UniProtKB - P04775 (SCN2A_RAT)
Protein
Sodium channel protein type 2 subunit alpha
Gene
Scn2a
Organism
Rattus norvegicus (Rat)
Status
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. Implicated in the regulation of hippocampal replay occurring within sharp wave ripples (SPW-R) important for memory (By similarity).By similarity3 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 330 | Binds Mu-conotoxin KIIIABy similarity | 1 | |
Sitei | 362 | Binds Mu-conotoxin KIIIABy similarity | 1 | |
Sitei | 909 | Binds SCN2B; via carbonyl oxygenBy similarity | 1 | |
Sitei | 916 | Binds Mu-conotoxin KIIIA; via amide nitrogenBy similarity | 1 | |
Sitei | 920 | Binds Mu-conotoxin KIIIA; via carbonyl oxygenBy similarity | 1 | |
Sitei | 945 | Binds Mu-conotoxin KIIIABy similarity | 1 | |
Sitei | 949 | Binds Mu-conotoxin KIIIABy similarity | 1 | |
Sitei | 1374 | Binds Mu-conotoxin KIIIA; via amide nitrogenBy similarity | 1 | |
Sitei | 1429 | Binds Mu-conotoxin KIIIABy similarity | 1 | |
Sitei | 1443 | Binds Mu-conotoxin KIIIABy similarity | 1 | |
Sitei | 1489 | Important for channel closure | 1 |
GO - Molecular functioni
- cation channel activity Source: GO_Central
- leucine zipper domain binding Source: RGD
- sodium ion binding Source: RGD
- voltage-gated ion channel activity involved in regulation of presynaptic membrane potential Source: SynGO
- voltage-gated sodium channel activity Source: UniProtKB
GO - Biological processi
- cellular response to hypoxia Source: UniProtKB
- intrinsic apoptotic signaling pathway in response to osmotic stress Source: UniProtKB
- membrane depolarization during action potential Source: GO_Central
- memory Source: UniProtKB
- myelination Source: BHF-UCL
- nervous system development Source: UniProtKB
- neuronal action potential Source: RGD
- neuron apoptotic process Source: UniProtKB
- regulation of ion transmembrane transport Source: UniProtKB-KW
- sodium ion transmembrane transport Source: UniProtKB
- sodium ion transport Source: RGD
Keywordsi
Molecular function | Ion channel, Sodium channel, Voltage-gated channel |
Biological process | Ion transport, Sodium transport, Transport |
Ligand | Sodium |
Enzyme and pathway databases
Reactomei | R-RNO-5576892, Phase 0 - rapid depolarisation |
Names & Taxonomyi
Protein namesi | Recommended name: Sodium channel protein type 2 subunit alphaAlternative name(s): Sodium channel protein brain II subunit alpha Sodium channel protein type II subunit alpha Voltage-gated sodium channel subunit alpha Nav1.2 |
Gene namesi | Name:Scn2a Synonyms:Scn2a1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3632, Scn2a |
Subcellular locationi
Plasma membrane
- Cell membrane 4 Publications; Multi-pass membrane protein 2 Publications
Plasma Membrane
- integral component of presynaptic membrane Source: RGD
- intrinsic component of plasma membrane Source: UniProtKB
- plasma membrane Source: UniProtKB
- T-tubule Source: RGD
- voltage-gated sodium channel complex Source: RGD
Other locations
- axon Source: RGD
- axon initial segment Source: RGD
- glutamatergic synapse Source: RGD
- intercalated disc Source: RGD
- membrane Source: RGD
- neuron projection Source: RGD
- node of Ranvier Source: BHF-UCL
- paranode region of axon Source: RGD
- sodium channel complex Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 129 | CytoplasmicCuratedAdd BLAST | 129 | |
Transmembranei | 130 – 148 | Helical; Name=S1 of repeat IBy similarityAdd BLAST | 19 | |
Topological domaini | 149 – 155 | ExtracellularCurated | 7 | |
Transmembranei | 156 – 176 | Helical; Name=S2 of repeat IBy similarityAdd BLAST | 21 | |
Topological domaini | 177 – 190 | CytoplasmicCuratedAdd BLAST | 14 | |
Transmembranei | 191 – 208 | Helical; Name=S3 of repeat IBy similarityAdd BLAST | 18 | |
Topological domaini | 209 – 214 | ExtracellularCurated | 6 | |
Transmembranei | 215 – 231 | Helical; Name=S4 of repeat IBy similarityAdd BLAST | 17 | |
Topological domaini | 232 – 250 | CytoplasmicCuratedAdd BLAST | 19 | |
Transmembranei | 251 – 270 | Helical; Name=S5 of repeat IBy similarityAdd BLAST | 20 | |
