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Q9ER60 (SCN4A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium channel protein type 4 subunit alpha
Alternative name(s):
Sodium channel protein skeletal muscle subunit alpha
Sodium channel protein type IV subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.4
Gene names
Name:Scn4a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1841 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. This sodium channel may be present in both denervated and innervated skeletal muscle.

Subunit structure

Muscle sodium channels contain an alpha subunit and a smaller beta subunit. Interacts with the PDZ domain of the syntrophin SNTA1, SNTB1 and SNTB2 By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in the myocardium. Ref.1

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

Phosphorylation at Ser-1322 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. Nav1.4/SCN4A subfamily. [View classification]

Contains 1 IQ domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18411841Sodium channel protein type 4 subunit alpha
PRO_0000371316

Regions

Topological domain1 – 128128Cytoplasmic Potential
Transmembrane129 – 15022Helical; Name=S1 of repeat I; Potential
Topological domain151 – 1588Extracellular Potential
Transmembrane159 – 17820Helical; Name=S2 of repeat I; Potential
Topological domain179 – 19012Cytoplasmic Potential
Transmembrane191 – 21020Helical; Name=S3 of repeat I; Potential
Topological domain211 – 2166Extracellular Potential
Transmembrane217 – 23620Helical; Voltage-sensor; Name=S4 of repeat I; Potential
Topological domain237 – 25216Cytoplasmic Potential
Transmembrane253 – 26614Helical; Name=S5 of repeat I; Potential
Topological domain267 – 417151Extracellular Potential
Transmembrane418 – 44326Helical; Name=S6 of repeat I; Potential
Topological domain444 – 567124Cytoplasmic Potential
Transmembrane568 – 59124Helical; Name=S1 of repeat II; Potential
Topological domain592 – 60211Extracellular Potential
Transmembrane603 – 62624Helical; Name=S2 of repeat II; Potential
Topological domain627 – 6348Cytoplasmic Potential
Transmembrane635 – 65420Helical; Name=S3 of repeat II; Potential
Topological domain655 – 6606Extracellular Potential
Transmembrane661 – 68020Helical; Voltage-sensor; Name=S4 of repeat II; Potential
Topological domain681 – 69515Cytoplasmic Potential
Transmembrane696 – 71823Helical; Name=S5 of repeat II; Potential
Topological domain719 – 77052Extracellular Potential
Transmembrane771 – 79626Helical; Name=S6 of repeat II; Potential
Topological domain797 – 1020224Cytoplasmic Potential
Transmembrane1021 – 104323Helical; Name=S1 of repeat III; Potential
Topological domain1044 – 105714Extracellular Potential
Transmembrane1058 – 108326Helical; Name=S2 of repeat III; Potential
Topological domain1084 – 10896Cytoplasmic Potential
Transmembrane1090 – 111021Helical; Name=S3 of repeat III; Potential
Topological domain1111 – 11155Extracellular Potential
Transmembrane1116 – 113722Helical; Voltage-sensor; Name=S4 of repeat III; Potential
Topological domain1138 – 115619Cytoplasmic Potential
Transmembrane1157 – 117822Helical; Name=S5 of repeat III; Potential
Topological domain1179 – 126284Extracellular Potential
Transmembrane1263 – 128927Helical; Name=S6 of repeat III; Potential
Topological domain1290 – 134253Cytoplasmic Potential
Transmembrane1343 – 136624Helical; Name=S1 of repeat IV; Potential
Topological domain1367 – 137711Extracellular Potential
Transmembrane1378 – 140124Helical; Name=S2 of repeat IV; Potential
Topological domain1402 – 14076Cytoplasmic Potential
Transmembrane1408 – 143124Helical; Name=S3 of repeat IV; Potential
Topological domain1432 – 14409Extracellular Potential
Transmembrane1441 – 146323Helical; Voltage-sensor; Name=S4 of repeat IV; Potential
Topological domain1464 – 147815Cytoplasmic Potential
Transmembrane1479 – 150123Helical; Name=S5 of repeat IV; Potential
Topological domain1502 – 156766Extracellular Potential
Transmembrane1568 – 159225Helical; Name=S6 of repeat IV; Potential
Topological domain1593 – 1841249Cytoplasmic Potential
Repeat128 – 444317I
Repeat565 – 790226II
Repeat1018 – 1275258III
Repeat1343 – 1589247IV
Domain1721 – 175030IQ

