UniProtKB - P15389 (SCN5A_RAT)
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Protein
Sodium channel protein type 5 subunit alpha
Gene
Scn5a
Organism
Rattus norvegicus (Rat)
Status
Functioni
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. It is a tetrodotoxin-resistant Na+ channel isoform. This channel is responsible for the initial upstroke of the action potential. Channel inactivation is regulated by intracellular calcium levels.By similarity
Miscellaneous
Na+ channels in mammalian cardiac membrane have functional properties quite distinct from Na+ channels in nerve and skeletal muscle.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sitei | 374 | Cys residue near the selectivity filter, which has a free thiol that is susceptible to reaction with methanethiosulfonate (MTSET); Sodium current is irreversibly blocked by MTSETBy similarity1 Publication | 1 |
GO - Molecular functioni
- ankyrin binding Source: RGD
- calmodulin binding Source: UniProtKB-KW
- fibroblast growth factor binding Source: RGD
- voltage-gated sodium channel activity Source: UniProtKB
- voltage-gated sodium channel activity involved in AV node cell action potential Source: BHF-UCL
- voltage-gated sodium channel activity involved in bundle of His cell action potential Source: BHF-UCL
- voltage-gated sodium channel activity involved in cardiac muscle cell action potential Source: BHF-UCL
- voltage-gated sodium channel activity involved in Purkinje myocyte action potential Source: BHF-UCL
- voltage-gated sodium channel activity involved in SA node cell action potential Source: BHF-UCL
GO - Biological processi
- atrial cardiac muscle cell action potential Source: BHF-UCL
- AV node cell action potential Source: BHF-UCL
- AV node cell to bundle of His cell communication Source: BHF-UCL
- brainstem development Source: RGD
- bundle of His cell action potential Source: BHF-UCL
- cardiac muscle cell action potential involved in contraction Source: BHF-UCL
- cardiac muscle contraction Source: BHF-UCL
- cellular response to calcium ion Source: UniProtKB
- cerebellum development Source: RGD
- membrane depolarization Source: BHF-UCL
- membrane depolarization during action potential Source: BHF-UCL
- membrane depolarization during AV node cell action potential Source: BHF-UCL
- membrane depolarization during bundle of His cell action potential Source: BHF-UCL
- membrane depolarization during cardiac muscle cell action potential Source: BHF-UCL
- membrane depolarization during Purkinje myocyte cell action potential Source: BHF-UCL
- membrane depolarization during SA node cell action potential Source: BHF-UCL
- neuronal action potential Source: GO_Central
- odontogenesis of dentin-containing tooth Source: RGD
- positive regulation of action potential Source: RGD
- positive regulation of epithelial cell proliferation Source: RGD
- positive regulation of heart rate Source: RGD
- positive regulation of sodium ion transport Source: BHF-UCL
- regulation of atrial cardiac muscle cell membrane depolarization Source: BHF-UCL
- regulation of atrial cardiac muscle cell membrane repolarization Source: BHF-UCL
- regulation of cardiac muscle cell contraction Source: BHF-UCL
- regulation of heart rate Source: BHF-UCL
- regulation of heart rate by cardiac conduction Source: BHF-UCL
- regulation of sodium ion transmembrane transport Source: BHF-UCL
- regulation of ventricular cardiac muscle cell membrane depolarization Source: BHF-UCL
- regulation of ventricular cardiac muscle cell membrane repolarization Source: BHF-UCL
- response to denervation involved in regulation of muscle adaptation Source: RGD
- SA node cell action potential Source: BHF-UCL
- sodium ion transmembrane transport Source: RGD
