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Protein

Sodium channel protein type 3 subunit alpha

Gene

Scn3a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • calmodulin binding Source: RGD
  • sodium ion binding Source: RGD
  • voltage-gated sodium channel activity Source: RGD

GO - Biological processi

  • cellular response to antibiotic Source: RGD
  • membrane depolarization during action potential Source: GO_Central
  • nervous system development Source: RGD
  • neuronal action potential Source: RGD
  • response to pyrethroid Source: RGD
  • response to wounding Source: RGD
  • sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Sodium transport, Transport

Keywords - Ligandi

Sodium

Protein family/group databases

TCDBi1.A.1.10.1. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium channel protein type 3 subunit alpha
Alternative name(s):
Sodium channel protein brain III subunit alpha
Sodium channel protein type III subunit alpha
Voltage-gated sodium channel subtype III
Voltage-gated sodium channel subunit alpha Nav1.3
Gene namesi
Name:Scn3a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3635. Scn3a.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 123CytoplasmicSequence analysisAdd BLAST123
Transmembranei124 – 147Helical; Name=S1 of repeat ISequence analysisAdd BLAST24
Topological domaini148 – 155ExtracellularSequence analysis8
Transmembranei156 – 175Helical; Name=S2 of repeat ISequence analysisAdd BLAST20
Topological domaini176 – 188CytoplasmicSequence analysisAdd BLAST13
Transmembranei189 – 207Helical; Name=S3 of repeat ISequence analysisAdd BLAST19
Topological domaini208 – 213ExtracellularSequence analysis6
Transmembranei214 – 233Helical; Voltage-sensor; Name=S4 of repeat ISequence analysisAdd BLAST20
Topological domaini234 – 248CytoplasmicSequence analysisAdd BLAST15
Transmembranei249 – 273Helical; Name=S5 of repeat ISequence analysisAdd BLAST25
Topological domaini274 – 400ExtracellularSequence analysisAdd BLAST127
Transmembranei401 – 426Helical; Name=S6 of repeat ISequence analysisAdd BLAST26
Topological domaini427 – 705CytoplasmicSequence analysisAdd BLAST279
Transmembranei706 – 730Helical; Name=S1 of repeat IISequence analysisAdd BLAST25
Topological domaini731 – 741ExtracellularSequence analysisAdd BLAST11
Transmembranei742 – 765Helical; Name=S2 of repeat IISequence analysisAdd BLAST24
Topological domaini766 – 773CytoplasmicSequence analysis8
Transmembranei774 – 793Helical; Name=S3 of repeat IISequence analysisAdd BLAST20
Topological domaini794 – 799ExtracellularSequence analysis6
Transmembranei800 – 820Helical; Voltage-sensor; Name=S4 of repeat IISequence analysisAdd BLAST21
Topological domaini821 – 835CytoplasmicSequence analysisAdd BLAST15
Transmembranei836 – 856Helical; Name=S5 of repeat IISequence analysisAdd BLAST21
Topological domaini857 – 909ExtracellularSequence analysisAdd BLAST53
Transmembranei910 – 935Helical; Name=S6 of repeat IISequence analysisAdd BLAST26
Topological domaini936 – 1152CytoplasmicSequence analysisAdd BLAST217
Transmembranei1153 – 1176Helical; Name=S1 of repeat IIISequence analysisAdd BLAST24
Topological domaini1177 – 1189ExtracellularSequence analysisAdd BLAST13
Transmembranei1190 – 1215Helical; Name=S2 of repeat IIISequence analysisAdd BLAST26
Topological domaini1216 – 1221CytoplasmicSequence analysis6
Transmembranei1222 – 1243Helical; Name=S3 of repeat IIISequence analysisAdd BLAST22
Topological domaini1244 – 1247ExtracellularSequence analysis4
Transmembranei1248 – 1269Helical; Voltage-sensor; Name=S4 of repeat IIISequence analysisAdd BLAST22
Topological domaini1270 – 1288CytoplasmicSequence analysisAdd BLAST19
Transmembranei1289 – 1310Helical; Name=S5 of repeat IIISequence analysisAdd BLAST22
Topological domaini1311 – 1392ExtracellularSequence analysisAdd BLAST82
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 – 1571ExtracellularSequence analysis10
Transmembranei1572 – 1593Helical; Voltage-sensor; Name=S4 of repeat IVSequence analysisAdd BLAST22
Topological domaini1594 – 1608CytoplasmicSequence analysisAdd BLAST15
Transmembranei1609 – 1631Helical; Name=S5 of repeat IVSequence analysisAdd BLAST23
Topological domaini1632 – 1697ExtracellularSequence analysisAdd BLAST66
Transmembranei1698 – 1722Helical; Name=S6 of repeat IVSequence analysisAdd BLAST25
Topological domaini1723 – 1951CytoplasmicSequence analysisAdd BLAST229

GO - Cellular componenti

  • axon Source: RGD
  • neuronal cell body Source: RGD
  • voltage-gated sodium channel complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4966.
GuidetoPHARMACOLOGYi580.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000484941 – 1951Sodium channel protein type 3 subunit alphaAdd BLAST1951

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi211N-linked (GlcNAc...)Sequence analysis1
Glycosylationi290N-linked (GlcNAc...)Sequence analysis1
Glycosylationi296N-linked (GlcNAc...)Sequence analysis1
Glycosylationi302N-linked (GlcNAc...)Sequence analysis1
Glycosylationi307N-linked (GlcNAc...)Sequence analysis1
Glycosylationi339N-linked (GlcNAc...)Sequence analysis1
Modified residuei484PhosphoserineCombined sources1
Modified residuei485PhosphoserineCombined sources1
Modified residuei486PhosphoserineCombined sources1
Glycosylationi1317N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1331N-linked (GlcNAc...)Sequence analysis1
Modified residuei1452Phosphoserine; by PKCBy similarity1

Post-translational modificationi

May be ubiquitinated by NEDD4L; which would promote 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

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP08104.
PRIDEiP08104.

PTM databases

iPTMnetiP08104.
PhosphoSitePlusiP08104.
SwissPalmiP08104.

Interactioni

Subunit structurei

The sodium channel consists of a large polypeptide and 2-3 smaller ones. This sequence represents a large polypeptide. Interacts with NEDD4L (By similarity).By similarity

GO - Molecular functioni

  • calmodulin binding Source: RGD

Protein-protein interaction databases

BioGridi269080. 2 interactors.
STRINGi10116.ENSRNOP00000006646.

Chemistry databases

BindingDBiP08104.

Structurei

Secondary structure

11951
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi161 – 174Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QG9NMR-A156-176[»]
ProteinModelPortaliP08104.
SMRiP08104.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08104.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati110 – 455ICuratedAdd BLAST346
Repeati693 – 965IICuratedAdd BLAST273
Repeati1139 – 1450IIICuratedAdd BLAST312
Repeati1459 – 1757IVCuratedAdd BLAST299
Domaini1851 – 1880IQAdd 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.
HOVERGENiHBG053100.
InParanoidiP08104.
KOiK04836.
PhylomeDBiP08104.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
IPR024583. Na_trans_cytopl.
[Graphical view]
PfamiPF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
PF11933. Na_trans_cytopl. 1 hit.
[Graphical view]
PRINTSiPR00170. NACHANNEL.

Sequencei

Sequence statusi: Complete.

P08104-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQALLVPPG PESFRLFTRE SLAAIEKRAA EEKAKKPKKE QDIDDENKPK
60 70 80 90 100
PNSDLEAGKN LPFIYGDIPP EMVSEPLEDL DPYYVSKKTF VVLNKGKAIF
110 120 130 140 150
RFSATSALYI LTPLNPVRKI AIKILVHSLF SMLIMCTILT NCVFMTLSNP
160 170 180 190 200
PDWTKNVEYT FTGIYTFESL IKILARGFCL EDFTFLRDPW NWLDFSVIVM
210 220 230 240 250
AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL IQSVKKLSDV
260 270 280 290 300
MILTVFCLSV FALIGLQLFM GNLRNKCSQW PPSDSAFETN TTSYFNGTMD
310 320 330 340 350
SNGTFVNVTM STFNWKDYIA DDSHFYVLDG QKDPLLCGNG SDAGQCPEGY
360 370 380 390 400
ICVKAGRNPN YGYTSFDTFS WAFLSLFRLM TQDYWENLYQ LTLRAAGKTY
410 420 430 440 450
MIFFVLVIFL GSFYLVNLIL AVVAMAYEEQ NQATLEEAEQ KEAEFQQMLE
460 470 480 490 500
QLKKQQEEAQ AVAAASAASR DFSGIGGLGE LLESSSEASK LSSKSAKEWR
510 520 530 540 550
NRRKKRRQRE HLEGNHRADG DRFPKSESED SVKRRSFLLS LDGNPLTGDK
560 570 580 590 600
KLCSPHQSLL SIRGSLFSPR RNSKTSIFSF RGRAKDVGSE NDFADDEHST
610 620 630 640 650
FEDSESRRDS LFVPHRPGER RNSNGTTTET EVRKRRLSSY QISMEMLEDS
660 670 680 690 700
SGRQRSMSIA SILTNTMEEL EESRQKCPPC WYRFANVFLI WDCCDAWLKV
710 720 730 740 750
KHLVNLIVMD PFVDLAITIC IVLNTLFMAM EHYPMTQQFS SVLTVGNLVF
760 770 780 790 800
TGIFTAEMVL KIIAMDPYYY FQEGWNIFDG IIVSLSLMEL GLANVEGLSV
810 820 830 840 850
LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL AIIVFIFAVV
860 870 880 890 900
GMQLFGKSYK ECVCKINVDC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW
910 920 930 940 950
DCMEVAGQTM CLIVFMLVMV IGNLVVLNLF LALLLSSFSS DNLAATDDDN
960 970 980 990 1000
EMNNLQIAVG RMQKGIDFVK NKIRECFRKA FFRKPKVIEI QEGNKIDSCM
1010 1020 1030 1040 1050
SNNTGIEISK ELNYLKDGNG TTSGVGTGSS VEKYVIDEND YMSFINNPSL
1060 1070 1080 1090 1100
TVTVPIAVGE SDFENLNTEE FSSESELEES KEKLNATSSS EGSTVDVAPP
1110 1120 1130 1140 1150
REGEQAEIEP EEDLKPEACF TEGCIKKFPF CQVSTEEGKG KIWWNLRKTC
1160 1170 1180 1190 1200
YSIVEHNWFE TFIVFMILLS SGALAFEDIY IEQRKTIKTM LEYADKVFTY
1210 1220 1230 1240 1250
IFILEMLLKW VAYGFQTYFT NAWCWLDFLI VDVSLVSLVA NALGYSELGA
1260 1270 1280 1290 1300
IKSLRTLRAL RPLRALSRFE GMRVVVNALV GAIPSIMNVL LVCLIFWLIF
1310 1320 1330 1340 1350
SIMGVNLFAG KFYHCVNTTT GNMFEIKEVN NFSDCQALGK QARWKNVKVN
1360 1370 1380 1390 1400
FDNVGAGYLA LLQVATFKGW MDIMYAAVDS RDVKLQPIYE ENLYMYLYFV
1410 1420 1430 1440 1450
IFIIFGSFFT LNLFIGVIID NFNQQKKKFG GQDIFMTEEQ KKYYNAMKKL
1460 1470 1480 1490 1500
GSKKPQKPIP RPANKFQGMV FDFVTRQVFD ISIMILICLN MVTMMVETDD
1510 1520 1530 1540 1550
QSKYMTLVLS RINLVFIVLF TGEFLLKLIS LRYYYFTIGW NIFDFVVVIL
1560 1570 1580 1590 1600
SIVGMFLAEL IEKYFVSPTL FRVIRLARIG RILRLIKGAK GIRTLLFALM
1610 1620 1630 1640 1650
MSLPALFNIG LLLFLVMFIY AIFGMSNFAY VKKEAGIDDM FNFETFGNSM
1660 1670 1680 1690 1700
ICLFQITTSA GWDGLLAPIL NSAPPDCDPD AIHPGSSVKG DCGNPSVGIF
1710 1720 1730 1740 1750
FFVSYIIISF LVVVNMYIAV ILENFSVATE ESAEPLSEDD FEMFYEVWEK
1760 1770 1780 1790 1800
FDPDATQFIE FCKLSDFAAA LDPPLLIAKP NKVQLIAMDL PMVSGDRIHC
1810 1820 1830 1840 1850
LDILFAFTKR VLGESGEMDA LRIQMEDRFM ASNPSKVSYE PITTTLKRKQ
1860 1870 1880 1890 1900
EEVSAAIIQR NYRCYLLKQR LKNISSKYDK ETIKGRIDLP IKGDMVIDKL
1910 1920 1930 1940 1950
NGNSTPEKTD GSSSTTSPPS YDSVTKPDKE KFEKDKPEKE IKGKEVRENQ

K
Length:1,951
Mass (Da):221,387
Last modified:August 1, 1988 - v1
Checksum:i74E5E851524BD10E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00766 mRNA. Translation: CAA68735.1.
PIRiS00320.
RefSeqiNP_037251.1. NM_013119.1.
UniGeneiRn.87394.

Genome annotation databases

GeneIDi497770.
KEGGirno:497770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00766 mRNA. Translation: CAA68735.1.
PIRiS00320.
RefSeqiNP_037251.1. NM_013119.1.
UniGeneiRn.87394.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QG9NMR-A156-176[»]
ProteinModelPortaliP08104.
SMRiP08104.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi269080. 2 interactors.
STRINGi10116.ENSRNOP00000006646.

Chemistry databases

BindingDBiP08104.
ChEMBLiCHEMBL4966.
GuidetoPHARMACOLOGYi580.

Protein family/group databases

TCDBi1.A.1.10.1. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiP08104.
PhosphoSitePlusiP08104.
SwissPalmiP08104.

Proteomic databases

PaxDbiP08104.
PRIDEiP08104.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi497770.
KEGGirno:497770.

Organism-specific databases

CTDi6328.
RGDi3635. Scn3a.

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOVERGENiHBG053100.
InParanoidiP08104.
KOiK04836.
PhylomeDBiP08104.

Miscellaneous databases

EvolutionaryTraceiP08104.
PROiP08104.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
IPR024583. Na_trans_cytopl.
[Graphical view]
PfamiPF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
PF11933. Na_trans_cytopl. 1 hit.
[Graphical view]
PRINTSiPR00170. NACHANNEL.
ProtoNetiSearch...

Entry informationi

Entry nameiSCN3A_RAT
AccessioniPrimary (citable) accession number: P08104
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 2, 2016
This is version 149 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.