1
Modified residuei1452Phosphoserine; by PKCBy similarity1
Glycosylationi1500N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1687N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Ubiquitinated by NEDD4L; which promotes its endocytosis.Curated
Phosphorylation at Ser-1452 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6QIY3.
PRIDEiQ6QIY3.

PTM databases

iPTMnetiQ6QIY3.
PhosphoSitePlusiQ6QIY3.

Expressioni

Tissue specificityi

Expressed in dorsal root ganglion and trigeminal ganglion.

Gene expression databases

CleanExiMM_SCN10A.

Interactioni

Subunit structurei

The channel consists of an ion conducting pore forming alpha-subunit regulated by one or more associated auxiliary subunits SCN1B, SCN2B and SCN3B; electrophysiological properties may vary depending on the type of the associated beta subunits. Found in a number of complexes with PRX, DYNLT1 and PDZD2. Interacts with proteins such as FSTL1, PRX, DYNLT1, PDZD2, S100A10 and many others (By similarity). Interacts with NEDD4 and NEDD4L.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203097. 2 interactors.
STRINGi10090.ENSMUSP00000081845.

Chemistry databases

BindingDBiQ6QIY3.

Structurei

3D structure databases

ProteinModelPortaliQ6QIY3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati116 – 404ICuratedAdd BLAST289
Repeati646 – 910IICuratedAdd BLAST265
Repeati1141 – 1450IIICuratedAdd BLAST310
Repeati1459 – 1758IVCuratedAdd BLAST300
Domaini1852 – 1881IQAdd BLAST30

Domaini

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.

