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Sodium channel protein type 5 subunit alpha (Sodium channel protein cardiac muscle subunit alpha) (Sodium channel protein type V subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.5) (mH1)

 SCN5A_MOUSE             Reviewed;        2019 AA.
Q9JJV9; E9Q1D2; Q3UH91;
16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 129.
RecName: Full=Sodium channel protein type 5 subunit alpha;
AltName: Full=Sodium channel protein cardiac muscle subunit alpha;
AltName: Full=Sodium channel protein type V subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.5;
AltName: Full=mH1;
Name=Scn5a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Heart;
PubMed=11834499; DOI=10.1152/ajpheart.00644.2001;
Zimmer T., Bollensdorff C., Haufe V., Birch-Hirschfeld E.,
Benndorf K.;
"Mouse heart Na+ channels: primary structure and function of two
isoforms and alternatively spliced variants.";
Am. J. Physiol. 282:H1007-H1017(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
INTERACTION WITH SNTA1; SNTB1 AND SNTB2.
PubMed=9412493;
Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R.,
Froehner S.C.;
"Interaction of muscle and brain sodium channels with multiple members
of the syntrophin family of dystrophin-associated proteins.";
J. Neurosci. 18:128-137(1998).
[5]
PHOSPHORYLATION BY CAMK2D.
PubMed=17124532; DOI=10.1172/JCI26620;
Wagner S., Dybkova N., Rasenack E.C., Jacobshagen C., Fabritz L.,
Kirchhof P., Maier S.K., Zhang T., Hasenfuss G., Brown J.H.,
Bers D.M., Maier L.S.;
"Ca2+/calmodulin-dependent protein kinase II regulates cardiac Na+
channels.";
J. Clin. Invest. 116:3127-3138(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457; SER-484 AND
SER-539, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Heart, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH FGF13.
PubMed=21817159; DOI=10.1161/CIRCRESAHA.111.247957;
Wang C., Hennessey J.A., Kirkton R.D., Wang C., Graham V.,
Puranam R.S., Rosenberg P.B., Bursac N., Pitt G.S.;
"Fibroblast growth factor homologous factor 13 regulates Na+ channels
and conduction velocity in murine hearts.";
Circ. Res. 109:775-782(2011).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23420830; DOI=10.1161/CIRCEP.111.000206;
Chakrabarti S., Wu X., Yang Z., Wu L., Yong S.L., Zhang C., Hu K.,
Wang Q.K., Chen Q.;
"MOG1 rescues defective trafficking of Na(v)1.5 mutations in Brugada
syndrome and sick sinus syndrome.";
Circ. Arrhythm. Electrophysiol. 6:392-401(2013).
[9]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-526, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: 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 (PubMed:11834499, PubMed:23420830). 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).
{ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:11834499,
ECO:0000269|PubMed:23420830}.
-!- SUBUNIT: Interacts with the PDZ domain of the syntrophin SNTA1,
SNTB1 and SNTB2 (PubMed:9412493). Interacts with NEDD4, NEDD4L,
WWP2 and GPD1L (By similarity). Interacts with CALM (By
similarity). Interacts with FGF13; the interaction is direct and
may regulate SNC5A density at membranes and function
(PubMed:21817159). Interacts with FGF12 and FGF14 (By similarity).
{ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:21817159,
ECO:0000269|PubMed:9412493}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11834499,
ECO:0000269|PubMed:23420830}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:D0E0C2}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:Q14524}. Note=RANGRF promotes trafficking
to the cell membrane. {ECO:0000269|PubMed:23420830}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9JJV9-1; Sequence=Displayed;
Name=2;
IsoId=Q9JJV9-2; Sequence=VSP_037444;
-!- TISSUE SPECIFICITY: Expressed in the myocardium.
{ECO:0000269|PubMed:11834499}.
-!- DOMAIN: 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. {ECO:0000305}.
-!- DOMAIN: The IQ domain mediates association with calmodulin.
{ECO:0000250|UniProtKB:Q14524}.
-!- PTM: 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). Regulated through
phosphorylation by CaMK2D (PubMed:17124532).
{ECO:0000250|UniProtKB:Q14524, ECO:0000269|PubMed:17124532}.
-!- PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. Does
not seem to be ubiquitinated by NEDD4 or WWP2.
{ECO:0000250|UniProtKB:Q14524}.
-!- PTM: Lacks the cysteine which covalently binds the conotoxin
GVIIJ. This cysteine (position 868) is speculated in other sodium
channel subunits alpha to be implied in covalent binding with the
sodium channel subunit beta-2 or beta-4.
{ECO:0000250|UniProtKB:P15389}.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.5/SCN5A subfamily. {ECO:0000305}.