Topological domaini | 271 – 369 | ExtracellularCuratedAdd BLAST | 99 | |
Intramembranei | 370 – 394 | Pore-formingBy similarityAdd BLAST | 25 | |
Topological domaini | 395 – 401 | ExtracellularCurated | 7 | |
Transmembranei | 402 – 422 | Helical; Name=S6 of repeat IBy similarityAdd BLAST | 21 | |
Topological domaini | 423 – 759 | CytoplasmicCuratedAdd BLAST | 337 | |
Transmembranei | 760 – 778 | Helical; Name=S1 of repeat IIBy similarityAdd BLAST | 19 | |
Topological domaini | 779 – 789 | ExtracellularCuratedAdd BLAST | 11 | |
Transmembranei | 790 – 809 | Helical; Name=S2 of repeat IIBy similarityAdd BLAST | 20 | |
Topological domaini | 810 – 823 | CytoplasmicCuratedAdd BLAST | 14 | |
Transmembranei | 824 – 843 | Helical; Name=S3 of repeat IIBy similarityAdd BLAST | 20 | |
Topological domaini | 844 – 845 | ExtracellularCurated | 2 | |
Transmembranei | 846 – 863 | Helical; Name=S4 of repeat IIBy similarityAdd BLAST | 18 | |
Topological domaini | 864 – 879 | CytoplasmicCuratedAdd BLAST | 16 | |
Transmembranei | 880 – 898 | Helical; Name=S5 of repeat IIBy similarityAdd BLAST | 19 | |
Topological domaini | 899 – 927 | ExtracellularCuratedAdd BLAST | 29 | |
Intramembranei | 928 – 948 | Pore-formingBy similarityAdd BLAST | 21 | |
Topological domaini | 949 – 961 | ExtracellularCuratedAdd BLAST | 13 | |
Transmembranei | 962 – 982 | Helical; Name=S6 of repeat IIBy similarityAdd BLAST | 21 | |
Topological domaini | 983 – 1209 | CytoplasmicCuratedAdd BLAST | 227 | |
Transmembranei | 1210 – 1227 | Helical; Name=S1 of repeat IIIBy similarityAdd BLAST | 18 | |
Topological domaini | 1228 – 1240 | ExtracellularCuratedAdd BLAST | 13 | |
Transmembranei | 1241 – 1259 | Helical; Name=S2 of repeat IIIBy similarityAdd BLAST | 19 | |
Topological domaini | 1260 – 1273 | CytoplasmicCuratedAdd BLAST | 14 | |
Transmembranei | 1274 – 1292 | Helical; Name=S3 of repeat IIIBy similarityAdd BLAST | 19 | |
Topological domaini | 1293 – 1300 | ExtracellularCurated | 8 | |
Transmembranei | 1301 – 1319 | Helical; Name=S4 of repeat IIIBy similarityAdd BLAST | 19 | |
Topological domaini | 1320 – 1336 | CytoplasmicCuratedAdd BLAST | 17 | |
Transmembranei | 1337 – 1356 | Helical; Name=S5 of repeat IIIBy similarityAdd BLAST | 20 | |
Topological domaini | 1357 – 1408 | ExtracellularCuratedAdd BLAST | 52 | |
Intramembranei | 1409 – 1430 | Pore-formingBy similarityAdd BLAST | 22 | |
Topological domaini | 1431 – 1447 | ExtracellularCuratedAdd BLAST | 17 | |
Transmembranei | 1448 – 1469 | Helical; Name=S6 of repeat IIIBy similarityAdd BLAST | 22 | |
Topological domaini | 1470 – 1532 | CytoplasmicCuratedAdd BLAST | 63 | |
Transmembranei | 1533 – 1550 | Helical; Name=S1 of repeat IVBy similarityAdd BLAST | 18 | |
Topological domaini | 1551 – 1561 | ExtracellularCuratedAdd BLAST | 11 | |
Transmembranei | 1562 – 1580 | Helical; Name=S2 of repeat IVBy similarityAdd BLAST | 19 | |
Topological domaini | 1581 – 1592 | CytoplasmicCuratedAdd BLAST | 12 | |
Transmembranei | 1593 – 1610 | Helical; Name=S3 of repeat IVBy similarityAdd BLAST | 18 | |
Topological domaini | 1611 – 1623 | ExtracellularCuratedAdd BLAST | 13 | |
Transmembranei | 1624 – 1640 | Helical; Name=S4 of repeat IVBy similarityAdd BLAST | 17 | |
Topological domaini | 1641 – 1659 | CytoplasmicCuratedAdd BLAST | 19 | |
Transmembranei | 1660 – 1677 | Helical; Name=S5 of repeat IVBy similarityAdd BLAST | 18 | |
Topological domaini | 1678 – 1699 | ExtracellularCuratedAdd BLAST | 22 | |
Intramembranei | 1700 – 1722 | Pore-formingBy similarityAdd BLAST | 23 | |
Topological domaini | 1723 – 1752 | ExtracellularCuratedAdd BLAST | 30 | |
Transmembranei | 1753 – 1775 | Helical; Name=S6 of repeat IVBy similarityAdd BLAST | 23 | |
Topological domaini | 1776 – 2005 | CytoplasmicCuratedAdd BLAST | 230 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 38 | K → Q: Abolishes SUMOylation. No increase of voltage-gated sodium current upon hypoxia. 1 Publication | 1 | |
