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Q62968 (SCNAA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Scn10a
Synonyms:Sns
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1956 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.9

Subunit structure

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. Interacts with NEDD4 and NEDD4L. Ref.3 Ref.7 Ref.8

Subcellular location

Membrane; Multi-pass membrane protein By similarity. Note: It can be translocated to the extracellular membrane through association with S100A10. Ref.7

Tissue specificity

Expressed in dorsal root ganglia, trigeminal ganglia, nodose ganglia and sciatic nerve. Ref.1 Ref.2 Ref.6

Developmental stage

Expressed in dorsal root ganglia at 15 dpc onwards. Ref.6

Induction

Down-regulated after axotomy in dorsal root ganglia. Ref.5

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.

Post-translational modification

Ubiquitinated by NEDD4L; which promotes its endocytosis By similarity.

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.

Sequence similarities

Belongs to the sodium channel (TC 1.A.1.10) family. Nav1.8/SCN10A subfamily. [View classification]

Contains 1 IQ domain.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q62968-1)

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.
Isoform 2 (identifier: Q62968-2)

Also known as: Nav1.8c;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19561956Sodium channel protein type 10 subunit alpha
PRO_0000048509

Regions

Transmembrane126 – 14924Helical; Name=S1 of repeat I; Potential
Transmembrane155 – 17420Helical; Name=S2 of repeat I; Potential
Transmembrane188 – 20619Helical; Name=S3 of repeat I; Potential
Transmembrane213 – 23220Helical; Voltage-sensor; Name=S4 of repeat I; Potential
Transmembrane249 – 27224Helical; Name=S5 of repeat I; Potential
Transmembrane373 – 39826Helical; Name=S6 of repeat I; Potential
Transmembrane659 – 68325Helical; Name=S1 of repeat II; Potential
Transmembrane695 – 71824Helical; Name=S2 of repeat II; Potential
Transmembrane727 – 74620Helical; Name=S3 of repeat II; Potential
Transmembrane753 – 77220Helical; Voltage-sensor; Name=S4 of repeat II; Potential
Transmembrane789 – 80921Helical; Name=S5 of repeat II; Potential
Transmembrane864 – 88926Helical; Name=S6 of repeat II; Potential
Transmembrane1149 – 117224Helical; Name=S1 of repeat III; Potential
Transmembrane1186 – 121126Helical; Name=S2 of repeat III; Potential
Transmembrane1218 – 123922Helical; Name=S3 of repeat III; Potential
Transmembrane1244 – 126522Helical; Voltage-sensor; Name=S4 of repeat III; Potential
Transmembrane1285 – 131228Helical; Name=S5 of repeat III; Potential
Transmembrane1393 – 141927Helical; Name=S6 of repeat III; Potential
Transmembrane1473 – 149624Helical; Name=S1 of repeat IV; Potential
Transmembrane1508 – 153124Helical; Name=S2 of repeat IV; Potential
Transmembrane1538 – 156124Helical; Name=S3 of repeat IV; Potential
Transmembrane1574 – 159522Helical; Voltage-sensor; Name=S4 of repeat IV; Potential
Transmembrane1611 – 163323Helical; Name=S5 of repeat IV; Potential
Transmembrane1699 – 172325Helical; Name=S6 of repeat IV; Potential
Repeat125 – 399275I
Repeat658 – 890233II
Repeat1148 – 1420273III
Repeat1472 – 1724253IV
Domain1852 – 188130IQ

Amino acid modifications

Modified residue14521Phosphoserine; by PKC By similarity
Glycosylation2791N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation13231N-linked (GlcNAc...) Potential
Glycosylation13291N-linked (GlcNAc...) Potential
Glycosylation13371N-linked (GlcNAc...) Potential
Glycosylation16871N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence10301Missing in isoform 2.
VSP_012258

Experimental info

Sequence conflict591A → D in CAA63095. Ref.1
Sequence conflict4321A → E in CAA63095. Ref.1
Sequence conflict5201T → TP in CAA63095. Ref.1
Sequence conflict5871D → H in CAA63095. Ref.1
Sequence conflict7571F → L in CAA63095. Ref.1
Sequence conflict9381R → H in CAA63095. Ref.1
Sequence conflict18961V → I in CAA63095. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8FC58EDAD263AC67

FASTA1,956219,733
        10         20         30         40         50         60 
MELPFASVGT TNFRRFTPES LAEIEKQIAA HRAAKKARTK HRGQEDKGEK PRPQLDLKAC 

        70         80         90        100        110        120 
NQLPKFYGEL PAELVGEPLE DLDPFYSTHR TFMVLNKSRT ISRFSATWAL WLFSPFNLIR 

       130        140        150        160        170        180 
RTAIKVSVHS WFSIFITITI LVNCVCMTRT DLPEKVEYVF TVIYTFEALI KILARGFCLN 

       190        200        210        220        230        240 
EFTYLRDPWN WLDFSVITLA YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI 

       250        260        270        280        290        300 
HSVRKLADVT ILTVFCLSVF ALVGLQLFKG NLKNKCIRNG TDPHKADNLS SEMAEYIFIK 

       310        320        330        340        350        360 
PGTTDPLLCG NGSDAGHCPG GYVCLKTPDN PDFNYTSFDS FAWAFLSLFR LMTQDSWERL 

       370        380        390        400        410        420 
YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE EQSQATIAEI EAKEKKFQEA 

       430        440        450        460        470        480 
LEVLQKEQEV LAALGIDTTS LQSHSGSPLA SKNANERRPR VKSRVSEGST DDNRSPQSDP 

       490        500        510        520        530        540 
YNQRRMSFLG LSSGRRRASH GSVFHFRAPS QDISFPDGIT DDGVFHGDQE SRRGSILLGR 

       550        560        570        580        590        600 
GAGQTGPLPR SPLPQSPNPG RRHGEEGQLG VPTGELTAGA PEGPALDTTG QKSFLSAGYL 

       610        620        630        640        650        660 
NEPFRAQRAM SVVSIMTSVI EELEESKLKC PPCLISFAQK YLIWECCPKW RKFKMALFEL 

       670        680        690        700        710        720 
VTDPFAELTI TLCIVVNTVF MAMEHYPMTD AFDAMLQAGN IVFTVFFTME MAFKIIAFDP 

       730        740        750        760        770        780 
YYYFQKKWNI FDCVIVTVSL LELSASKKGS LSVLRTFRLL RVFKLAKSWP TLNTLIKIIG 

       790        800        810        820        830        840 
NSVGALGNLT FILAIIVFIF ALVGKQLLSE DYGCRKDGVS VWNGEKLRWH MCDFFHSFLV 

       850        860        870        880        890        900 
VFRILCGEWI ENMWVCMEVS QKSICLILFL TVMVLGNLVV LNLFIALLLN SFSADNLTAP 

       910        920        930        940        950        960 
EDDGEVNNLQ LALARIQVLG HRASRAIASY ISSHCRFRWP KVETQLGMKP PLTSSEAKNH 

       970        980        990       1000       1010       1020 
IATDAVSAAV GNLTKPALSS PKENHGDFIT DPNVWVSVPI AEGESDLDEL EEDMEQASQS 

      1030       1040       1050       1060       1070       1080 
SWQEEDPKGQ QEQLPQVQKC ENHQAARSPA SMMSSEDLAP YLGESWKRKD SPQVPAEGVD 

      1090       1100       1110       1120       1130       1140 
DTSSSEGSTV DCPDPEEILR KIPELADDLD EPDDCFTEGC TRRCPCCNVN TSKSPWATGW 

      1150       1160       1170       1180       1190       1200 
QVRKTCYRIV EHSWFESFII FMILLSSGAL AFEDNYLEEK PRVKSVLEYT DRVFTFIFVF 

      1210       1220       1230       1240       1250       1260 
EMLLKWVAYG FKKYFTNAWC WLDFLIVNIS LTSLIAKILE YSDVASIKAL RTLRALRPLR 

      1270       1280       1290       1300       1310       1320 
ALSRFEGMRV VVDALVGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFSK CVDTRNNPFS 

      1330       1340       1350       1360       1370       1380 
NVNSTMVNNK SECHNQNSTG HFFWVNVKVN FDNVAMGYLA LLQVATFKGW MDIMYAAVDS 

      1390       1400       1410       1420       1430       1440 
GEINSQPNWE NNLYMYLYFV VFIIFGGFFT LNLFVGVIID NFNQQKKKLG GQDIFMTEEQ 

      1450       1460       1470       1480       1490       1500 
KKYYNAMKKL GSKKPQKPIP RPLNKYQGFV FDIVTRQAFD IIIMVLICLN MITMMVETDE 

      1510       1520       1530       1540       1550       1560 
QGEEKTKVLG RINQFFVAVF TGECVMKMFA LRQYYFTNGW NVFDFIVVIL SIGSLLFSAI 

      1570       1580       1590       1600       1610       1620 
LKSLENYFSP TLFRVIRLAR IGRILRLIRA AKGIRTLLFA LMMSLPALFN IGLLLFLVMF 

      1630       1640       1650       1660       1670       1680 
IYSIFGMASF ANVVDEAGID DMFNFKTFGN SMLCLFQITT SAGWDGLLSP ILNTGPPYCD 

      1690       1700       1710       1720       1730       1740 
PNLPNSNGSR GNCGSPAVGI IFFTTYIIIS FLIVVNMYIA VILENFNVAT EESTEPLSED 

      1750       1760       1770       1780       1790       1800 
DFDMFYETWE KFDPEATQFI AFSALSDFAD TLSGPLRIPK PNQNILIQMD LPLVPGDKIH 

      1810       1820       1830       1840       1850       1860 
CLDILFAFTK NVLGESGELD SLKTNMEEKF MATNLSKASY EPIATTLRWK QEDLSATVIQ 

      1870       1880       1890       1900       1910       1920 
KAYRSYMLHR SLTLSNTLHV PRAEEDGVSL PGEGYVTFMA NSGLPDKSET ASATSFPPSY 

      1930       1940       1950 
DSVTRGLSDR ANINPSSSMQ NEDEVAAKEG NSPGPQ 

« Hide

Isoform 2 (Nav1.8c) [UniParc].