Sequence similaritiesi

Contains 1 IQ domain.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOGENOMiHOG000231755.
HOVERGENiHBG053100.
InParanoidiQ6QIY3.
KOiK04842.
PhylomeDBiQ6QIY3.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR028809. Na_channel_a10su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PANTHERiPTHR10037:SF208. PTHR10037:SF208. 3 hits.
PfamiPF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSiPR00170. NACHANNEL.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6QIY3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEFPFGSVGT TNFRRFTPES LAEIEKQIAA HRAAKKGRPK QRGQKDKSEK
60 70 80 90 100
PRPQLDLKAC NQLPRFYGEL PAELVGEPLE DLDPFYSTHR TFIVLDKSRT
110 120 130 140 150
ISRFSATWAL WLFSPFNLIR RTAIKVSVHS WFSIFITVTI LVNCVCMTRT
160 170 180 190 200
DLPEKLEYAF TVVYTFEALI KILARGFCLN EFTYLRDPWN WLDFSVITLA
210 220 230 240 250
YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI HSVRKLADVT
260 270 280 290 300
ILTVFCLSVF ALVGLQLFKG NLKNKCIKNG TDPHKADNLS SEMAGDIFIK
310 320 330 340 350
PGTTDPLLCG NGSDAGHCPN DYVCRKTSDN PDFNYTSFDS FAWAFLSLFR
360 370 380 390 400
LMTQDSWERL YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE
410 420 430 440 450
EQSQATIAEI EAKEKKFKEA LEVLQKEQEV LAALGIDTTS LYSHNGSPLA
460 470 480 490 500
PKNANERRPR VKSRMSEGST DDNRSLQSDP YNQRRMSFLG LSSGRRRASH
510 520 530 540 550
SSVFHFRAPS QDVSFPDGIL DDGVFHGDQE SRRSSILLGR GAGQAGPLPR
560 570 580 590 600
SPLPQSPNPG PRRGEEGQRG VPTGELATGA PEGPALDAAG QKNFLSADYL
610 620 630 640 650
NEPFRAQRAM SVVSIMTSVI EELEESKLKC PPCLISLAQK YLIWECCPKW
660 670 680 690 700
KKFKMVLFEL VTDPFAELTI TLCIVVNTVF MAMEHYPMTD AFDAMLQAGN
710 720 730 740 750
IVFTVFFTME MAFKIIAFDP YYYFQKKWNI FDCVIVTVSL LELSTSKKGS
760 770 780 790 800
LSVLRTFRLL RVFKLAKSWP TLNMLIKIIG NSVGALGNLT FILAIIVFIF
810 820 830 840 850
ALVGKQLLSE NYGCRRDGIS VWNGERLRWH MCDFFHSFLV VFRILCGEWI
860 870 880 890 900
ENMWVCMEVS QDYICLTLFL TVMVLGNLVV LNLFIALLLN SFSADNLTAP
910 920 930 940 950
EDDGEVNNLQ VALARIQVFG HRASRAITSY IRSHCRLRWP KVETQLGMKP
960 970 980 990 1000
PLTSCKAENH IATDAVNAAV GNLAKPALGG PKENHGDFIT DPNVWVSVPI
1010 1020 1030 1040 1050
AEGESDLDEL EEDVEHASQS SWQEESPKGQ QELLQQVQKC EDHQAARSPP
1060 1070 1080 1090 1100
SGMSSEDLAP YLGERWQREE SPRVPAEGVD DTSSSEGSTV DCPDPEEILR
1110 1120 1130 1140 1150
KIPELAEELD EPDDCFPEGC TRRCPCCKVN TSKFPWATGW QVRKTCYRIV
1160 1170 1180 1190 1200
EHSWFESFII FMILLSSGAL AFEDNYLEEK PRVKSVLEYT DRVFTFIFVF
1210 1220 1230 1240 1250
EMLLKWVAYG FKKYFTNAWC WLDFLIVNIS LTSLIAKILE YSDVASIKAL
1260 1270 1280 1290 1300
RTLRALRPLR ALSRFEGMRV VVDALVGAIP SIMNVLLVCL IFWLIFSIMG
1310 1320 1330 1340 1350
VNLFAGKFSR CVDTRSNPFS VVNSTFVTNK SDCYNQNNTG HFFWVNVKVN
1360 1370 1380 1390 1400
FDNVAMGYLA LLQVATFKGW MDIMYAAVDS RDINSQPNWE ESLYMYLYFV
1410 1420 1430 1440 1450
VFIIFGGFFT LNLFVGVIID NFNQQKKKLG GQDIFMTEEQ KKYYNAMKKL
1460 1470 1480 1490 1500
GSKKPQKPIP RPLNKYQGFV FDIVTRQAFD IIIMALICLN MITMMVETDN
1510 1520 1530 1540 1550
QSEEKTKVLG RINQFFVAVF TGECVMKMFA LRQYYFTNGW NVFDFIVVIL
1560 1570 1580 1590 1600
SISSLLFSAI LSSLESYFSP TLLRVIRLAR IGRILRLIRA AKGIRTLLFA
1610 1620 1630 1640 1650
LMMSLPALFN IGLLLFLVMF IYSIFGMASF ANVIDEAGID DMFNFKTFGN
1660 1670 1680 1690 1700
SMLCLFQITT SAGWDGLLSP ILNTGPPYCD PNRPNSNGSK GNCGSPAVGI
1710 1720 1730 1740 1750
LFFTTYIIIS FLIVVNMYIA VILENFNVAT EESTEPLSED DFDMFYETWE
1760 1770 1780 1790 1800
KFDPEATQFI AFSALSDFAD TLSGPLRIPK PNQNILIQMD LPLVPGDKIH
1810 1820 1830 1840 1850
CLDILFAFTK NVLGESGELD SLKTNMEEKF MATNLSKASY EPIATTLRCK
1860 1870 1880 1890 1900
QEDISATIIQ KAYRNYMLQR SLMLSNPLHV PRAEEDGVSL PREGYVTFMA
1910 1920 1930 1940 1950
NDNGGLPDKS ETASATSFPP SYDSVTRGLS DRANISTSSS MQNEDEVTAK

EGKSPGPQ
Length:1,958
Mass (Da):220,552
Last modified:December 21, 2004 - v2
Checksum:i24830634E86490FF
GO
Isoform 2 (identifier: Q6QIY3-2) [UniParc]FASTAAdd to basket
Also known as: Nav1.8c

The sequence of this isoform differs from the canonical sequence as follows:
     1030-1030: Missing.