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EMBL; AJ271477; CAB70096.1; -; mRNA.
EMBL; AK147254; BAE27800.1; -; mRNA.
EMBL; AK147517; BAE27966.1; -; mRNA.
EMBL; AC121922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC171201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001240789.1; NM_001253860.1.
RefSeq; NP_067519.2; NM_021544.4.
UniGene; Mm.103584; -.
ProteinModelPortal; Q9JJV9; -.
BioGrid; 203101; 2.
DIP; DIP-46142N; -.
IntAct; Q9JJV9; 4.
MINT; Q9JJV9; -.
STRING; 10090.ENSMUSP00000066228; -.
iPTMnet; Q9JJV9; -.
PhosphoSitePlus; Q9JJV9; -.
PaxDb; Q9JJV9; -.
PRIDE; Q9JJV9; -.
Ensembl; ENSMUST00000120420; ENSMUSP00000113272; ENSMUSG00000032511. [Q9JJV9-1]
GeneID; 20271; -.
KEGG; mmu:20271; -.
UCSC; uc009sbc.2; mouse. [Q9JJV9-2]
CTD; 6331; -.
MGI; MGI:98251; Scn5a.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128242; -.
HOGENOM; HOG000231755; -.
InParanoid; Q9JJV9; -.
KO; K04838; -.
TreeFam; TF323985; -.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
PRO; PR:Q9JJV9; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032511; Expressed in 136 organ(s), highest expression level in heart.
ExpressionAtlas; Q9JJV9; baseline and differential.
Genevisible; Q9JJV9; MM.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0016328; C:lateral plasma membrane; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0042383; C:sarcolemma; ISO:MGI.
GO; GO:0034706; C:sodium channel complex; IPI:MGI.
GO; GO:0030315; C:T-tubule; IDA:MGI.
GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:MGI.
GO; GO:0030018; C:Z disc; ISO:MGI.
GO; GO:0030506; F:ankyrin binding; ISO:MGI.
GO; GO:0005516; F:calmodulin binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
GO; GO:0086060; F:voltage-gated sodium channel activity involved in AV node cell action potential; ISO:MGI.
GO; GO:0086061; F:voltage-gated sodium channel activity involved in bundle of His cell action potential; ISO:MGI.
GO; GO:0086006; F:voltage-gated sodium channel activity involved in cardiac muscle cell action potential; IDA:MGI.
GO; GO:0086062; F:voltage-gated sodium channel activity involved in Purkinje myocyte action potential; ISO:MGI.
GO; GO:0086063; F:voltage-gated sodium channel activity involved in SA node cell action potential; IMP:MGI.
GO; GO:0086014; P:atrial cardiac muscle cell action potential; ISO:MGI.
GO; GO:0086016; P:AV node cell action potential; ISO:MGI.
GO; GO:0086067; P:AV node cell to bundle of His cell communication; ISO:MGI.
GO; GO:0086043; P:bundle of His cell action potential; ISO:MGI.
GO; GO:0055074; P:calcium ion homeostasis; IDA:MGI.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:MGI.
GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
GO; GO:0003231; P:cardiac ventricle development; IMP:MGI.
GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
GO; GO:0051899; P:membrane depolarization; ISO:MGI.
GO; GO:0086010; P:membrane depolarization during action potential; ISO:MGI.
GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; ISO:MGI.
GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISO:MGI.
GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; ISO:MGI.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISO:MGI.
GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; ISO:MGI.
GO; GO:0086046; P:membrane depolarization during SA node cell action potential; ISO:MGI.
GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
GO; GO:0045760; P:positive regulation of action potential; ISO:MGI.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
GO; GO:0010460; P:positive regulation of heart rate; ISO:MGI.
GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; ISO:MGI.
GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:MGI.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:MGI.
GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:MGI.
GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISO:MGI.
GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; ISO:MGI.
GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; ISO:MGI.
GO; GO:0014070; P:response to organic cyclic compound; IMP:MGI.
GO; GO:0086015; P:SA node cell action potential; ISO:MGI.
GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
GO; GO:0006814; P:sodium ion transport; IDA:MGI.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR008053; Na_channel_a5su.
InterPro; IPR001696; Na_channel_asu.
InterPro; IPR010526; Na_trans_assoc.
InterPro; IPR024583; Na_trans_cytopl.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF06512; Na_trans_assoc; 1.
Pfam; PF11933; Na_trans_cytopl; 1.
PRINTS; PR00170; NACHANNEL.
PRINTS; PR01666; NACHANNEL5.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; Cell membrane;
Complete proteome; Cytoplasm; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Methylation; Phosphoprotein;
Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
Voltage-gated channel.
CHAIN 1 2019 Sodium channel protein type 5 subunit
alpha.