Checksum: 4C6677DF46388F43
Show »

FASTA1,955219,605

References

[1]"A tetrodotoxin-resistant voltage-gated sodium channel expressed by sensory neurons."
Akopian A.N., Sivilotti L., Wood J.N.
Nature 379:257-262(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION.
Tissue: Spinal ganglion.
[2]"Structure and function of a novel voltage-gated, tetrodotoxin-resistant sodium channel specific to sensory neurons."
Sangameswaran L., Delgado S.G., Fish L.M., Koch B.D., Jakeman L.B., Stewart G.R., Sze P., Hunter J.C., Eglen R.M., Herman R.C.
J. Biol. Chem. 271:5953-5956(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION.
Strain: Sprague-Dawley.
Tissue: Spinal ganglion.
[3]"Role of auxiliary beta1-, beta2-, and beta3-subunits and their interaction with Na(v)1.8 voltage-gated sodium channel."
Vijayaragavan K., Powell A.J., Kinghorn I.J., Chahine M.
Biochem. Biophys. Res. Commun. 319:531-540(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), INTERACTION WITH SCN1B; SCN2B AND SCN3B.
Strain: Sprague-Dawley.
Tissue: Spinal ganglion.
[4]"Novel isoforms of the sodium channels Nav1.8 and Nav1.5 are produced by a conserved mechanism in mouse and rat."
Kerr N.C.H., Holmes F.E., Wynick D.
J. Biol. Chem. 279:24826-24833(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 963-1097 (ISOFORMS 1 AND 2).
Strain: Wistar.
Tissue: Spinal ganglion and Trigeminal ganglion.
[5]"Unilateral nerve injury down-regulates mRNA for Na+ channel SCN10A bilaterally in rat dorsal root ganglia."
Oaklander A.L., Belzberg A.J.
Brain Res. Mol. Brain Res. 52:162-165(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"Developmental expression of the TTX-resistant voltage-gated sodium channels Nav1.8 (SNS) and Nav1.9 (SNS2) in primary sensory neurons."
Benn S.C., Costigan M., Tate S., Fitzgerald M., Woolf C.J.
J. Neurosci. 21:6077-6085(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"Annexin II light chain regulates sensory neuron-specific sodium channel expression."
Okuse K., Malik-Hall M., Baker M.D., Poon W.-Y.L., Kong H., Chao M.V., Wood J.N.
Nature 417:653-656(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH S100A10.
[8]"Sensory neuron proteins interact with the intracellular domains of sodium channel NaV1.8."
Malik-Hall M., Poon W.-Y.L., Baker M.D., Wood J.N., Okuse K.
Brain Res. Mol. Brain Res. 110:298-304(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FSTL1; PRX; DYNLT1 AND PDZD2, IDENTIFICATION IN COMPLEXES WITH PRX; DYNLT1 AND PDZD2.
[9]"Redistribution of Na(V)1.8 in uninjured axons enables neuropathic pain."
Gold M.S., Weinreich D., Kim C.-S., Wang R., Treanor J., Porreca F., Lai J.
J. Neurosci. 23:158-166(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92184 mRNA. Translation: CAA63095.1.
U53833 Genomic DNA. Translation: AAC52619.1.
AJ623271 mRNA. Translation: CAF25041.1.
PIRS68453.
RefSeqNP_058943.1. NM_017247.1.
XP_006244144.1. XM_006244082.1.
UniGeneRn.10246.

3D structure databases

ProteinModelPortalQ62968.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ62968. 23 interactions.

Chemistry

BindingDBQ62968.
ChEMBLCHEMBL4017.
GuidetoPHARMACOLOGY585.

Protein family/group databases

TCDB1.A.1.10.6. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteQ62968.

Proteomic databases

PaxDbQ62968.
PRIDEQ62968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29571.
KEGGrno:29571.
UCSCRGD:3629. rat. [Q62968-1]

Organism-specific databases

CTD6336.
RGD3629. Scn10a.

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231755.
HOVERGENHBG053100.
InParanoidQ62968.
KOK04842.
TreeFamTF323985.

Gene expression databases

ArrayExpressQ62968.
GenevestigatorQ62968.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR028809. Na_channel_a10su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PANTHERPTHR10037:SF170. PTHR10037:SF170. 1 hit.
PfamPF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSPR00170. NACHANNEL.
ProtoNetSearch...

Other

NextBio609654.
PROQ62968.

Entry information

Entry nameSCNAA_RAT
AccessionPrimary (citable) accession number: Q62968
Secondary accession number(s): Q63554, Q6EWG6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families