Mutagenesisi | 385 | F → C: Sodium current is irreversibly blocked by methanethiosulfonate (MTSET); the mutated Cys residue has a free thiol susceptible to reaction with MTSET, and inhibition of current is due to the fact that the residue is close to the selectivity filter. By similarity1 Publication | 1 | |
Mutagenesisi | 879 – 881 | GAL → QQQ: Slowed inactivation and increased persistent current. Gain of function mutation. 1 Publication | 3 | |
Mutagenesisi | 910 | C → L: >1000-fold reduction of sensitivity to the conotoxin GVIIJ(SSG). 1 Publication | 1 | |
Mutagenesisi | 1489 | F → Q: Strongly impairs channel inactivation. 1 Publication | 1 | |
Mutagenesisi | 1506 | S → A: Blocks the reduction of Na+ current and the slowing of inactivation caused by PKC. 1 Publication | 1 | |
Mutagenesisi | 1613 | E → D: Increase in sensitivity to the scorpion toxin BMK M1. 1 Publication | 1 | |
Mutagenesisi | 1975 | Y → A: Abolishes interaction with NEDD4L. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3399 |
DrugCentrali | P04775 |
GuidetoPHARMACOLOGYi | 579 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000048492 | 1 – 2005 | Sodium channel protein type 2 subunit alphaAdd BLAST | 2005 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 4 | Phosphoserine1 Publication | 1 | |
Cross-linki | 38 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication | ||
Glycosylationi | 212 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 278 ↔ 338 | By similarity | ||
Glycosylationi | 285 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 291 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 297 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 303 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 308 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 340 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 468 | Phosphoserine1 Publication | 1 | |
Modified residuei | 471 | Phosphoserine1 Publication | 1 | |
Modified residuei | 484 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 526 | PhosphoserineCombined sources | 1 | |
Modified residuei | 528 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 531 | PhosphoserineCombined sources | 1 | |
Modified residuei | 553 | PhosphoserineCombined sources | 1 | |
Modified residuei | 554 | PhosphoserineCombined sources2 Publications | 1 | |
Modified residuei | 554 | Phosphoserine; by PKC; in vitroCombined sources2 Publications | 1 | |
Modified residuei | 558 | PhosphoserineCombined sources | 1 | |
Modified residuei | 573 | Phosphoserine; by PKC; in vitro1 Publication | 1 | |
Modified residuei | 576 | Phosphoserine; by PKC; in vitro1 Publication | 1 | |
Modified residuei | 589 | PhosphoserineCombined sources | 1 | |
Modified residuei | 610 | Phosphoserine1 Publication | 1 | |
Modified residuei | 623 | Phosphoserine1 Publication | 1 | |
Modified residuei | 687 | Phosphoserine1 Publication | 1 | |
Modified residuei | 688 | Phosphoserine1 Publication | 1 | |
Modified residuei | 721 | PhosphoserineCombined sources1 Publication | 1 | |
Disulfide bondi | 910 | Interchain; with SCN2B or SCN4B1 Publication1 Publication | ||
Disulfide bondi | 910 | Interchain; with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B; the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin)1 Publication | ||
Disulfide bondi | 912 ↔ 918 | By similarity | ||
Disulfide bondi | 950 ↔ 959 | By similarity | ||
Disulfide bondi | 1366 ↔ 1386 | By similarity | ||
Glycosylationi | 1368 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1382 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1393 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 1506 | Phosphoserine; by PKC2 Publications | 1 | |
Disulfide bondi | 1731 ↔ 1746 | By similarity | ||
Modified residuei | 1930 | Phosphoserine1 Publication | 1 | |
Modified residuei | 1943 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1963 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1966 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 1971 | Phosphoserine1 Publication | 1 |
Post-translational modificationi
May be ubiquitinated by NEDD4L; which would promote its endocytosis.