- sodium ion transport Source: UniProtKB
- telencephalon development Source: RGD
Keywordsi
| Molecular function | Calmodulin-binding, Ion channel, Sodium channel, Voltage-gated channel |
| Biological process | Ion transport, Sodium transport, Transport |
| Ligand | Sodium |
Names & Taxonomyi
| Protein namesi | Recommended name: Sodium channel protein type 5 subunit alphaAlternative name(s): Sodium channel protein cardiac muscle subunit alpha Sodium channel protein type V subunit alpha Voltage-gated sodium channel subunit alpha Nav1.5 |
| Gene namesi | Name:Scn5a |
| 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 | 3637. Scn5a. |
Subcellular locationi
- Cell membrane By similarity; Multi-pass membrane protein By similarity
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Topological domaini | 1 – 132 | CytoplasmicCuratedAdd BLAST | 132 | |
| Transmembranei | 133 – 151 | Helical; Name=S1 of repeat IBy similarityAdd BLAST | 19 | |
| Topological domaini | 152 – 158 | ExtracellularCurated | 7 | |
| Transmembranei | 159 – 179 | Helical; Name=S2 of repeat IBy similarityAdd BLAST | 21 | |
| Topological domaini | 180 – 193 | CytoplasmicCuratedAdd BLAST | 14 | |
| Transmembranei | 194 – 211 | Helical; Name=S3 of repeat IBy similarityAdd BLAST | 18 | |
| Topological domaini | 212 – 217 | ExtracellularCurated | 6 | |
| Transmembranei | 218 – 234 | Helical; Name=S4 of repeat IBy similarityAdd BLAST | 17 | |
| Topological domaini | 235 – 253 | CytoplasmicCuratedAdd BLAST | 19 | |
| Transmembranei | 254 – 273 | Helical; Name=S5 of repeat IBy similarityAdd BLAST | 20 | |
| Topological domaini | 274 – 358 | ExtracellularCuratedAdd BLAST | 85 | |
| Intramembranei | 359 – 383 | Pore-formingBy similarityAdd BLAST | 25 | |
| Topological domaini | 384 – 390 | ExtracellularCurated | 7 | |
| Transmembranei | 391 – 411 | Helical; Name=S6 of repeat IBy similarityAdd BLAST | 21 | |
| Topological domaini | 412 – 718 | CytoplasmicCuratedAdd BLAST | 307 | |
| Transmembranei | 719 – 737 | Helical; Name=S1 of repeat IIBy similarityAdd BLAST | 19 | |
| Topological domaini | 738 – 748 | ExtracellularCuratedAdd BLAST | 11 | |
| Transmembranei | 749 – 768 | Helical; Name=S2 of repeat IIBy similarityAdd BLAST | 20 | |
| Topological domaini | 769 – 782 | CytoplasmicCuratedAdd BLAST | 14 | |
| Transmembranei | 783 – 802 | Helical; Name=S3 of repeat IIBy similarityAdd BLAST | 20 | |
| Topological domaini | 803 – 804 | ExtracellularCurated | 2 | |
| Transmembranei | 805 – 822 | Helical; Name=S4 of repeat IIBy similarityAdd BLAST | 18 | |
| Topological domaini | 823 – 838 | CytoplasmicCuratedAdd BLAST | 16 | |
| Transmembranei | 839 – 857 | Helical; Name=S5 of repeat IIBy similarityAdd BLAST | 19 | |
| Topological domaini | 858 – 886 | ExtracellularCuratedAdd BLAST | 29 | |
| Intramembranei | 887 – 907 | Pore-formingBy similarityAdd BLAST | 21 | |
| Topological domaini | 908 – 920 | ExtracellularCuratedAdd BLAST | 13 | |
| Transmembranei | 921 – 941 | Helical; Name=S6 of repeat IIBy similarityAdd BLAST | 21 | |
| Topological domaini | 942 – 1208 | CytoplasmicCuratedAdd BLAST | 267 | |
| Transmembranei | 1209 – 1226 | Helical; Name=S1 of repeat IIIBy similarityAdd BLAST | 18 | |
| Topological domaini | 1227 – 1239 | ExtracellularCuratedAdd BLAST | 13 | |
| Transmembranei | 1240 – 1258 | Helical; Name=S2 of repeat IIIBy similarityAdd BLAST | 19 | |
| Topological domaini | 1259 – 1272 | CytoplasmicCuratedAdd BLAST | 14 | |
| Transmembranei | 1273 – 1291 | Helical; Name=S3 of repeat IIIBy similarityAdd BLAST | 19 | |
| Topological domaini | 1292 – 1299 | ExtracellularCurated | 8 | |
| Transmembranei | 1300 – 1318 | Helical; Name=S4 of repeat IIIBy similarityAdd BLAST | 19 | |
| Topological domaini | 1319 – 1335 | CytoplasmicCuratedAdd BLAST | 17 | |