Amino acid modifications

Modified residue13221Phosphoserine; by PKC By similarity
Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3271N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation11851N-linked (GlcNAc...) Potential
Glycosylation11991N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1311A → T in CAM23795. Ref.2
Sequence conflict10561R → Q in CAM23795. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9ER60 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 0766DFD33A9E0E55

FASTA1,841208,798
        10         20         30         40         50         60 
MASSSLPTLV PPGPHCLRPF TPESLAAIEQ RAMEEEARLQ RNKQMEIEEP ERKPRSDLEA 

        70         80         90        100        110        120 
GKNLPLIYGD PPPEVIGVPL EDLDPYYSDK KTFIVLNKGK AIFRFSATPA LYMLSPFSIV 

       130        140        150        160        170        180 
RRVAIKVLIH ALFSMFIMIT ILTNCVFMTM SNPPSWSKDV EYTFTGIYTF ESLIKMLARG 

       190        200        210        220        230        240 
FCIDDFTFLR DPWNWLDFSV ITMAYVTEFV DLGNISALRT FRVLRALKTI TVIPGLKTIV 

       250        260        270        280        290        300 
GALIQSVKKL SDVMILTVFC LSVFALVGLQ LFMGNLRQKC VRWPPPMNDT NTTWYGNDTW 

       310        320        330        340        350        360 
YGNDTWYGND TWYGNDTWNS QESWVSNSTF DWEAYINDEG NFYFLEGSND ALLCGNSSDA 

       370        380        390        400        410        420 
GHCPEGYECM KAGRNPNYGY TSYDTFSWAF LALFRLMTQD YWENLFQLTL RAAGKTYMIF 

       430        440        450        460        470        480 
FVVIIFLGSF YLINLILAVV AMAYAEQNEA TLAEDQEKEE EFQQMLEKFK KHQEELEKAK 

       490        500        510        520        530        540 
AAQALEGGEE ADGDPTHSKD CNGSLDTSGE KGPPRPSCSA ESAISDAMEE LEEAHQKCPP 

       550        560        570        580        590        600 
WWYKCAHKVL IWNCCAPWVK FKHIILLIVM DPFVDLGITI CIVLNTLFMA MEHYPMTEHF 

       610        620        630        640        650        660 
DNVLSVGNLV FTGIFTAEMV LKLIAMDPYE YFQQGWNIFD SFIVTLSLVE LGLANVQGLS 

       670        680        690        700        710        720 
VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS VGALGNLTLV LAIIVFIFAV VGMQLFGKSY 

       730        740        750        760        770        780 
KECVCKIASD CSLPRWHMHD FFHSFLIVFR ILCGEWIETM WDCMEVAGQA MCLTVFLMVM 

       790        800        810        820        830        840 
VIGNLVVLNL FLALLLSSFS ADSLAASDED GEMNNLQIAI GRIKWGIAFA KTFLLGLLHG 

       850        860        870        880        890        900 
KILSLKDIML SLGEPGGAGE NGESPPEDEK KEPPPEDGNK ELKDNHILNH VGLTDGPRSS 

       910        920        930        940        950        960 
IEMDHLNFIN NPYLTIHVPI ASEESDLEMP TEEETDTFSE PEDIKKPLQP LYDGNSSVCS 

       970        980        990       1000       1010       1020 
TADYKPPEED PEEQAEENPE GELPEECFTE ACVKRCPCLY VDISQGRGKM WWTLRRACFK 

      1030       1040       1050       1060       1070       1080 
IVEHNWFETF IVFMILLSSG ALAFEDIYIE QRRVIRTILE YADKVFTYIF ILEMLLKWVA 

      1090       1100       1110       1120       1130       1140 
YGFKVYFTNA WCWLDFLIVD VSIISLVANW LGYSELGPIK SLRTLRALRP LRALSRFEGM 

