SCN3A_HUMAN
ID SCN3A_HUMAN Reviewed; 2000 AA.
AC Q9NY46; Q16142; Q53SX0; Q9BZB3; Q9C006; Q9NYK2; Q9P2J1; Q9UPD1; Q9Y6P4;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Sodium channel protein type 3 subunit alpha;
DE AltName: Full=Sodium channel protein brain III subunit alpha;
DE AltName: Full=Sodium channel protein type III subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subtype III;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.3;
GN Name=SCN3A; Synonyms=KIAA1356, NAC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Chen Y., Dale T.J., Romanos M.A., Whitaker W.R., Xie X., Clare J.J.;
RT "Cloning, distribution and functional analysis of the human brain type III
RT sodium channel from human brain.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Jeong S.-Y., Goto J., Kanazawa I.;
RT "Cloning of cDNA for human voltage-gated sodium channel alpha subunit,
RT SCN3A.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH NEDD4L, POSSIBLE UBIQUITINATION, AND MUTAGENESIS OF
RP TYR-1970.
RX PubMed=15548568; DOI=10.1152/ajpcell.00460.2004;
RA Rougier J.-S., van Bemmelen M.X., Bruce M.C., Jespersen T., Gavillet B.,
RA Apotheloz F., Cordonier S., Staub O., Rotin D., Abriel H.;
RT "Molecular determinants of voltage-gated sodium channel regulation by the
RT Nedd4/Nedd4-like proteins.";
RL Am. J. Physiol. 288:C692-C701(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANT
RP THR-606.
RX PubMed=11245985; DOI=10.1016/s0378-1119(00)00594-1;
RA Kasai N., Fukushima K., Ueki Y., Prasad S., Nosakowski J., Sugata K.,
RA Sugata A., Nishizaki K., Meyer N.C., Smith R.J.H.;
RT "Genomic structures of SCN2A and SCN3A -- candidate genes for deafness at
RT the DFNA16 locus.";
RL Gene 264:113-122(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1415 (ISOFORMS 2 AND 4).
RC TISSUE=Brain;
RX PubMed=9589372; DOI=10.1007/bf02737087;
RA Lu C.M., Brown G.B.;
RT "Isolation of a human-brain sodium-channel gene encoding two isoforms of
RT the subtype III alpha-subunit.";
RL J. Mol. Neurosci. 10:67-70(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1324-1413.
RC TISSUE=Placenta;
RX PubMed=8159690; DOI=10.1073/pnas.91.8.2975;
RA Malo M.S., Srivastava K., Andresen J.M., Chen X.N., Korenberg J.R.,
RA Ingram V.M.;
RT "Targeted gene walking by low stringency polymerase chain reaction:
RT assignment of a putative human brain sodium channel gene (SCN3A) to
RT chromosome 2q24-31.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2975-2979(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1482-2000.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1669-1750.
RC TISSUE=Kidney;
RA Tonkovich G.S., Kyle J.W.;
RT "Endogenous sodium current in HEK293 cells: increase in cell surface
RT expression of endogenous currents by stable transfection of the Beta 1
RT subunit.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP INVOLVEMENT IN FFEVF4, FUNCTION, AND VARIANTS FFEVF4 GLN-357; ASN-815;
RP LYS-1160 AND VAL-1372.
RX PubMed=24157691; DOI=10.1016/j.nbd.2013.10.015;
RA Vanoye C.G., Gurnett C.A., Holland K.D., George A.L. Jr., Kearney J.A.;
RT "Novel SCN3A variants associated with focal epilepsy in children.";
RL Neurobiol. Dis. 62:313-322(2014).
RN [11]
RP INTERACTION WITH THE CONOTOXIN GVIIJ.