Phosphorylation at Ser-1506 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.3 Publications
Sumoylated at Lys-38. Sumoylation is induced by hypoxia, increases voltage-gated sodium current and mediates the early response to acute hypoxia in neurons (PubMed:28029095). Sumoylated SCN2A is located at the cell membrane (PubMed:28029095).1 Publication
Keywords - PTMi
Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P04775 |
PRIDEi | P04775 |
PTM databases
GlyGeni | P04775, 10 sites |
iPTMneti | P04775 |
PhosphoSitePlusi | P04775 |
SwissPalmi | P04775 |
Expressioni
Tissue specificityi
Interactioni
Subunit structurei
Heterooligomer of a large alpha subunit and a smaller beta subunit. Heterooligomer with SCN2B or SCN4B; disulfide-linked (PubMed:26894959). Heterooligomer with SCN1B or SCN3B; non-covalently linked.
Interacts with NEDD4L.
Interacts with CALM.
Interacts with the conotoxin GVIIJ (PubMed:24497506).
Interacts with the scorpion toxin BMK M1 (PubMed:20678086).
5 PublicationsBinary interactionsi
Hide detailsP04775
With | #Exp. | IntAct |
---|---|---|
Syt1 [P21707] | 2 | EBI-2619448,EBI-458098 |
CAM [P07463] from Paramecium tetraurelia. | 2 | EBI-2619448,EBI-15916571 |
GO - Molecular functioni
- leucine zipper domain binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 246890, 4 interactors |
CORUMi | P04775 |
DIPi | DIP-57088N |
IntActi | P04775, 2 interactors |
STRINGi | 10116.ENSRNOP00000007069 |
Chemistry databases
BindingDBi | P04775 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | P04775 |
SMRi | P04775 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P04775 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 111 – 456 | ICuratedAdd BLAST | 346 | |
Repeati | 741 – 1013 | IICuratedAdd BLAST | 273 | |
Repeati | 1190 – 1504 | IIICuratedAdd BLAST | 315 | |
Repeati | 1513 – 1811 | IVCuratedAdd BLAST | 299 | |
Domaini | 1905 – 1934 | IQPROSITE-ProRule annotationAdd BLAST | 30 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 917 – 918 | Binds SCN2BBy similarity | 2 |
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.Curated
Sequence similaritiesi
Belongs to the sodium channel (TC 1.A.1.10) family. Nav1.2/SCN2A subfamily. [View classification]Curated
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG2301, Eukaryota |
InParanoidi | P04775 |
OrthoDBi | 56920at2759 |
PhylomeDBi | P04775 |
Family and domain databases
Gene3Di | 1.20.120.350, 4 hits |
InterProi | View protein in InterPro IPR005821, Ion_trans_dom IPR000048, IQ_motif_EF-hand-BS IPR001696, Na_channel_asu IPR010526, Na_trans_assoc IPR024583, Na_trans_cytopl IPR043203, VGCC_Ca_Na IPR027359, Volt_channel_dom_sf |
PANTHERi | PTHR10037, PTHR10037, 1 hit |
Pfami | View protein in Pfam PF00520, Ion_trans, 4 hits PF06512, Na_trans_assoc, 1 hit PF11933, Na_trans_cytopl, 1 hit |
PRINTSi | PR00170, NACHANNEL |
SMARTi | View protein in SMART SM00015, IQ, 1 hit |
