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Q9WTU3 (SCN8A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 8 subunit alpha
Alternative name(s):
Sodium channel protein type VIII subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.6
Gene names
Name:Scn8a
Synonyms:Nbna1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1978 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. In macrophages, isoform 5 may participate in the control of podosome and invadopodia formation. Ref.8 Ref.9

Subunit structure

Interacts with FGF13; may regulate SCN8A activity By similarity. Interacts with NEDD4 and NEDD4L. Ref.6

Subcellular location

Membrane; Multi-pass membrane protein Ref.8.

Tissue specificity

Expressed in brain, cerebellum and spinal cord. Isoform 5 may be expressed in non-neuronal tissues, such as peritoneal macrophages. Ref.1 Ref.2 Ref.8

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. Ref.9

Post-translational modification

May be ubiquitinated by NEDD4L; which would promote its endocytosis By similarity.

Phosphorylation at Ser-1495 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents By similarity.

Involvement in disease

Defects in Scn8a are the cause of motor endplate disease (med). Med is a recessive neuromuscular disorder that is characterized by lack of signal transmission at the neuromuscular junction, excess preterminal arborization and degeneration of cerebellar Purkinje cells. It produces early onset progressive paralysis of hind limbs, severe muscle atrophy and juvenile lethality. Ref.2 Ref.4 Ref.10

Defects in Scn8a are the cause of the jolting mutant (medjo), a mild form of motor endplate disease which is characterized by the absence of spontaneous, regular, simple discharges from Purkinje cells. After 3 weeks of age, jolting mice are unsteady and have wide-based gait and a rhythmical tremor of head and neck induced by attempted movement. Ref.2 Ref.4 Ref.10

Defects in Scn8a are a cause of degenerating muscle (dmu). Dmu is an autosomal recessive neuromuscular disorder that is characterized by skeletal and cardiac muscle degeneration. It produces early onset progressive loss of mobility of the hind limbs and subsequent lethality in the first month of life. Ref.2 Ref.4 Ref.10

Sequence similarities

Belongs to the sodium channel (TC 1.A.1.10) family. Nav1.6/SCN8A subfamily. [View classification]

Contains 1 IQ domain. Ref.9

Ontologies

Keywords
   Biological processIon transport
Sodium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
Sodium
   Molecular functionIon channel
Sodium channel
Voltage-gated channel
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from mutant phenotype PubMed 3674018. Source: MGI

adult walking behavior

Inferred from mutant phenotype Ref.2. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 12920299. Source: MGI

membrane depolarization during action potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

muscle organ development

Inferred from mutant phenotype PubMed 15170223. Source: MGI

neuromuscular process

Inferred from mutant phenotype PubMed 3674018. Source: MGI

neuronal action potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to toxic substance

Inferred from direct assay PubMed 16029194. Source: MGI

sensory perception of sound

Inferred from mutant phenotype PubMed 12204355. Source: MGI

sodium ion transmembrane transport

Non-traceable author statement Ref.1. Source: GOC

sodium ion transport

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentZ disc

Inferred from direct assay PubMed 17884088. Source: BHF-UCL

dendrite

Inferred from direct assay PubMed 17928448. Source: MGI

membrane

Inferred from direct assay PubMed 17537961. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 17928448. Source: MGI

node of Ranvier

Inferred from direct assay PubMed 11807096. Source: BHF-UCL

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

sodium channel complex

Inferred from physical interaction PubMed 15272007. Source: MGI

voltage-gated sodium channel complex

Inferred by curator Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 22474336. Source: IntAct

voltage-gated sodium channel activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Map1bP148737EBI-6396042,EBI-764653

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.7 (identifier: Q9WTU3-1)

Also known as: 18A;

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 Ref.1 (identifier: Q9WTU3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     428-673: Missing.
Isoform 3 Ref.1 (identifier: Q9WTU3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     664-664: E → EVKIDKAATDS
Isoform 4 Ref.7 (identifier: Q9WTU3-4)

Also known as: 18N;

The sequence of this isoform differs from the canonical sequence as follows:
     1273-1280: SLVSLIAN → PLSLSGLI
     1281-1978: Missing.
Isoform 5 Ref.7 (identifier: Q9WTU3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1272-1312: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19781978Sodium channel protein type 8 subunit alpha
PRO_0000048501