| Transmembranei | 1336 – 1355 | Helical; Name=S5 of repeat IIIBy similarityAdd BLAST | 20 | |
| Topological domaini | 1356 – 1407 | ExtracellularCuratedAdd BLAST | 52 | |
| Intramembranei | 1408 – 1429 | Pore-formingBy similarityAdd BLAST | 22 | |
| Topological domaini | 1430 – 1446 | ExtracellularCuratedAdd BLAST | 17 | |
| Transmembranei | 1447 – 1468 | Helical; Name=S6 of repeat IIIBy similarityAdd BLAST | 22 | |
| Topological domaini | 1469 – 1531 | CytoplasmicCuratedAdd BLAST | 63 | |
| Transmembranei | 1532 – 1549 | Helical; Name=S1 of repeat IVBy similarityAdd BLAST | 18 | |
| Topological domaini | 1550 – 1560 | ExtracellularCuratedAdd BLAST | 11 | |
| Transmembranei | 1561 – 1579 | Helical; Name=S2 of repeat IVBy similarityAdd BLAST | 19 | |
| Topological domaini | 1580 – 1591 | CytoplasmicCuratedAdd BLAST | 12 | |
| Transmembranei | 1592 – 1609 | Helical; Name=S3 of repeat IVBy similarityAdd BLAST | 18 | |
| Topological domaini | 1610 – 1622 | ExtracellularCuratedAdd BLAST | 13 | |
| Transmembranei | 1623 – 1639 | Helical; Name=S4 of repeat IVBy similarityAdd BLAST | 17 | |
| Topological domaini | 1640 – 1658 | CytoplasmicCuratedAdd BLAST | 19 | |
| Transmembranei | 1659 – 1676 | Helical; Name=S5 of repeat IVBy similarityAdd BLAST | 18 | |
| Topological domaini | 1677 – 1698 | ExtracellularCuratedAdd BLAST | 22 | |
| Intramembranei | 1699 – 1721 | Pore-formingBy similarityAdd BLAST | 23 | |
| Topological domaini | 1722 – 1750 | ExtracellularCuratedAdd BLAST | 29 | |
| Transmembranei | 1751 – 1773 | Helical; Name=S6 of repeat IVBy similarityAdd BLAST | 23 | |
| Topological domaini | 1774 – 2019 | CytoplasmicCuratedAdd BLAST | 246 |
GO - Cellular componenti
- caveola Source: BHF-UCL
- endoplasmic reticulum Source: BHF-UCL
- integral component of membrane Source: UniProtKB
- intercalated disc Source: BHF-UCL
- T-tubule Source: BHF-UCL
- voltage-gated sodium channel complex Source: BHF-UCL
- Z disc Source: BHF-UCL
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 869 | L → C: >1000-fold increase of sensitivity to the conotoxin GVIIJ(SSG). 1 Publication | 1 | |
| Mutagenesisi | 1612 | D → N or R: Little change in voltage-dependence of conductance and decrease in affinity to the sea anemone toxin anthopleurin-B (residue Lys-37). 1 Publication | 1 |
Chemistry databases
| ChEMBLi | CHEMBL3866. |
| GuidetoPHARMACOLOGYi | 582. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000048498 | 1 – 2019 | Sodium channel protein type 5 subunit alphaAdd BLAST | 2019 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 37 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 39 | PhosphothreonineBy similarity | 1 | |
| Glycosylationi | 215 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 281 ↔ 336 | By similarity | ||
| Glycosylationi | 284 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 289 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 292 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 319 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 329 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Modified residuei | 458 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 461 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 484 | PhosphoserineCombined sources | 1 | |
| Modified residuei | 485 | PhosphoserineCombined sources | 1 | |
| Modified residuei | 487 | PhosphothreonineCombined sources | 1 | |
| Modified residuei | 498 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 511 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 527 | Dimethylated arginine; alternateBy similarity | 1 | |
| Modified residuei | 527 | Omega-N-methylarginine; alternateBy similarity | 1 | |
| Modified residuei | 540 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 572 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 665 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 668 | PhosphoserineBy similarity | 1 | |
| Glycosylationi | 741 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 804 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 865 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 909 ↔ 918 | By similarity | ||
| Glycosylationi | 1367 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 1376 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 1382 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 1390 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Modified residuei | 1505 | Phosphoserine; by PKCBy similarity | 1 |
Post-translational modificationi
Phosphorylation at Ser-1505 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. Regulated through phosphorylation by CaMK2D.By similarity
Ubiquitinated by NEDD4L; which promotes its endocytosis. Does not seem to be ubiquitinated by NEDD4 or WWP2.By similarity
Lacks the cysteine which covalently binds the conotoxin GVIIJ. This cysteine (position 869) is speculated in other sodium channel subunits alpha to be implied in covalent binding with the sodium channel subunit beta-2 or beta-4.1 Publication
Keywords - PTMi
Disulfide bond, Glycoprotein, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
| PaxDbi | P15389. |
| PRIDEi | P15389. |
PTM databases
| iPTMneti | P15389. |
| PhosphoSitePlusi | P15389. |
Expressioni
Tissue specificityi
Strongly expressed in the heart. Also expressed in adult and fetal brain, spinal cord, testis, and at moderate levels in kidney, adrenal gland, lung, skeletal muscle, spleen, stomach and bladder. Isoform 2 is expressed in brain.2 Publications
Interactioni
Subunit structurei
Interacts with the PDZ domain of the syntrophin SNTA1, SNTB1 and SNTB2. Interacts with NEDD4, NEDD4L, WWP2 and GPD1L. Interacts with CALM. Interacts with FGF13; the interaction is direct and may regulate SNC5A density at membranes and function. May also interact with FGF12 and FGF14.By similarity
GO - Molecular functioni
- ankyrin binding Source: RGD
- calmodulin binding Source: UniProtKB-KW
- fibroblast growth factor binding Source: RGD
Protein-protein interaction databases
| DIPi | DIP-60063N. |
| STRINGi | 10116.ENSRNOP00000060180. |
Chemistry databases
| BindingDBi | P15389. |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Repeati | 114 – 421 | ICuratedAdd BLAST | 308 | |
| Repeati | 700 – 972 | IICuratedAdd BLAST | 273 | |
| Repeati | 1189 – 1503 | IIICuratedAdd BLAST | 315 | |
| Repeati | 1512 – 1809 | IVCuratedAdd BLAST | 298 | |
| Domaini | 1903 – 1932 | IQAdd BLAST | 30 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Regioni | 1841 – 1903 | Interaction with FGF13By similarityAdd BLAST | 63 | |
| Regioni | 1977 – 1980 | Interaction with NEDD4, NEDD4L and WWP2By similarity | 4 |
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
The IQ domain mediates association with calmodulin.By similarity
Sequence similaritiesi
Belongs to the sodium channel (TC 1.A.1.10) family. Nav1.5/SCN5A subfamily. [View classification]Curated
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
| eggNOGi | KOG2301. Eukaryota. ENOG410XNP6. LUCA. |
| HOGENOMi | HOG000231755. |
| HOVERGENi | HBG053100. |
| InParanoidi | P15389. |
| KOi | K04838. |
| PhylomeDBi | P15389. |
Family and domain databases
| InterProi | View protein in InterPro IPR005821. Ion_trans_dom. IPR008053. Na_channel_a5su. IPR001696. Na_channel_asu. IPR010526. Na_trans_assoc. IPR024583. Na_trans_cytopl. |
| 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. PR01666. NACHANNEL5. |
Sequences (2)i
Sequence statusi: Complete.
This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P15389-1) [UniParc]FASTAAdd to basket
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.
10 20 30 40 50
MANLLLPRGT SSFRRFTRES LAAIEKRMAE KQARGGSATS QESREGLQEE
60 70 80 90 100
EAPRPQLDLQ ASKKLPDLYG NPPRELIGEP LEDLDPFYST QKTFIVLNKG
110 120 130 140 150
KTIFRFSATN ALYVLSPFHP VRRAAVKILV HSLFSMLIMC TILTNCVFMA
160 170 180 190 200
QHDPPPWTKY VEYTFTAIYT FESLVKILAR GFCLHAFTFL RDPWNWLDFS
210 220 230 240 250
VIVMAYTTEF VDLGNVSALR TFRVLRALKT ISVISGLKTI VGALIQSVKK
260 270 280 290 300
LADVMVLTVF CLSVFALIGL QLFMGNLRHK CVRNFTELNG TNGSVEADGL
310 320 330 340 350
VWNSLDVYLN DPANYLLKNG TTDVLLCGNS SDAGTCPEGY RCLKAGENPD
360 370 380 390 400
HGYTSFDSFA WAFLALFRLM TQDCWERLYQ QTLRSAGKIY MIFFMLVIFL
410 420 430 440 450
GSFYLVNLIL AVVAMAYEEQ NQATIAETEE KEKRFQEAME MLKKEHEALT
460 470 480 490 500
IRGVDTVSRS SLEMSPLAPV TNHERKSKRR KRLSSGTEDG GDDRLPKSDS
510 520 530 540 550
EDGPRALNQL SLTHGLSRTS MRPRSSRGSI FTFRRRDQGS EADFADDENS
560 570 580 590 600
TAGESESHRT SLLVPWPLRH PSAQGQPGPG ASAPGYVLNG KRNSTVDCNG
610 620 630 640 650
VVSLLGAGDA EATSPGSYLL RPMVLDRPPD TTTPSEEPGG PQMLTPQAPC
660 670 680 690 700
ADGFEEPGAR QRALSAVSVL TSALEELEES HRKCPPCWNR FAQHYLIWEC
710 720 730 740 750
CPLWMSIKQK VKFVVMDPFA DLTITMCIVL NTLFMALEHY NMTAEFEEML
760 770 780 790 800
QVGNLVFTGI FTAEMTFKII ALDPYYYFQQ GWNIFDSIIV ILSLMELGLS
810 820 830 840 850
RMGNLSVLRS FRLLRVFKLA KSWPTLNTLI KIIGNSVGAL GNLTLVLAII
860 870 880 890 900
VFIFAVVGMQ LFGKNYSELR HRISDSGLLP RWHMMDFFHA FLIIFRILCG
910 920 930 940 950
EWIETMWDCM EVSGQSLCLL VFLLVMVIGN LVVLNLFLAL LLSSFSADNL
960 970 980 990 1000
TAPDEDGEMN NLQLALARIQ RGLRFVKRTT WDFCCGILRR RPKKPAALAT
1010 1020 1030 1040 1050
HSQLPSCITA PRSPPPPEVE KVPPARKETR FEEDKRPGQG TPGDSEPVCV
1060 1070 1080 1090 1100
PIAVAESDTE DQEEDEENSL GTEEESSKQE SQVVSGGHEP YQEPRAWSQV
1110 1120 1130 1140 1150
SETTSSEAGA STSQADWQQE QKTEPQAPGC GETPEDSYSE GSTADMTNTA
1160 1170 1180 1190 1200
DLLEQIPDLG EDVKDPEDCF TEGCVRRCPC CMVDTTQSPG KVWWRLRKTC
1210 1220 1230 1240 1250
YRIVEHSWFE TFIIFMILLS SGALAFEDIY LEERKTIKVL LEYADKMFTY
1260 1270 1280 1290 1300
VFVLEMLLKW VAYGFKKYFT NAWCWLDFLI VDVSLVSLVA NTLGFAEMGP
1310 1320 1330 1340 1350
IKSLRTLRAL RPLRALSRFE GMRVVVNALV GAIPSIMNVL LVCLIFWLIF