PROSITEi | View protein in PROSITE PS50096, IQ, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
P04775-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MARSVLVPPG PDSFRFFTRE SLAAIEQRIA EEKAKRPKQE RKDEDDENGP
60 70 80 90 100
KPNSDLEAGK SLPFIYGDIP PEMVSEPLED LDPYYINKKT FIVLNKGKAI
110 120 130 140 150
SRFSATSALY ILTPFNPIRK LAIKILVHSL FNVLIMCTIL TNCVFMTMSN
160 170 180 190 200
PPDWTKNVEY TFTGIYTFES LIKILARGFC LEDFTFLRNP WNWLDFTVIT
210 220 230 240 250
FAYVTEFVNL GNVSALRTFR VLRALKTISV IPGLKTIVGA LIQSVKKLSD
260 270 280 290 300
VMILTVFCLS VFALIGLQLF MGNLRNKCLQ WPPDNSTFEI NITSFFNNSL
310 320 330 340 350
DWNGTAFNRT VNMFNWDEYI EDKSHFYFLE GQNDALLCGN SSDAGQCPEG
360 370 380 390 400
YICVKAGRNP NYGYTSFDTF SWAFLSLFRL MTQDFWENLY QLTLRAAGKT
410 420 430 440 450
YMIFFVLVIF LGSFYLINLI LAVVAMAYEE QNQATLEEAE QKEAEFQQML
460 470 480 490 500
EQLKKQQEEA QAAAAAASAE SRDFSGAGGI GVFSESSSVA SKLSSKSEKE
510 520 530 540 550
LKNRRKKKKQ KEQAGEEEKE DAVRKSASED SIRKKGFQFS LEGSRLTYEK
560 570 580 590 600
RFSSPHQSLL SIRGSLFSPR RNSRASLFNF KGRVKDIGSE NDFADDEHST
610 620 630 640 650
FEDNDSRRDS LFVPHRHGER RPSNVSQASR ASRGIPTLPM NGKMHSAVDC
660 670 680 690 700
NGVVSLVGGP SALTSPVGQL LPEGTTTETE IRKRRSSSYH VSMDLLEDPS
710 720 730 740 750
RQRAMSMASI LTNTMEELEE SRQKCPPCWY KFANMCLIWD CCKPWLKVKH
760 770 780 790 800
VVNLVVMDPF VDLAITICIV LNTLFMAMEH YPMTEQFSSV LSVGNLVFTG
810 820 830 840 850
IFTAEMFLKI IAMDPYYYFQ EGWNIFDGFI VSLSLMELGL ANVEGLSVLR
860 870 880 890 900
SFRLLRVFKL AKSWPTLNML IKIIGNSVGA LGNLTLVLAI IVFIFAVVGM
910 920 930 940 950
QLFGKSYKEC VCKISNDCEL PRWHMHHFFH SFLIVFRVLC GEWIETMWDC
960 970 980 990 1000
MEVAGQTMCL TVFMMVMVIG NLVVLNLFLA LLLSSFSSDN LAATDDDNEM
1010 1020 1030 1040 1050
NNLQIAVGRM QKGIDFVKRK IREFIQKAFV RKQKALDEIK PLEDLNNKKD
1060 1070 1080 1090 1100
SCISNHTTIE IGKDLNYLKD GNGTTSGIGS SVEKYVVDES DYMSFINNPS
1110 1120 1130 1140 1150
LTVTVPIALG ESDFENLNTE EFSSESDMEE SKEKLNATSS SEGSTVDIGA
1160 1170 1180 1190 1200
PAEGEQPEAE PEESLEPEAC FTEDCVRKFK CCQISIEEGK GKLWWNLRKT
1210 1220 1230 1240 1250
CYKIVEHNWF ETFIVFMILL SSGALAFEDI YIEQRKTIKT MLEYADKVFT
1260 1270 1280 1290 1300
YIFILEMLLK WVAYGFQMYF TNAWCWLDFL IVDVSLVSLT ANALGYSELG
1310 1320 1330 1340 1350
AIKSLRTLRA LRPLRALSRF EGMRVVVNAL LGAIPSIMNV LLVCLIFWLI
1360 1370 1380 1390 1400
FSIMGVNLFA GKFYHCINYT TGEMFDVSVV NNYSECQALI ESNQTARWKN
1410 1420 1430 1440 1450
VKVNFDNVGL GYLSLLQVAT FKGWMDIMYA AVDSRNVELQ PKYEDNLYMY
1460 1470 1480 1490 1500
LYFVIFIIFG SFFTLNLFIG VIIDNFNQQK KKFGGQDIFM TEEQKKYYNA
1510 1520 1530 1540 1550
MKKLGSKKPQ KPIPRPANKF QGMVFDFVTK QVFDISIMIL ICLNMVTMMV
1560 1570 1580 1590 1600
ETDDQSQEMT NILYWINLVF IVLFTGECVL KLISLRHYYF TIGWNIFDFV
1610 1620 1630 1640 1650
VVILSIVGMF LAELIEKYFV SPTLFRVIRL ARIGRILRLI KGAKGIRTLL
1660 1670 1680 1690 1700
FALMMSLPAL FNIGLLLFLV MFIYAIFGMS NFAYVKREVG IDDMFNFETF
1710 1720 1730 1740 1750
GNSMICLFQI TTSAGWDGLL APILNSGPPD CDPEKDHPGS SVKGDCGNPS
1760 1770 1780 1790 1800
VGIFFFVSYI IISFLVVVNM YIAVILENFS VATEESAEPL SEDDFEMFYE
1810 1820 1830 1840 1850
VWEKFDPDAT QFIEFCKLSD FAAALDPPLL IAKPNKVQLI AMDLPMVSGD