Regions

Topological domain1 – 127127Cytoplasmic Potential
Transmembrane128 – 15124Helical; Name=S1 of repeat I; Potential
Topological domain152 – 1598Extracellular Potential
Transmembrane160 – 17920Helical; Name=S2 of repeat I; Potential
Topological domain180 – 19213Cytoplasmic Potential
Transmembrane193 – 21119Helical; Name=S3 of repeat I; Potential
Topological domain212 – 2176Extracellular Potential
Transmembrane218 – 23720Helical; Name=S4 of repeat I; Potential
Topological domain238 – 25215Cytoplasmic Potential
Transmembrane253 – 27725Helical; Voltage-sensor; Name=S5 of repeat I; Potential
Topological domain278 – 387110Extracellular Potential
Transmembrane388 – 41326Helical; Name=S6 of repeat I; Potential
Topological domain414 – 745332Cytoplasmic Potential
Transmembrane746 – 77025Helical; Name=S1 of repeat II; Potential
Topological domain771 – 78111Extracellular Potential
Transmembrane782 – 80524Helical; Name=S2 of repeat II; Potential
Topological domain806 – 8138Cytoplasmic Potential
Transmembrane814 – 83320Helical; Name=S3 of repeat II; Potential
Topological domain834 – 8396Extracellular Potential
Transmembrane840 – 86021Helical; Voltage-sensor; Name=S4 of repeat II; Potential
Topological domain861 – 87515Cytoplasmic Potential
Transmembrane876 – 89621Helical; Name=S5 of repeat II; Potential
Topological domain897 – 94953Extracellular Potential
Transmembrane950 – 97526Helical; Name=S6 of repeat II; Potential
Topological domain976 – 1191216Cytoplasmic Potential
Transmembrane1192 – 121524Helical; Name=S1 of repeat III; Potential
Topological domain1216 – 122813Extracellular Potential
Transmembrane1229 – 125426Helical; Name=S2 of repeat III; Potential
Topological domain1255 – 12606Cytoplasmic Potential
Transmembrane1261 – 128222Helical; Name=S3 of repeat III; Potential
Topological domain1283 – 12864Extracellular Potential
Transmembrane1287 – 130822Helical; Voltage-sensor; Name=S4 of repeat III; Potential
Topological domain1309 – 132719Cytoplasmic Potential
Transmembrane1328 – 134922Helical; Name=S5 of repeat III; Potential
Topological domain1350 – 143586Extracellular Potential
Transmembrane1436 – 146227Helical; Name=S6 of repeat III; Potential
Topological domain1463 – 151553Cytoplasmic Potential
Transmembrane1516 – 153924Helical; Name=S1 of repeat IV; Potential
Topological domain1540 – 155011Extracellular Potential
Transmembrane1551 – 157424Helical; Name=S2 of repeat IV; Potential
Topological domain1575 – 15806Cytoplasmic Potential
Transmembrane1581 – 160424Helical; Name=S3 of repeat IV; Potential
Topological domain1605 – 161410Extracellular Potential
Transmembrane1615 – 163622Helical; Voltage-sensor; Name=S4 of repeat IV; Potential
Topological domain1637 – 165115Cytoplasmic Potential
Transmembrane1652 – 167423Helical; Name=S5 of repeat IV; Potential
Topological domain1675 – 173965Extracellular Potential
Transmembrane1740 – 176425Helical; Name=S6 of repeat IV; Potential
Topological domain1765 – 1978214Cytoplasmic Potential
Repeat114 – 442329I Ref.9
Repeat733 – 1005273II Ref.9
Repeat1178 – 1493316III Ref.9
Repeat1502 – 1799298IV Ref.9
Domain1893 – 192230IQ Ref.9
Nucleotide binding891 – 8988ATP Potential Ref.9

Amino acid modifications

Modified residue14951Phosphoserine; by PKC By similarity
Glycosylation2151N-linked (GlcNAc...) Potential Ref.9
Glycosylation2891N-linked (GlcNAc...) Potential Ref.9
Glycosylation2951N-linked (GlcNAc...) Potential Ref.9
Glycosylation3081N-linked (GlcNAc...) Potential Ref.9
Glycosylation3261N-linked (GlcNAc...) Potential Ref.9
Glycosylation13561N-linked (GlcNAc...) Potential Ref.9
Glycosylation13701N-linked (GlcNAc...) Potential Ref.9
Glycosylation13811N-linked (GlcNAc...) Potential Ref.9

