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P15389

- SCN5A_RAT

UniProt

P15389 - SCN5A_RAT

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Protein

Sodium channel protein type 5 subunit alpha

Gene

Scn5a

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

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. Channel inactivation is regulated by intracellular calcium levels (By similarity).By similarity

GO - Molecular functioni

  1. ankyrin binding Source: BHF-UCL
  2. fibroblast growth factor binding Source: RGD
  3. voltage-gated sodium channel activity Source: UniProtKB

GO - Biological processi

  1. brainstem development Source: RGD
  2. cellular response to calcium ion Source: UniProtKB
  3. cerebellum development Source: RGD
  4. membrane depolarization during action potential Source: RefGenome
  5. neuronal action potential Source: RefGenome
  6. odontogenesis of dentin-containing tooth Source: RGD
  7. positive regulation of action potential Source: RGD
  8. positive regulation of epithelial cell proliferation Source: RGD
  9. positive regulation of heart rate Source: RGD
  10. response to denervation involved in regulation of muscle adaptation Source: RGD
  11. sodium ion transmembrane transport Source: RGD
  12. sodium ion transport Source: UniProtKB
  13. telencephalon development 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

Calmodulin-binding, Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium channel protein type 5 subunit alpha
Alternative 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3637. Scn5a.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. intercalated disc Source: BHF-UCL
  3. T-tubule Source: BHF-UCL
  4. voltage-gated sodium channel complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20192019Sodium channel protein type 5 subunit alphaPRO_0000048498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei39 – 391PhosphothreonineBy similarity
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
Modified residuei458 – 4581PhosphoserineBy similarity
Modified residuei461 – 4611PhosphoserineBy similarity
Modified residuei484 – 4841PhosphoserineBy similarity
Modified residuei485 – 4851PhosphoserineBy similarity
Modified residuei498 – 4981PhosphoserineBy similarity
Modified residuei511 – 5111PhosphoserineBy similarity
Modified residuei527 – 5271Dimethylated arginine; alternateBy similarity
Modified residuei527 – 5271Omega-N-methylarginine; alternateBy similarity
Modified residuei572 – 5721PhosphoserineBy similarity
Modified residuei665 – 6651PhosphoserineBy similarity
Modified residuei668 – 6681PhosphoserineBy similarity
Glycosylationi741 – 7411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi804 – 8041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi865 – 8651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1367 – 13671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1376 – 13761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1382 – 13821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1390 – 13901N-linked (GlcNAc...)Sequence Analysis
Modified residuei1505 – 15051Phosphoserine; by PKCBy similarity

Post-translational modificationi

Regulated through phosphorylation by CaMK2D.By similarity
Ubiquitinated by NEDD4L; which promotes its endocytosis.By similarity
Phosphorylation at Ser-1505 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents.By similarity

Keywords - PTMi

Glycoprotein, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP15389.
PRIDEiP15389.

PTM databases

PhosphoSiteiP15389.

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

Gene expression databases

GenevestigatoriP15389.

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 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-60063N.

Structurei

3D structure databases

ProteinModelPortaliP15389.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 127127CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini152 – 1598ExtracellularSequence Analysis
Topological domaini180 – 19213CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini212 – 2176ExtracellularSequence Analysis
Topological domaini238 – 25316CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini278 – 390113ExtracellularSequence AnalysisAdd
BLAST
Topological domaini417 – 712296CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini738 – 74811ExtracellularSequence AnalysisAdd
BLAST
Topological domaini773 – 7808CytoplasmicSequence Analysis
Topological domaini801 – 8066ExtracellularSequence Analysis
Topological domaini827 – 84216CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini864 – 91653ExtracellularSequence AnalysisAdd
BLAST
Topological domaini943 – 1202260CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1227 – 123913ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1266 – 12716CytoplasmicSequence Analysis
Topological domaini1294 – 12974ExtracellularSequence Analysis
Topological domaini1320 – 133819CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1362 – 144584ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1473 – 152553CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1550 – 156011ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1585 – 15906CytoplasmicSequence Analysis
Topological domaini1615 – 162410ExtracellularSequence Analysis
Topological domaini1647 – 166115CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1685 – 174965ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1775 – 2019245CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei128 – 15124Helical; Name=S1 of repeat ISequence AnalysisAdd
BLAST
Transmembranei160 – 17920Helical; Name=S2 of repeat ISequence AnalysisAdd
BLAST
Transmembranei193 – 21119Helical; Name=S3 of repeat ISequence AnalysisAdd
BLAST
Transmembranei218 – 23720Helical; Voltage-sensor; Name=S4 of repeat ISequence AnalysisAdd
BLAST
Transmembranei254 – 27724Helical; Name=S5 of repeat ISequence AnalysisAdd
BLAST
Transmembranei391 – 41626Helical; Name=S6 of repeat ISequence AnalysisAdd
BLAST
Transmembranei713 – 73725Helical; Name=S1 of repeat IISequence AnalysisAdd
BLAST
Transmembranei749 – 77224Helical; Name=S2 of repeat IISequence AnalysisAdd
BLAST
Transmembranei781 – 80020Helical; Name=S3 of repeat IISequence AnalysisAdd
BLAST
Transmembranei807 – 82620Helical; Voltage-sensor; Name=S4 of repeat IISequence AnalysisAdd
BLAST
Transmembranei843 – 86321Helical; Name=S5 of repeat IISequence AnalysisAdd
BLAST
Transmembranei917 – 94226Helical; Name=S6 of repeat IISequence AnalysisAdd
BLAST
Transmembranei1203 – 122624Helical; Name=S1 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1240 – 126526Helical; Name=S2 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1272 – 129322Helical; Name=S3 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1298 – 131922Helical; Voltage-sensor; Name=S4 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1339 – 136123Helical; Name=S5 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1446 – 147227Helical; Name=S6 of repeat IIISequence AnalysisAdd
BLAST
Transmembranei1526 – 154924Helical; Name=S1 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1561 – 158424Helical; Name=S2 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1591 – 161424Helical; Name=S3 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1625 – 164622Helical; Voltage-sensor; Name=S4 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1662 – 168423Helical; Name=S5 of repeat IVSequence AnalysisAdd
BLAST
Transmembranei1750 – 177425Helical; Name=S6 of repeat IVSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1903 – 193230IQAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1841 – 190363Interaction with FGF13By similarityAdd
BLAST
Regioni1977 – 19804Interaction with NEDD4, NEDD4L and WWP2By similarity

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.
The IQ domain mediates association with calmodulin.By similarity

Sequence similaritiesi

Contains 1 IQ domain.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
HOGENOMiHOG000231755.
HOVERGENiHBG053100.
InParanoidiP15389.
KOiK04838.
PhylomeDBiP15389.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR024583. DUF3451.
IPR005821. Ion_trans_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR008053. Na_channel_a5su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PfamiPF11933. DUF3451. 1 hit.
PF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSiPR00170. NACHANNEL.
PR01666. NACHANNEL5.
SMARTiSM00015. IQ. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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.

« Hide

        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
Length:2,019
Mass (Da):227,367
Last modified:April 1, 1990 - v1
Checksum:iCFC3B03CEAE708AD
GO
Isoform 2 (identifier: P15389-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1080-1132: Missing.

Show »
Length:1,966
Mass (Da):221,706
Checksum:iE4AC1FB7CF825647
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1080 – 113253Missing in isoform 2. 1 PublicationVSP_037482Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27902 mRNA. Translation: AAA42114.1.
AF353637 mRNA. Translation: AAK38884.1.
PIRiA33996.
RefSeqiNP_001153634.1. NM_001160162.1. [P15389-2]
NP_037257.1. NM_013125.2. [P15389-1]
UniGeneiRn.32074.

Genome annotation databases

GeneIDi25665.
KEGGirno:25665.
UCSCiRGD:3637. rat. [P15389-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

3D structure databases

ProteinModelPortali P15389.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60063N.

Chemistry

BindingDBi P15389.
ChEMBLi CHEMBL3866.
GuidetoPHARMACOLOGYi 582.

PTM databases

PhosphoSitei P15389.

Proteomic databases

PaxDbi P15389.
PRIDEi P15389.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25665.
KEGGi rno:25665.
UCSCi RGD:3637. rat. [P15389-1 ]

Organism-specific databases

CTDi 6331.
RGDi 3637. Scn5a.

Phylogenomic databases

eggNOGi COG1226.
HOGENOMi HOG000231755.
HOVERGENi HBG053100.
InParanoidi P15389.
KOi K04838.
PhylomeDBi P15389.

Miscellaneous databases

NextBioi 607581.
PROi P15389.

Gene expression databases

Genevestigatori P15389.

Family and domain databases

Gene3Di 1.20.120.350. 4 hits.
InterProi IPR027359. Channel_four-helix_dom.
IPR024583. DUF3451.
IPR005821. Ion_trans_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR008053. Na_channel_a5su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view ]
Pfami PF11933. DUF3451. 1 hit.
PF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view ]
PRINTSi PR00170. NACHANNEL.
PR01666. NACHANNEL5.
SMARTi SM00015. IQ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of a putative tetrodotoxin-resistant rat heart Na+ channel isoform."
    Rogart R.B., Cribbs L.L., Muglia L.K., Kephart D.D., Kaiser M.W.
    Proc. Natl. Acad. Sci. U.S.A. 86:8170-8174(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  2. "Characterisation of the novel voltage-gated Na+ channel rNav1.5a isolated from the rat hippocampal progenitor stem cell line HiB5."
    Korsgaard M.P.G., Christophersen P., Ahring P.K., Olesen S.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: Sprague-Dawley.
  3. "New variants of Nav1.5/SCN5A encode Na+ channels in the brain."
    Wang J., Ou S.-W., Wang Y.-J., Zong Z.-H., Lin L., Kameyama M., Kameyama A.
    J. Neurogenet. 22:57-75(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  4. "Analysis of four novel variants of Nav1.5/SCN5A cloned from the brain."
    Wang J., Ou S.-W., Wang Y.-J., Kameyama M., Kameyama A., Zong Z.-H.
    Neurosci. Res. 64:339-347(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSCN5A_RAT
AccessioniPrimary (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: October 29, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Na+ channels in mammalian cardiac membrane have functional properties quite distinct from Na+ channels in nerve and skeletal muscle.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3