1860 1870 1880 1890 1900
RIHCLDILFA FTKRVLGESG EMDALRIQME ERFMASNPSK VSYEPITTTL
1910 1920 1930 1940 1950
KRKQEEVSAI VIQRAYRRYL LKQKVKKVSS IYKKDKGKED EGTPIKEDII
1960 1970 1980 1990 2000
TDKLNENSTP EKTDVTPSTT SPPSYDSVTK PEKEKFEKDK SEKEDKGKDI
RESKK
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF1M9G9 | F1M9G9_RAT | Sodium channel protein | Scn2a Scn2a1 | 1,944 | Annotation score: | ||
A0A0G2K207 | A0A0G2K207_RAT | Sodium channel protein | Scn2a | 1,860 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X03639 mRNA Translation: CAA27287.1 |
RefSeqi | NP_036779.1, NM_012647.1 |
Genome annotation databases
GeneIDi | 24766 |
KEGGi | rno:24766 |
UCSCi | RGD:3632, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X03639 mRNA Translation: CAA27287.1 |
RefSeqi | NP_036779.1, NM_012647.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BYY | NMR | - | A | 1474-1526 | [»] | |
2KXW | NMR | - | B | 1901-1927 | [»] | |
2M5E | NMR | - | B | 1901-1927 | [»] | |
BMRBi | P04775 | |||||
SMRi | P04775 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 246890, 4 interactors |
CORUMi | P04775 |
DIPi | DIP-57088N |
IntActi | P04775, 2 interactors |
STRINGi | 10116.ENSRNOP00000007069 |
Chemistry databases
BindingDBi | P04775 |
ChEMBLi | CHEMBL3399 |
DrugCentrali | P04775 |
GuidetoPHARMACOLOGYi | 579 |
PTM databases
GlyGeni | P04775, 10 sites |
iPTMneti | P04775 |
PhosphoSitePlusi | P04775 |
SwissPalmi | P04775 |
Proteomic databases
PaxDbi | P04775 |
PRIDEi | P04775 |
Protocols and materials databases
ABCDi | P04775, 1 sequenced antibody |
Genome annotation databases
GeneIDi | 24766 |
KEGGi | rno:24766 |
UCSCi | RGD:3632, rat |
Organism-specific databases
CTDi | 6326 |
RGDi | 3632, Scn2a |
Phylogenomic databases
eggNOGi | KOG2301, Eukaryota |
InParanoidi | P04775 |
OrthoDBi | 56920at2759 |
PhylomeDBi | P04775 |
Enzyme and pathway databases
Reactomei | R-RNO-5576892, Phase 0 - rapid depolarisation |
Miscellaneous databases
EvolutionaryTracei | P04775 |
PROi | PR:P04775 |
Family and domain databases
Gene3Di | 1.20.120.350, 4 hits |
InterProi | View protein in InterPro IPR005821, Ion_trans_dom IPR000048, IQ_motif_EF-hand-BS IPR001696, Na_channel_asu IPR010526, Na_trans_assoc IPR024583, Na_trans_cytopl IPR043203, VGCC_Ca_Na IPR027359, Volt_channel_dom_sf |
PANTHERi | PTHR10037, PTHR10037, 1 hit |
Pfami | View protein in Pfam PF00520, Ion_trans, 4 hits PF06512, Na_trans_assoc, 1 hit PF11933, Na_trans_cytopl, 1 hit |
PRINTSi | PR00170, NACHANNEL |
SMARTi | View protein in SMART SM00015, IQ, 1 hit |
PROSITEi | View protein in PROSITE PS50096, IQ, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SCN2A_RAT | |
Accessioni | P04775Primary (citable) accession number: P04775 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 13, 1987 |
Last sequence update: | August 13, 1987 | |
Last modified: | February 10, 2021 | |
This is version 172 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families