Natural variations

Alternative sequence428 – 673246Missing in isoform 2. Ref.9
VSP_050594
Alternative sequence6641E → EVKIDKAATDS in isoform 3. Ref.1
VSP_050595
Alternative sequence1272 – 131241Missing in isoform 5. Ref.7
VSP_050598
Alternative sequence1273 – 12808SLVSLIAN → PLSLSGLI in isoform 4. Ref.7
VSP_050596
Alternative sequence1281 – 1978698Missing in isoform 4. Ref.7
VSP_050597
Natural variant51V → L. Ref.3 Ref.9
Natural variant13171A → T in medjo. Ref.9

Experimental info

Sequence conflict2071V → I in BAE34580. Ref.3
Sequence conflict2121D → N in BAE34580. Ref.3
Sequence conflict5541P → T in BAE34580. Ref.3
Sequence conflict5961G → D in BAE34580. Ref.3
Sequence conflict14981P → A in AAA65599. Ref.5
Sequence conflict15041R → E in AAA65599. Ref.5

Secondary structure

... 1978
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (18A) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 9EA4A8E610707220

FASTA1,978225,141
        10         20         30         40         50         60 
MAARVLAPPG PDSFKPFTPE SLANIERRIA ESKLKKPPKA DGSHREDDED SKPKPNSDLE 

        70         80         90        100        110        120 
AGKSLPFIYG DIPQGLVAVP LEDFDPYYLT QKTFVVLNRG KTLFRFSATP ALYILSPFNL 

       130        140        150        160        170        180 
IRRIAIKILI HSVFSMIIMC TILTNCVFMT FSNPPEWSKN VEYTFTGIYT FESLVKIIAR 

       190        200        210        220        230        240 
GFCIDGFTFL RDPWNWLDFS VIMMAYVTEF VDLGNVSALR TFRVLRALKT ISVIPGLKTI 

       250        260        270        280        290        300 
VGALIQSVKK LSDVMILTVF CLSVFALIGL QLFMGNLRNK CVVWPINFNE SYLENGTRGF 

       310        320        330        340        350        360 
DWEEYINNKT NFYMVPGMLE PLLCGNSSDA GQCPEGFQCM KAGRNPNYGY TSFDTFSWAF 

       370        380        390        400        410        420 
LALFRLMTQD YWENLYQLTL RAAGKTYMIF FVLVIFVGSF YLVNLILAVV AMAYEEQNQA 

       430        440        450        460        470        480 
TLEEAEQKEA EFKAMLEQLK KQQEEAQAAA MATSAGTVSE DAIEEEGEDG VGSPRSSSEL 

       490        500        510        520        530        540 
SKLSSKSAKE RRNRRKKRKQ KELSEGEEKG DPEKVFKSES EDGMRRKAFR LPDNRIGRKF 

       550        560        570        580        590        600 
SIMNQSLLSI PGSPFLSRHN SKSSIFSFRG PGRFRDPGSE NEFADDEHST VEESEGRRDS 

       610        620        630        640        650        660 
LFIPIRARER RSSYSGYSGY SQCSRSSRIF PSLRRSVKRN STVDCNGVVS LIGPGSHIGR 

       670        680        690        700        710        720 
LLPEATTEVE IKKKGPGSLL VSMEQLASYG RKDRINSIMS VVTNTLVEEL EESQRKCPPC 

       730        740        750        760        770        780 
WYKFANTFLI WECHPYWIKL KEIVNLIVMD PFVDLAITIC IVLNTLFMAM EHHPMTPQFE 

       790        800        810        820        830        840 
HVLAVGNLVF TGIFTAEMFL KLIAMDPYYY FQEGWNIFDG FIVSLSLMEL GLADVEGLSV 

       850        860        870        880        890        900 
LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL AIIVFIFAVV GMQLFGKSYK 

       910        920        930        940        950        960 
ECVCKISQEC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW DCMEVAGQAM CLIVFMMVMV 

       970        980        990       1000       1010       1020 
IGNLVVLNLF LALLLSSFSA DNLAATDDDG EMNNLQISVI RIKKGVAWAK VKVHAFMQAH 

