LipidDB ID

LipidDB-10116-00315

Entry Name

UniProt Accession

P04775;

Theoretical PI

5.58

Molecular Weight

227873.8

Genbank Protein ID

CAA27287.1;

Genbank Nucleotide ID

X03639;

Protein Name

Sodium channel protein type 2 subunit alpha

Protein Synonyms/Alias

Sodium channel protein brain II subunit alpha; Sodium channel protein type II subunit alpha; Voltage-gated sodium channel subunit alpha Nav1.2;

Gene Name

Scn2a

Gene Synonyms/Alias

Scn2a1;

Created Date

13-AUG-1987

Organism

Rattus norvegicus (Rat)

NCBI Taxa ID

10116

Reference

[1] Predicted from GPS-Lipid

Functional Description

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.

Sequence Annotation

Topological domain: 1 124 Cytoplasmic.
Transmembrane: 125 148 Helical; Name=S1 of repeat I.
Topological domain: 149 156 Extracellular.
Transmembrane: 157 176 Helical; Name=S2 of repeat I.
Topological domain: 177 189 Cytoplasmic.
Transmembrane: 190 208 Helical; Name=S3 of repeat I.
Topological domain: 209 214 Extracellular.
Transmembrane: 215 234 Helical; Voltage-sensor; Name=S4 ofrepeat I.
Topological domain: 235 250 Cytoplasmic.
Transmembrane: 251 274 Helical; Name=S5 of repeat I.
Topological domain: 275 401 Extracellular.
Transmembrane: 402 427 Helical; Name=S6 of repeat I.
Topological domain: 428 753 Cytoplasmic.
Transmembrane: 754 778 Helical; Name=S1 of repeat II.
Topological domain: 779 789 Extracellular.
Transmembrane: 790 813 Helical; Name=S2 of repeat II.
Topological domain: 814 821 Cytoplasmic.
Transmembrane: 822 841 Helical; Name=S3 of repeat II.
Topological domain: 842 847 Extracellular.
Transmembrane: 848 867 Helical; Voltage-sensor; Name=S4 ofrepeat II.
Topological domain: 868 883 Cytoplasmic.
Transmembrane: 884 904 Helical; Name=S5 of repeat II.
Topological domain: 905 957 Extracellular.
Transmembrane: 958 983 Helical; Name=S6 of repeat II.
Topological domain: 984 1203 Cytoplasmic.
Transmembrane: 1204 1227 Helical; Name=S1 of repeat III.
Topological domain: 1228 1240 Extracellular.
Transmembrane: 1241 1266 Helical; Name=S2 of repeat III.
Topological domain: 1267 1272 Cytoplasmic.
Transmembrane: 1273 1294 Helical; Name=S3 of repeat III.
Topological domain: 1295 1298 Extracellular.
Transmembrane: 1299 1320 Helical; Voltage-sensor; Name=S4 ofrepeat III.
Topological domain: 1321 1339 Cytoplasmic.
Transmembrane: 1340 1367 Helical; Name=S5 of repeat III.
Topological domain: 1368 1446 Extracellular.
Transmembrane: 1447 1473 Helical; Name=S6 of repeat III.
Topological domain: 1474 1526 Cytoplasmic.
Transmembrane: 1527 1550 Helical; Name=S1 of repeat IV.
Topological domain: 1551 1561 Extracellular.
Transmembrane: 1562 1585 Helical; Name=S2 of repeat IV.
Topological domain: 1586 1591 Cytoplasmic.
Transmembrane: 1592 1615 Helical; Name=S3 of repeat IV.
Topological domain: 1616 1625 Extracellular.
Transmembrane: 1626 1647 Helical; Voltage-sensor; Name=S4 ofrepeat IV.
Topological domain: 1648 1662 Cytoplasmic.
Transmembrane: 1663 1685 Helical; Name=S5 of repeat IV.
Topological domain: 1686 1751 Extracellular.
Transmembrane: 1752 1776 Helical; Name=S6 of repeat IV.
Topological domain: 1777 2005 Cytoplasmic.
Domain: 1905 1934 IQ.
Functional site: 1489 1489 Important for channel closure.
Modified residue: 4 4 Phosphoserine.
Modified residue: 468 468 Phosphoserine.
Modified residue: 471 471 Phosphoserine.
Modified residue: 484 484 Phosphoserine.
Modified residue: 528 528 Phosphoserine.
Modified residue: 554 554 Phosphoserine.
Modified residue: 554 554 Phosphoserine; by PKC; in vitro.
Modified residue: 573 573 Phosphoserine; by PKC; in vitro.
Modified residue: 576 576 Phosphoserine; by PKC; in vitro.
Modified residue: 610 610 Phosphoserine.
Modified residue: 623 623 Phosphoserine.
Modified residue: 687 687 Phosphoserine.
Modified residue: 688 688 Phosphoserine.
Modified residue: 721 721 Phosphoserine.
Modified residue: 1506 1506 Phosphoserine; by PKC.
Modified residue: 1930 1930 Phosphoserine.
Modified residue: 1963 1963 Phosphothreonine.
Modified residue: 1966 1966 Phosphothreonine.
Modified residue: 1971 1971 Phosphoserine.

Protein Length

2005 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0043194; C:axon initial segment; IDA:RGD
GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB
GO:0043005; C:neuron projection; IDA:RGD
GO:0033268; C:node of Ranvier; IDA:BHF-UCL
GO:0034706; C:sodium channel complex; IDA:UniProtKB
GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD
GO:0043522; F:leucine zipper domain binding; IPI:RGD
GO:0031402; F:sodium ion binding; IDA:RGD
GO:0005248; F:voltage-gated sodium channel activity; IDA:UniProtKB
GO:0086010; P:membrane depolarization during action potential; IBA:RefGenome
GO:0042552; P:myelination; IEP:BHF-UCL
GO:0019228; P:neuronal action potential; IDA:RGD
GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB
GO:0006814; P:sodium ion transport; IDA:RGD

Interpro

InterPro; IPR027359; Channel_four-helix_dom
InterPro; IPR024583; DUF3451
InterPro; IPR005821; Ion_trans_dom
InterPro; IPR000048; IQ_motif_EF-hand-BS
InterPro; IPR001696; Na_channel_asu
InterPro; IPR010526; Na_trans_assoc

Pfam

Pfam; PF11933; DUF3451;
Pfam; PF00520; Ion_trans;
Pfam; PF06512; Na_trans_assoc;

SMART

SMART; SM00015; IQ;

PROSITE

PROSITE; PS50096; IQ;

PRINTS

PRINTS; PR00170; NACHANNEL;