Show »
Length:1,957
Mass (Da):220,424
Checksum:i23426D535A65601D
GO
Isoform 3 (identifier: Q6QIY3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1435: Missing.

Show »
Length:523
Mass (Da):58,512
Checksum:iD9DB3D0D96A3C622
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0122561 – 1435Missing in isoform 3. CuratedAdd BLAST1435
Alternative sequenceiVSP_0122571030Missing in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ622906 Genomic DNA. Translation: CAF22039.1.
AJ623269 mRNA. Translation: CAF25039.1.
AJ623270 mRNA. Translation: CAF25040.1.
L42342 mRNA. Translation: AAA68000.1.
AY538273 mRNA. Translation: AAS45602.1.
CCDSiCCDS57716.1. [Q6QIY3-1]
RefSeqiNP_033160.2. NM_009134.3. [Q6QIY3-2]
XP_017168712.1. XM_017313223.1. [Q6QIY3-1]
UniGeneiMm.247042.
Mm.455125.
Mm.489505.

Genome annotation databases

GeneIDi20264.
KEGGimmu:20264.
UCSCiuc009sbf.2. mouse. [Q6QIY3-3]
uc009sbg.3. mouse. [Q6QIY3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ622906 Genomic DNA. Translation: CAF22039.1.
AJ623269 mRNA. Translation: CAF25039.1.
AJ623270 mRNA. Translation: CAF25040.1.
L42342 mRNA. Translation: AAA68000.1.
AY538273 mRNA. Translation: AAS45602.1.
CCDSiCCDS57716.1. [Q6QIY3-1]
RefSeqiNP_033160.2. NM_009134.3. [Q6QIY3-2]
XP_017168712.1. XM_017313223.1. [Q6QIY3-1]
UniGeneiMm.247042.
Mm.455125.
Mm.489505.

3D structure databases

ProteinModelPortaliQ6QIY3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203097. 2 interactors.
STRINGi10090.ENSMUSP00000081845.

Chemistry databases

BindingDBiQ6QIY3.
ChEMBLiCHEMBL5158.

PTM databases

iPTMnetiQ6QIY3.
PhosphoSitePlusiQ6QIY3.

Proteomic databases

PaxDbiQ6QIY3.
PRIDEiQ6QIY3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi20264.
KEGGimmu:20264.
UCSCiuc009sbf.2. mouse. [Q6QIY3-3]
uc009sbg.3. mouse. [Q6QIY3-2]

Organism-specific databases

CTDi6336.
MGIiMGI:108029. Scn10a.

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOGENOMiHOG000231755.
HOVERGENiHBG053100.
InParanoidiQ6QIY3.
KOiK04842.
PhylomeDBiQ6QIY3.

Miscellaneous databases

PROiQ6QIY3.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SCN10A.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR028809. Na_channel_a10su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PANTHERiPTHR10037:SF208. PTHR10037:SF208. 3 hits.
PfamiPF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSiPR00170. NACHANNEL.
ProtoNetiSearch...

Entry informationi

Entry nameiSCNAA_MOUSE
AccessioniPrimary (citable) accession number: Q6QIY3
Secondary accession number(s): Q62243
, Q6EWG7, Q6KCH7, Q703F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Mus musculus is sensitive to the pain-inducing components of the bark scorpion (Centruroides sculpturatus) venom while Onychomys torridus is not. Gln-861 may account for the difference between both rodents and its replacement by a glutamate, the corresponding amino acid found in the Onychomys torridus ortholog, allows inhibition of Snc10a by the venom, which in turn, inhibits sodium currents, blocks action potential propagation and may induce analgesia (PubMed:24159039).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.