      1030       1040       1050       1060       1070       1080 
FKQREADEVK PLDELYEKKA NCIANHTGVD IHRNGDFQKN GNGTTSGIGS SVEKYIIDED 

      1090       1100       1110       1120       1130       1140 
HMSFINNPNL TVRVPIAVGE SDFENLNTED VSSESDPEGS KDKLDDTSSS EGSTIDIKPE 

      1150       1160       1170       1180       1190       1200 
VEEVPVEQPE EYLDPDACFT EGCVQRFKCC QVNIEEGLGK SWWILRKTCF LIVEHNWFET 

      1210       1220       1230       1240       1250       1260 
FIIFMILLSS GALAFEDIYI EQRKTIRTIL EYADKVFTYI FILEMLLKWT AYGFVKFFTN 

      1270       1280       1290       1300       1310       1320 
AWCWLDFLIV AVSLVSLIAN ALGYSELGAI KSLRTLRALR PLRALSRFEG MRVVVNALVG 

      1330       1340       1350       1360       1370       1380 
AIPSIMNVLL VCLIFWLIFS IMGVNLFAGK YHYCFNETSE IRFEIDEVNN KTDCEKLMEG 

      1390       1400       1410       1420       1430       1440 
NNTEIRWKNV KINFDNVGAG YLALLQVATF KGWMDIMYAA VDSRKPDEQP DYEGNIYMYI 

      1450       1460       1470       1480       1490       1500 
YFVIFIIFGS FFTLNLFIGV IIDNFNQQKK KFGGQDIFMT EEQKKYYNAM KKLGSKKPQK 

      1510       1520       1530       1540       1550       1560 
PIPRPLNKIQ GIVFDFVTQQ AFDIVIMMLI CLNMVTMMVE TDTQSKQMEN ILYWINLVFV 

      1570       1580       1590       1600       1610       1620 
IFFTCECVLK MFALRHYYFT IGWNIFDFVV VILSIVGMFL ADIIEKYFVS PTLFRVIRLA 

      1630       1640       1650       1660       1670       1680 
RIGRILRLIK GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIFSIFGMSN FAYVKHEAGI 

      1690       1700       1710       1720       1730       1740 
DDMFNFETFG NSMICLFQIT TSAGWDGLLL PILNRPPDCS LDKEHPGSGF KGDCGNPSVG 

      1750       1760       1770       1780       1790       1800 
IFFFVSYIII SFLIVVNMYI AIILENFSVA TEESADPLSE DDFETFYEIW EKFDPDATQF 

      1810       1820       1830       1840       1850       1860 
IEYCKLADFA DALEHPLRVP KPNTIELIAM DLPMVSGDRI HCLDILFAFT KRVLGDSGEL 

      1870       1880       1890       1900       1910       1920 
DILRQQMEER FVASNPSKVS YEPITTTLRR KQEEVSAVVL QRAYRGHLAR RGFICRKITS 

      1930       1940       1950       1960       1970 
NKLENGGTHR EKKESTPSTA SLPSYDSVTK PDKEKQQRAE EGRRERAKRQ KEVRESKC 

« Hide

Isoform 2 [UniParc].

Checksum: 7A7CF0DB544EBCF6
Show »

FASTA1,732197,648
Isoform 3 [UniParc].

Checksum: 4DF697091BEFF58B
Show »

FASTA1,988226,170
Isoform 4 (18N) [UniParc].

Checksum: 829683D208A54355
Show »

FASTA1,280145,012
Isoform 5 [UniParc].

Checksum: 12C51774C21ADF5E
Show »