/FTId=PRO_0000376895.
TOPO_DOM 1 131 Cytoplasmic. {ECO:0000305}.
TRANSMEM 132 150 Helical; Name=S1 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 151 157 Extracellular. {ECO:0000305}.
TRANSMEM 158 178 Helical; Name=S2 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 179 192 Cytoplasmic. {ECO:0000305}.
TRANSMEM 193 210 Helical; Name=S3 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 211 216 Extracellular. {ECO:0000305}.
TRANSMEM 217 233 Helical; Name=S4 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 234 252 Cytoplasmic. {ECO:0000305}.
TRANSMEM 253 272 Helical; Name=S5 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 273 357 Extracellular. {ECO:0000305}.
INTRAMEM 358 382 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 383 389 Extracellular. {ECO:0000305}.
TRANSMEM 390 410 Helical; Name=S6 of repeat I.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 411 717 Cytoplasmic. {ECO:0000305}.
TRANSMEM 718 736 Helical; Name=S1 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 737 747 Extracellular. {ECO:0000305}.
TRANSMEM 748 767 Helical; Name=S2 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 768 781 Cytoplasmic. {ECO:0000305}.
TRANSMEM 782 801 Helical; Name=S3 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 802 803 Extracellular. {ECO:0000305}.
TRANSMEM 804 821 Helical; Name=S4 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 822 837 Cytoplasmic. {ECO:0000305}.
TRANSMEM 838 856 Helical; Name=S5 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 857 885 Extracellular. {ECO:0000305}.
INTRAMEM 886 906 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 907 919 Extracellular. {ECO:0000305}.
TRANSMEM 920 940 Helical; Name=S6 of repeat II.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 941 1208 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1209 1226 Helical; Name=S1 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1227 1239 Extracellular. {ECO:0000305}.
TRANSMEM 1240 1258 Helical; Name=S2 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1259 1272 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1273 1291 Helical; Name=S3 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1292 1299 Extracellular. {ECO:0000305}.
TRANSMEM 1300 1318 Helical; Name=S4 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1319 1335 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1336 1355 Helical; Name=S5 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1356 1407 Extracellular. {ECO:0000305}.
INTRAMEM 1408 1429 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1430 1446 Extracellular. {ECO:0000305}.
TRANSMEM 1447 1468 Helical; Name=S6 of repeat III.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1469 1531 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1532 1549 Helical; Name=S1 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1550 1560 Extracellular. {ECO:0000305}.
TRANSMEM 1561 1579 Helical; Name=S2 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1580 1591 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1592 1609 Helical; Name=S3 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1610 1622 Extracellular. {ECO:0000305}.
TRANSMEM 1623 1639 Helical; Name=S4 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1640 1658 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1659 1676 Helical; Name=S5 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1677 1698 Extracellular. {ECO:0000305}.
INTRAMEM 1699 1721 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1722 1750 Extracellular. {ECO:0000305}.
TRANSMEM 1751 1773 Helical; Name=S6 of repeat IV.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1774 2019 Cytoplasmic. {ECO:0000305}.
REPEAT 113 420 I. {ECO:0000305}.
REPEAT 699 971 II. {ECO:0000305}.
REPEAT 1189 1503 III. {ECO:0000305}.
REPEAT 1512 1809 IV. {ECO:0000305}.
DOMAIN 1903 1932 IQ.
REGION 1841 1903 Interaction with FGF13.
{ECO:0000250|UniProtKB:Q14524}.
REGION 1977 1980 Interaction with NEDD4, NEDD4L and WWP2.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 38 38 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 457 457 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 486 486 Phosphothreonine.
{ECO:0000250|UniProtKB:P15389}.
MOD_RES 497 497 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 510 510 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 526 526 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 526 526 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 539 539 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 571 571 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 1505 1505 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q14524}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 740 740 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 803 803 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 864 864 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1367 1367 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1376 1376 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1382 1382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1390 1390 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 280 335 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 908 917 {ECO:0000250|UniProtKB:D0E0C2}.
VAR_SEQ 206 211 TTEFVD -> VSENIK (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_037444.
CONFLICT 215 215 V -> L (in Ref. 2; BAE27966/BAE27800).
{ECO:0000305}.
CONFLICT 234 234 S -> P (in Ref. 2; BAE27966/BAE27800).
{ECO:0000305}.
CONFLICT 1008 1009 AA -> TT (in Ref. 1; CAB70096).
{ECO:0000305}.
CONFLICT 1078 1078 K -> KQ (in Ref. 2; BAE27966/BAE27800).
{ECO:0000305}.
CONFLICT 1133 1133 T -> S (in Ref. 1; CAB70096).
{ECO:0000305}.