      1150       1160       1170       1180       1190       1200 
RVVVNALLGA IPSIMNVLLV CLIFWLIFSI MGVNLFAGKF YYCINTTTSE RFDISVVNNK 

      1210       1220       1230       1240       1250       1260 
SECESLMYTG QVRWMNVKVN YDNVGLGYLS LLQVATFKGW MDIMYAAVDS REKEEQPDYE 

      1270       1280       1290       1300       1310       1320 
VNLYMYLYFV IFIIFGSFFT LNLFIGVIID NFNQQKKKFG GKDIFMTEEQ KKYYNAMKKL 

      1330       1340       1350       1360       1370       1380 
GSKKPQKPIP RPQNKIQGMV YDFVTKQVFD ISIMILICLN MVTMMVETDD QSQLKVDILY 

      1390       1400       1410       1420       1430       1440 
NINMVFIIVF TGECVLKMFA LRHYYFTIGW NIFDFVVVIL SIVGLALSDL IQKYFVSPTL 

      1450       1460       1470       1480       1490       1500 
FRVIRLARIG RVLRLIRGAK GIRTLLFALM MSLPALFNIG LLLFLVMFIY SIFGMSNFAY 

      1510       1520       1530       1540       1550       1560 
VKKESGIDDM FNFETFGNSI ICLFEITTSA GWDGLLNPIL NSGPPDCDPT LENPGTNIKG 

      1570       1580       1590       1600       1610       1620 
DCGNPSIGIC FFCSYIIISF LIVVNMYIAI ILENFNVATE ESSEPLCEDD FEMFYETWEK 

      1630       1640       1650       1660       1670       1680 
FDPDATQFID YSRLSDFVDT LQEPLKIAKP NKIKLITLDL PMVPGDKIHC LDILFALTKE 

      1690       1700       1710       1720       1730       1740 
VLGDSGEMDA LKQTMEEKFM AANPSKVSYE PITTTLKRKQ EEVCAIKIQR AYRRHLLQRS 

      1750       1760       1770       1780       1790       1800 
VKQASYMYRH SQEGNGDGAP EKEGLLANTM NKMYGSEKED NGVQSQGEKE KDSTEDAGPT 

      1810       1820       1830       1840 
TEVTAPSSSD TALTPPPPSP PPPSSPPQGQ TVRPGVKESL V 

« Hide

References

« Hide 'large scale' references
[1]"Mouse heart Na+ channels: primary structure and function of two isoforms and alternatively spliced variants."
Zimmer T., Bollensdorff C., Haufe V., Birch-Hirschfeld E., Benndorf K.
Am. J. Physiol. 282:H1007-H1017(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Heart.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1841.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ278787 mRNA. Translation: CAC17146.1.
AL604045 Genomic DNA. Translation: CAM23795.1.
BC129805 mRNA. Translation: AAI29806.1.
CCDSCCDS48961.1.
RefSeqNP_573462.2. NM_133199.2.
UniGeneMm.432528.

3D structure databases

ProteinModelPortalQ9ER60.
SMRQ9ER60. Positions 131-272, 582-796, 1014-1290, 1349-1748.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000102431.

PTM databases

PhosphoSiteQ9ER60.

Proteomic databases

PaxDbQ9ER60.
PRIDEQ9ER60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID110880.
KEGGmmu:110880.

Organism-specific databases

CTD6329.
MGIMGI:98250. Scn4a.

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231755.
InParanoidB1ARK0.
KOK04837.
PhylomeDBQ9ER60.

Gene expression databases

GenevestigatorQ9ER60.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR028826. Na_channel_a4su.
IPR008052. Na_channel_a4su_mammal.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PANTHERPTHR10037:SF193. PTHR10037:SF193. 1 hit.
PfamPF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSPR00170. NACHANNEL.
PR01665. NACHANNEL4.
SMARTSM00015. IQ. 1 hit.
[Graphical view]
PROSITEPS50096. IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio364857.
PROQ9ER60.
SOURCESearch...

Entry information

Entry nameSCN4A_MOUSE
AccessionPrimary (citable) accession number: Q9ER60
Secondary accession number(s): A2VDE9, B1ARK0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 92 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

MGD cross-references

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