FASTA1,937220,659

References

« Hide 'large scale' references
[1]"Exon organization, coding sequence, physical mapping, and polymorphic intragenic markers for the human neuronal sodium channel gene SCN8A."
Plummer N.W., Galt J., Jones J.M., Burgess D.L., Sprunger L.K., Kohrman D.C., Meisler M.H.
Genomics 54:287-296(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 3).
Strain: C57BL/6J.
[2]"Mutation of a new sodium channel gene, Scn8a, in the mouse mutant 'motor endplate disease'."
Burgess D.L., Kohrman D.C., Galt J., Plummer N.W., Jones J.M., Spear B., Meisler M.H.
Nat. Genet. 10:461-465(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DISEASE.
Strain: C57BL/6J.
Tissue: Brain.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-804, VARIANT LEU-5.
Strain: C57BL/6J.
Tissue: Visual cortex.
[4]"Mutation detection in the med and medJ alleles of the sodium channel Scn8a. Unusual splicing due to a minor class AT-AC intron."
Kohrman D.C., Harris J.B., Meisler M.H.
J. Biol. Chem. 271:17576-17581(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-205, DISEASE.
Strain: 129/Sv.
Tissue: Brain.
[5]"A putative novel Na channel alpha subunit cDNA isolated from mouse NB2a neuroblastoma cells."
Fan Z., Kyle J.W., Makielski J.C.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1411-1686.
[6]"Regulation of neuronal voltage-gated sodium channels by the ubiquitin-protein ligases Nedd4 and Nedd4-2."
Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.
J. Biol. Chem. 279:28930-28935(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEDD4 AND NEDD4L.
[7]"Alternative splicing of the sodium channel SCN8A predicts a truncated two-domain protein in fetal brain and non-neuronal cells."
Plummer N.W., McBurney M.W., Meisler M.H.
J. Biol. Chem. 272:24008-24015(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 4 AND 5).
Tissue: Brain and Fetal brain.
[8]"Regulation of podosome formation in macrophages by a splice variant of the sodium channel SCN8A."
Carrithers M.D., Chatterjee G., Carrithers L.M., Offoha R., Iheagwara U., Rahner C., Graham M., Waxman S.G.
J. Biol. Chem. 284:8114-8126(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"A missense mutation in the sodium channel Scn8a is responsible for cerebellar ataxia in the mouse mutant jolting."
Kohrman D.C., Smith M.R., Goldin A.L., Harris J., Meisler M.H.
J. Neurosci. 16:5993-5999(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MEDJO THR-1317, VARIANT LEU-5.
Strain: DBA/2WyDi.
[10]"Pathological and genetic analysis of the degenerating muscle (dmu) mouse: a new allele of Scn8a."
De Repentigny Y., Cote P.D., Pool M., Bernier G., Girard S., Vidal S.M., Kothary R.
Hum. Mol. Genet. 10:1819-1827(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF049617 mRNA. Translation: AAD20438.1.
U26707 mRNA. Translation: AAC52242.1.
AK158609 mRNA. Translation: BAE34580.1.
U59964, U59963 Genomic DNA. Translation: AAC52708.1.
U23158 mRNA. Translation: AAA65599.1.
CCDSCCDS57011.1. [Q9WTU3-1]
RefSeqNP_001070967.1. NM_001077499.2.
NP_035453.2. NM_011323.3.
UniGeneMm.385012.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3WFNX-ray1.95B/C/D/E1893-1914[»]
ProteinModelPortalQ9WTU3.
SMRQ9WTU3. Positions 128-273, 761-975, 1186-1463, 1513-1913.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203103. 3 interactions.
IntActQ9WTU3. 1 interaction.
STRING10090.ENSMUSP00000080842.

Chemistry

BindingDBQ9WTU3.
ChEMBLCHEMBL1914275.
GuidetoPHARMACOLOGY583.

PTM databases

PhosphoSiteQ9WTU3.

Proteomic databases

PaxDbQ9WTU3.
PRIDEQ9WTU3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID20273.
KEGGmmu:20273.
UCSCuc007xsh.1. mouse. [Q9WTU3-1]

Organism-specific databases

CTD6334.
MGIMGI:103169. Scn8a.

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231755.
HOVERGENHBG091796.
KOK04840.
PhylomeDBQ9WTU3.

Gene expression databases

CleanExMM_SCN8A.
GenevestigatorQ9WTU3.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR024583. DUF3451.
IPR005821. Ion_trans_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR008054. Na_channel_a8su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PfamPF11933. DUF3451. 1 hit.
PF00520. Ion_trans. 4 hits.
PF00612. IQ. 1 hit.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSPR00170. NACHANNEL.
PR01667. NACHANNEL8.
SMARTSM00015. IQ. 1 hit.
[Graphical view]
PROSITEPS50096. IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSCN8A. mouse.
NextBio297955.
PROQ9WTU3.
SOURCESearch...

Entry information

Entry nameSCN8A_MOUSE
AccessionPrimary (citable) accession number: Q9WTU3
Secondary accession number(s): Q3TYI3 expand/collapse secondary AC list , Q60828, Q60858, Q62449
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 116 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot