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Protein

Sodium channel protein type 10 subunit alpha

Gene

SCN10A

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

GO - Molecular functioni

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):
NaNG
Sodium channel protein type X subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.8
Gene namesi
Name:SCN10A
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 125125CytoplasmicSequence analysisAdd
BLAST
Transmembranei126 – 14924Helical; Name=S1 of repeat ISequence analysisAdd
BLAST
Topological domaini150 – 1545ExtracellularSequence analysis
Transmembranei155 – 17420Helical; Name=S2 of repeat ISequence analysisAdd
BLAST
Topological domaini175 – 18713CytoplasmicSequence analysisAdd
BLAST
Transmembranei188 – 20619Helical; Name=S3 of repeat ISequence analysisAdd
BLAST
Topological domaini207 – 2126ExtracellularSequence analysis
Transmembranei213 – 23220Helical; Voltage-sensor; Name=S4 of repeat ISequence analysisAdd
BLAST
Topological domaini233 – 24816CytoplasmicSequence analysisAdd
BLAST
Transmembranei249 – 27224Helical; Name=S5 of repeat ISequence analysisAdd
BLAST
Topological domaini273 – 382110ExtracellularSequence analysisAdd
BLAST
Transmembranei383 – 40826Helical; Name=S6 of repeat ISequence analysisAdd
BLAST
Topological domaini409 – 668260CytoplasmicSequence analysisAdd
BLAST
Transmembranei669 – 69325Helical; Name=S1 of repeat IISequence analysisAdd
BLAST
Topological domaini694 – 70411ExtracellularSequence analysisAdd
BLAST
Transmembranei705 – 72824Helical; Name=S2 of repeat IISequence analysisAdd
BLAST
Topological domaini729 – 7368CytoplasmicSequence analysis
Transmembranei737 – 75620Helical; Name=S3 of repeat IISequence analysisAdd
BLAST
Topological domaini757 – 7626ExtracellularSequence analysis
Transmembranei763 – 78220Helical; Voltage-sensor; Name=S4 of repeat IISequence analysisAdd
BLAST
Topological domaini783 – 79816CytoplasmicSequence analysisAdd
BLAST
Transmembranei799 – 81921Helical; Name=S5 of repeat IISequence analysisAdd
BLAST
Topological domaini820 – 87354ExtracellularSequence analysisAdd
BLAST
Transmembranei874 – 89926Helical; Name=S6 of repeat IISequence analysisAdd
BLAST
Topological domaini900 – 1154255CytoplasmicSequence analysisAdd
BLAST
Transmembranei1155 – 117824Helical; Name=S1 of repeat IIISequence analysisAdd
BLAST
Topological domaini1179 – 119113ExtracellularSequence analysisAdd
BLAST
Transmembranei1192 – 121726Helical; Name=S2 of repeat IIISequence analysisAdd
BLAST
Topological domaini1218 – 12236CytoplasmicSequence analysis
Transmembranei1224 – 124522Helical; Name=S3 of repeat IIISequence analysisAdd
BLAST
Topological domaini1246 – 12494ExtracellularSequence analysis
Transmembranei1250 – 127122Helical; Voltage-sensor; Name=S4 of repeat IIISequence analysisAdd
BLAST
Topological domaini1272 – 129019CytoplasmicSequence analysisAdd
BLAST
Transmembranei1291 – 131828Helical; Name=S5 of repeat IIISequence analysisAdd
BLAST
Topological domaini1319 – 139880ExtracellularSequence analysisAdd
BLAST
Transmembranei1399 – 142527Helical; Name=S6 of repeat IIISequence analysisAdd
BLAST
Topological domaini1426 – 147853CytoplasmicSequence analysisAdd
BLAST
Transmembranei1479 – 150224Helical; Name=S1 of repeat IVSequence analysisAdd
BLAST
Topological domaini1503 – 151311ExtracellularSequence analysisAdd
BLAST
Transmembranei1514 – 153724Helical; Name=S2 of repeat IVSequence analysisAdd
BLAST
Topological domaini1538 – 15436CytoplasmicSequence analysis
Transmembranei1544 – 156724Helical; Name=S3 of repeat IVSequence analysisAdd
BLAST
Topological domaini1568 – 157912ExtracellularSequence analysisAdd
BLAST
Transmembranei1580 – 160122Helical; Voltage-sensor; Name=S4 of repeat IVSequence analysisAdd
BLAST
Topological domaini1602 – 161615CytoplasmicSequence analysisAdd
BLAST
Transmembranei1617 – 163923Helical; Name=S5 of repeat IVSequence analysisAdd
BLAST
Topological domaini1640 – 170465ExtracellularSequence analysisAdd
BLAST
Transmembranei1705 – 172925Helical; Name=S6 of repeat IVSequence analysisAdd
BLAST
Topological domaini1730 – 1962233CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19621962Sodium channel protein type 10 subunit alphaPRO_0000048506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence analysis
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence analysis
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence analysis
Modified residuei450 – 4501PhosphoserineBy similarity
Modified residuei453 – 4531PhosphoserineBy similarity
Modified residuei476 – 4761PhosphoserineBy similarity
Modified residuei488 – 4881PhosphoserineBy similarity
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei624 – 6241PhosphoserineBy similarity
Glycosylationi828 – 8281N-linked (GlcNAc...)Sequence analysis
Glycosylationi1319 – 13191N-linked (GlcNAc...)Sequence analysis
Glycosylationi1335 – 13351N-linked (GlcNAc...)Sequence analysis
Glycosylationi1343 – 13431N-linked (GlcNAc...)Sequence analysis
Modified residuei1458 – 14581Phosphoserine; by PKCBy similarity
Glycosylationi1693 – 16931N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Ubiquitinated by NEDD4L; which promotes its endocytosis.By similarity
Phosphorylation at Ser-1458 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