1360 1370 1380 1390 1400
SIMGVNLFAG KFGRCINQTE GDLPLNYTIV NNKSECESFN VTGELYWTKV
1410 1420 1430 1440 1450
KVNFDNVGAG YLALLQVATF KGWMDIMYAA VDSRGYEEQP QWEDNLYMYI
1460 1470 1480 1490 1500
YFVVFIIFGS FFTLNLFIGV IIDNFNQQKK KLGGQDIFMT EEQKKYYNAM
1510 1520 1530 1540 1550
KKLGSKKPQK PIPRPLNKYQ GFIFDIVTKQ AFDVTIMFLI CLNMVTMMVE
1560 1570 1580 1590 1600
TDDQSPEKVN ILAKINLLFV AIFTGECIVK MAALRHYYFT NSWNIFDFVV
1610 1620 1630 1640 1650
VILSIVGTVL SDIIQKYFFS PTLFRVIRLA RIGRILRLIR GAKGIRTLLF
1660 1670 1680 1690 1700
ALMMSLPALF NIGLLLFLVM FIYSIFGMAN FAYVKWEAGI DDMFNFQTFA
1710 1720 1730 1740 1750
NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLPNSNGS RGNCGSPAVG
1760 1770 1780 1790 1800
ILFFTTYIII SFLIVVNMYI AIILENFSVA TEESTEPLSE DDFDMFYEIW
1810 1820 1830 1840 1850
EKFDPEATQF IEYLALSDFA DALSEPLRIA KPNQISLINM DLPMVSGDRI
1860 1870 1880 1890 1900
HCMDILFAFT KRVLGESGEM DALKIQMEEK FMAANPSKIS YEPITTTLRR
1910 1920 1930 1940 1950
KHEEVSATVI QRAFRRHLLQ RSVKHASFLF RQQAGGSGLS DEDAPEREGL
1960 1970 1980 1990 2000
IAYMMNGNFS RRSAPLSSSS ISSTSFPPSY DSVTRATSDN LPVRASDYSR
2010
SEDLADFPPS PDRDRESIV
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Alternative sequenceiVSP_037482 | 1080 – 1132 | Missing in isoform 2. 1 PublicationAdd BLAST | 53 |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M27902 mRNA. Translation: AAA42114.1. AF353637 mRNA. Translation: AAK38884.1. |
| PIRi | A33996. |
| RefSeqi | NP_001153634.1. NM_001160162.1. [P15389-2] NP_037257.1. NM_013125.2. [P15389-1] |
| UniGenei | Rn.32074. |
Genome annotation databases
| GeneIDi | 25665. |
| KEGGi | rno:25665. |
| UCSCi | RGD:3637. rat. [P15389-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar 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. |
Entry informationi
| Entry namei | SCN5A_RAT | |
| Accessioni | P15389Primary (citable) accession number: P15389 Secondary accession number(s): Q925G6 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
| Last sequence update: | April 1, 1990 | |
| Last modified: | May 10, 2017 | |
| This is version 135 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
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families