SEQUENCE 2019 AA; 227576 MW; 5A3BC3C191859E79 CRC64;
MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSATSQ ESREGLPEEE APRPQLDLQA
SKKLPDLYGN PPRELIGEPL EDLDPFYSTQ KTFIVLNKGK TIFRFSATNA LYVLSPFHPV
RRAAVKILVH SLFSMLIMCT ILTNCVFMAQ HDPPPWTKYV EYTFTAIYTF ESLVKILARG
FCLHAFTFLR DPWNWLDFSV IVMAYTTEFV DLGNVSALRT FRVLRALKTI SVISGLKTIV
GALIQSVKKL ADVMVLTVFC LSVFALIGLQ LFMGNLRHKC VRNFTELNGT NGSVEADGIV
WNSLDVYLND PANYLLKNGT TDVLLCGNSS DAGTCPEGYR CLKAGENPDH GYTSFDSFAW
AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG SFYLVNLILA VVAMAYEEQN
QATIAETEEK EKRFQEAMEM LKKEHEALTI RGVDTVSRSS LEMSPLAPVT NHERRSKRRK
RLSSGTEDGG DDRLPKSDSE DGPRALNQLS LTHGLSRTSM RPRSSRGSIF TFRRRDQGSE
ADFADDENST AGESESHRTS LLVPWPLRRP STQGQPGFGT SAPGHVLNGK RNSTVDCNGV
VSLLGAGDAE ATSPGSHLLR PIVLDRPPDT TTPSEEPGGP QMLTPQAPCA DGFEEPGARQ
RALSAVSVLT SALEELEESH RKCPPCWNRF AQHYLIWECC PLWMSIKQKV KFVVMDPFAD
LTITMCIVLN TLFMALEHYN MTAEFEEMLQ VGNLVFTGIF TAEMTFKIIA LDPYYYFQQG
WNIFDSIIVI LSLMELGLSR MGNLSVLRSF RLLRVFKLAK SWPTLNTLIK IIGNSVGALG
NLTLVLAIIV FIFAVVGMQL FGKNYSELRH RISDSGLLPR WHMMDFFHAF LIIFRILCGE
WIETMWDCME VSGQSLCLLV FLLVMVIGNL VVLNLFLALL LSSFSADNLT APDEDGEMNN
LQLALARIQR GLRFVKRTTW DFCCGLLRRR PKKPAALATH SQLPSCIAAP RSPPPPEVEK
APPARKETRF EEDKRPGQGT PGDTEPVCVP IAVAESDTDD QEEDEENSLG TEEEESSKQE
SQVVSGGHEP PQEPRAWSQV SETTSSEAEA STSQADWQQE REAEPRAPGC GETPEDSYSE
GSTADMTNTA DLLEQIPDLG EDVKDPEDCF TEGCVRRCPC CMVDTTQAPG KVWWRLRKTC
YRIVEHSWFE TFIIFMILLS SGALAFEDIY LEERKTIKVL LEYADKMFTY VFVLEMLLKW
VAYGFKKYFT NAWCWLDFLI VDVSLVSLVA NTLGFAEMGP IKSLRTLRAL RPLRALSRFE
GMRVVVNALV GAIPSIMNVL LVCLIFWLIF SIMGVNLFAG KFGRCINQTE GDLPLNYTIV
NNKSECESFN VTGELYWTKV KVNFDNVGAG YLALLQVATF KGWMDIMYAA VDSRGYEEQP
QWEDNLYMYI YFVVFIIFGS FFTLNLFIGV IIDNFNQQKK KLGGQDIFMT EEQKKYYNAM
KKLGSKKPQK PIPRPLNKYQ GFIFDIVTKQ AFDVTIMFLI CLNMVTMMVE TDDQSPEKVN
ILAKINLLFV AIFTGECIVK MAALRHYYFT NSWNIFDFVV VILSIVGTVL SDIIQKYFFS
PTLFRVIRLA RIGRILRLIR GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIYSIFGMAN
FAYVKWEAGI DDMFNFQTFA NSMLCLFQIT TSAGWDGLLS PILNTGPPYC DPNLPNSNGS
RGNCGSPAVG ILFFTTYIII SFLIVVNMYI AIILENFSVA TEESTEPLSE DDFDMFYEIW
EKFDPEATQF IEYLALSDFA DALSEPLRIA KPNQISLINM DLPMVSGDRI HCMDILFAFT
KRVLGESGEM DALKIQMEEK FMAANPSKIS YEPITTTLRR KHEEVSATVI QRAFRRHLLQ
RSVKHASFLF RQQAGSSGLS DEDAPEREGL IAYMMNENFS RRSGPLSSSS ISSTSFPPSY
DSVTRATSDN LPVRASDYSR SEDLADFPPS PDRDRESIV


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