PaxDbiO46669.
PRIDEiO46669.

Expressioni

Tissue specificityi

Expressed in nodose ganglia, but not in cortex, hippocampus, cerebellum, liver, heart and skeletal muscle.1 Publication

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 similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000011447.

Structurei

3D structure databases

ProteinModelPortaliO46669.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati116 – 414299ICuratedAdd
BLAST
Repeati656 – 920265IICuratedAdd
BLAST
Repeati1147 – 1456310IIICuratedAdd
BLAST
Repeati1465 – 1764300IVCuratedAdd
BLAST
Domaini1858 – 188730IQAdd
BLAST

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.Curated

Sequence similaritiesi

Contains 1 IQ domain.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOGENOMiHOG000231755.
HOVERGENiHBG053100.
InParanoidiO46669.
KOiK04842.

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.

Sequencei

Sequence statusi: Complete.

O46669-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFPFGSLET TNFRRFTPES LVEIEKRIAA KQAAKKAKGK HREQKDQEEK
60 70 80 90 100
PRPQLDLKAC NQPPKFYGEL PAELVGEPLE DLDPFYSTHR TFMVLDKGRT
110 120 130 140 150
ISRFSATRAL WLFSPFNLIR RTAIKVSVHS WFSLFITVTI LVNCVGMTQT
160 170 180 190 200
ELPDRIEYVF TVIYTFEALI KILARGFCLN EFAYLRDPWD WLDFSVITLA
210 220 230 240 250
YIGEATALRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI HSVRKLADVT
260 270 280 290 300
ILTVFCLSVF ALVGLQLFKG NLKNKCVKNC AALNETGNYS SYGKQEWNFC
310 320 330 340 350
HRDEDFYYNK PGTSDPLLCG NGSDAGHCPK GYLCLKTSDN PDFNYTSFDS
360 370 380 390 400
FAWAFLSLFR LMTQDSWERL YQQTLRASGK MYMVFFVLVI FLGSFYLVNL
410 420 430 440 450
ILAVVTMAYE EQNQATIDEI EAKEKTFQET LEMPRKEQEV LAALGIDTAS
460 470 480 490 500
LHSCNGSPLP SKNASERMRR MKPRVSEGST DDNKSPQSDP YNQRRMSFLG
510 520 530 540 550
LTSGRRRASH GSVFHFRTPC LDTSFPDGVT DDGVFPGDRE SHRGSLLLGG
560 570 580 590 600
GTSQQGPLLR SPLPQPPNPG SGHGEDGHST LPTGELAPGG IEVSAFDAGQ
610 620 630 640 650
KKTFLSAEYL NEPFRAQRAM SVVSIMTSVL EELEESERRC PPCLTSFAQK
660 670 680 690 700
YLIWECCPTW VKLKTVLFGI VTDPFAELTT TLCIVVNTVF MAMEHHGMSS
710 720 730 740 750
AFEAMLQIGN IVFTVFFTAE MVFKIIAFDP YYYFQKRWNI FDCIIVTVSL
760 770 780 790 800
IELGAARKGS LSVLRTFRLL RVFKLAKSWP TLNTLIKIIG NSVGALGNLT
810 820 830 840 850
IILAIIVFVF ALVGKQLLGE NYRDNRRNIS APNEEWPRWH MHDFFHSFLI
860 870 880 890 900
VFRILCGEWI ENMWACMEVG QKSICLILFL TVMVLGNLVV LNLFTALLLN
910 920 930 940 950
SFSADNLATP DEDGEVNNLQ VALARIQAFG HRTKKAICNF FTRPCLLPWP
960 970 980 990 1000
KAEPQLVVKL PLSSSKAENH IAANAAVGSP GGLSVSRGLR DDHSDFITNP
1010 1020 1030 1040 1050
NIWVSVPIAE GESDLDDLEE DGEEDSQSSQ QEVILQGQEQ LQVETCEGHT
1060 1070 1080 1090 1100
APRSPGSGMS SEDLASYVDE KWKDEAVAQA PAEGGDDSSS SGGSTVDCLD
1110 1120 1130 1140 1150
PEEILRKIPE LADDLEEPDD CFTEGCLRRC PCCKVDISKF PWTVGWQVRK
1160 1170 1180 1190 1200
TCYRIVEHSW FESFIIFMIL LSSGSLAFED YHLDQKPTVK ALLEYTDRMF
1210 1220 1230 1240 1250
TFIFVLEMLL KWVAYGFKKY FTNAWCWLDF LIVNISLISL IAKILQYSDV
1260 1270 1280 1290 1300
ASIKALRTLR ALRPLRALSR FEGMRVVVDA LVGAIPSIMN VLLVCLIFWL
1310 1320 1330 1340 1350
IFSTMGVNFF AGKFGRCINK TNEYFSLVPL SIVNNISDCK YQNHTGSFFW
1360 1370 1380 1390 1400
VNVKVNFDNV AMGYLALLQV ATFKGWMDIM YAAVDARDVN LQPKWEDNVY
1410 1420 1430 1440 1450
MYLYFVIFII FGGFFTLNLF VGVIIDNFNQ QKKKLGGQDI FMTEEQKKYY
1460 1470 1480 1490 1500
NAMKKLGSKK PQKPIPRPLN KYQGFVFDIV TKQAFDIVIM VLICLNMITM
1510 1520 1530 1540 1550
MVETDEQSAE KTKILNKINQ FFVAVFTGEC VMKMFALRHY YFTNGWNVFD
1560 1570 1580 1590 1600
FIVVVLSIGS LVFSVILTSL ENYFSPTLFR VIRLARIGRI LRLIRAAKGI
1610 1620 1630 1640 1650
RTLLFALMMS LPALFNIGLL LFLVMFIYSI FGMASFPHVS WEAGIDDMFN
1660 1670 1680 1690 1700
FQTFANSMLC LFQITTSAGW DGLLSPILNT GPPYCDPNLP NSNGSRGNCG
1710 1720 1730 1740 1750
SPAVGILFFT TYIIISFLIV VNMYIAVILE NFNVATQESS EPLSEDDFDM
1760 1770 1780 1790 1800
FYETWEKFDP EATQFITFSA LSDFADTLSG PLRIPKPNQN ILIQMDLPLV
1810 1820 1830 1840 1850
PGDKIHCLDI LFAFTKNVLG ESGELDSLKA NIEEKFMATN VSKASYEPIA
1860 1870 1880 1890 1900
TTLRWKQEDI SATVIQKAYR SYVLHRSMTI SNPPAVPRAE EAVPPPDEAF
1910 1920 1930 1940 1950
VEFMVNENCA LPDKSETASA ASFPPSYDSV TRGLSDQINM STSSSMQNED
1960
EGTSKKVTAP GP
Length:1,962
Mass (Da):220,702
Last modified:June 1, 1998 - v1
Checksum:i5D32D20D4AF47A68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60590 mRNA. Translation: AAC39164.1.
RefSeqiNP_001003203.1. NM_001003203.1.
UniGeneiCfa.3714.

Genome annotation databases

GeneIDi477026.
KEGGicfa:477026.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60590 mRNA. Translation: AAC39164.1.
RefSeqiNP_001003203.1. NM_001003203.1.
UniGeneiCfa.3714.

3D structure databases

ProteinModelPortaliO46669.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000011447.

Proteomic databases

PaxDbiO46669.
PRIDEiO46669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi477026.
KEGGicfa:477026.

Organism-specific databases

CTDi6336.

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOGENOMiHOG000231755.
HOVERGENiHBG053100.
InParanoidiO46669.
KOiK04842.

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_CANLF
AccessioniPrimary (citable) accession number: O46669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.