RX PubMed=24497506; DOI=10.1073/pnas.1324189111;
RA Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
RA Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
RA Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G., Wickenden A.D.,
RA Olivera B.M., Yoshikami D., Zhang M.M.;
RT "A disulfide tether stabilizes the block of sodium channels by the
RT conotoxin muO[section sign]-GVIIJ.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
RN [12]
RP INVOLVEMENT IN FFEVF4, VARIANT FFEVF4 PRO-247, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=28235671; DOI=10.1016/j.nbd.2017.02.006;
RA Lamar T., Vanoye C.G., Calhoun J., Wong J.C., Dutton S.B.B., Jorge B.S.,
RA Velinov M., Escayg A., Kearney J.A.;
RT "SCN3A deficiency associated with increased seizure susceptibility.";
RL Neurobiol. Dis. 102:38-48(2017).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=29142310; DOI=10.1038/s41598-017-15834-3;
RA Strege P.R., Knutson K., Eggers S.J., Li J.H., Wang F., Linden D.,
RA Szurszewski J.H., Milescu L., Leiter A.B., Farrugia G., Beyder A.;
RT "1.3 is important for enterochromaffin cell excitability and serotonin
RT release.";
RL Sci. Rep. 7:15650-15650(2017).
RN [14]
RP INVOLVEMENT IN DEE62, VARIANTS DEE62 THR-875; LEU-1333; CYS-1642; ALA-1769
RP AND GLN-1799, CHARACTERIZATION OF VARIANTS DEE62 THR-875; LEU-1333;
RP CYS-1642; ALA-1769 AND GLN-1799, AND FUNCTION.
RX PubMed=29466837; DOI=10.1002/ana.25188;
RA Zaman T., Helbig I., Bozovic I.B., DeBrosse S.D., Bergqvist A.C.,
RA Wallis K., Medne L., Maver A., Peterlin B., Helbig K.L., Zhang X.,
RA Goldberg E.M.;
RT "Mutations in SCN3A cause early infantile epileptic encephalopathy.";
RL Ann. Neurol. 83:703-717(2018).
RN [15]
RP VARIANTS ASN-43 DEL AND SER-1813.
RX PubMed=12610651; DOI=10.1038/sj.mp.4001241;
RA Weiss L.A., Escayg A., Kearney J.A., Trudeau M., MacDonald B.T., Mori M.,
RA Reichert J., Buxbaum J.D., Meisler M.H.;
RT "Sodium channels SCN1A, SCN2A and SCN3A in familial autism.";
RL Mol. Psychiatry 8:186-194(2003).
RN [16]
RP VARIANT ILE-1084.
RX PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
RA Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
RA Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
RT "Homozygous missense mutation in the LMAN2L gene segregates with
RT intellectual disability in a large consanguineous Pakistani family.";
RL J. Med. Genet. 53:138-144(2016).
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, forms a sodium-
CC selective channel through which Na(+) ions may pass in accordance with
CC their electrochemical gradient (PubMed:24157691, PubMed:28235671,
CC PubMed:29466837). May contribute to the regulation of serotonin/5-
CC hydroxytryptamine release by enterochromaffin cells (By similarity). In
CC pancreatic endocrine cells, required for both glucagon and glucose-
CC induced insulin secretion (By similarity).
CC {ECO:0000250|UniProtKB:A2ASI5, ECO:0000269|PubMed:24157691,
CC ECO:0000269|PubMed:28235671, ECO:0000269|PubMed:29466837}.
CC -!- SUBUNIT: Heterooligomer of a large alpha subunit and 2-3 smaller beta
CC subunits. Heterooligomer with SCN2B or SCN4B; disulfide-linked.
CC Interacts with NEDD4L (PubMed:15548568). Interacts with the conotoxin
CC GVIIJ (PubMed:24497506). {ECO:0000269|PubMed:15548568,
CC ECO:0000269|PubMed:24497506}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28235671};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Exons 6A and 6N only differ by a single residue.;
CC Name=1; Synonyms=6A-12+12b;
CC IsoId=Q9NY46-1; Sequence=Displayed;
CC Name=2; Synonyms=6A-12;
CC IsoId=Q9NY46-2; Sequence=VSP_001034;
CC Name=3; Synonyms=6N-12+12b;
CC IsoId=Q9NY46-3; Sequence=VSP_001033;
CC Name=4; Synonyms=6N-12;
CC IsoId=Q9NY46-4; Sequence=VSP_001033, VSP_001034;
CC -!- TISSUE SPECIFICITY: Expressed in enterochromaffin cells in both colon
CC and small bowel (at protein level). {ECO:0000269|PubMed:29142310}.
CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000305}.
CC -!- PTM: May be ubiquitinated by NEDD4L; which would promote its
CC endocytosis. {ECO:0000269|PubMed:15548568}.
CC -!- PTM: Phosphorylation at Ser-1501 by PKC in a highly conserved
CC cytoplasmic loop slows inactivation of the sodium channel and reduces
CC peak sodium currents. {ECO:0000250}.
CC -!- DISEASE: Epilepsy, familial focal, with variable foci 4 (FFEVF4)
CC [MIM:617935]: An autosomal dominant form of epilepsy characterized by
CC focal seizures arising from different cortical regions, including the
CC temporal, frontal, parietal, and occipital lobes. Seizure types
CC commonly include temporal lobe epilepsy, frontal lobe epilepsy, and
CC nocturnal frontal lobe epilepsy. Some patients may have intellectual
CC disability or autism spectrum disorders. Seizure onset usually occurs
CC in the first or second decades, although later onset has been reported,
CC and there is phenotypic variability within families. A subset of
CC patients have structural brain abnormalities. Penetrance of the
CC disorder is incomplete. FFEVF4 is characterized by onset of focal
CC seizures in the first years of life. {ECO:0000269|PubMed:24157691,
CC ECO:0000269|PubMed:28235671}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Developmental and epileptic encephalopathy 62 (DEE62)
CC [MIM:617938]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE62 is characterized by onset of seizures in the
CC first year of life. {ECO:0000269|PubMed:29466837}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.3/SCN3A subfamily. {ECO:0000305}.
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DR EMBL; AJ251507; CAB85895.1; -; mRNA.
DR EMBL; AF225987; AAK00219.1; -; mRNA.
DR EMBL; AF330135; AAG53414.1; -; Genomic_DNA.
DR EMBL; AF330118; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330119; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330120; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330121; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330122; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330123; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330124; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330125; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330126; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330127; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330128; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330129; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330130; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330131; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330132; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330133; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330134; AAG53414.1; JOINED; Genomic_DNA.
DR EMBL; AF330135; AAG53415.1; -; Genomic_DNA.
DR EMBL; AF330118; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330119; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330120; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330121; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330122; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330123; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330124; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330125; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330126; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330127; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330128; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330129; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330130; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330131; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330132; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330133; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AF330134; AAG53415.1; JOINED; Genomic_DNA.
DR EMBL; AC013463; AAY15072.1; -; Genomic_DNA.
DR EMBL; AF035685; AAC29514.1; -; mRNA.
DR EMBL; AF035686; AAC29515.1; -; mRNA.
DR EMBL; S69887; AAB30530.1; -; Genomic_DNA.
DR EMBL; AB037777; BAA92594.1; -; mRNA.
DR EMBL; AF239921; AAF44690.1; -; mRNA.
DR CCDS; CCDS33312.1; -. [Q9NY46-3]
DR CCDS; CCDS46440.1; -. [Q9NY46-2]
DR PIR; A54937; A54937.
DR RefSeq; NP_001075145.1; NM_001081676.1. [Q9NY46-4]
DR RefSeq; NP_001075146.1; NM_001081677.1. [Q9NY46-2]
DR RefSeq; NP_008853.3; NM_006922.3. [Q9NY46-3]
DR RefSeq; XP_011509912.1; XM_011511610.2. [Q9NY46-3]
DR RefSeq; XP_016860149.1; XM_017004660.1. [Q9NY46-1]
DR PDB; 7W77; EM; 3.30 A; D=1-1951.
DR PDB; 7W7F; EM; 3.35 A; D=1-2000.
DR PDBsum; 7W77; -.
DR PDBsum; 7W7F; -.
DR AlphaFoldDB; Q9NY46; -.
DR BMRB; Q9NY46; -.
DR SMR; Q9NY46; -.
DR BioGRID; 112233; 12.
DR IntAct; Q9NY46; 6.
DR MINT; Q9NY46; -.
DR STRING; 9606.ENSP00000283254; -.
DR BindingDB; Q9NY46; -.
DR ChEMBL; CHEMBL5163; -.
DR DrugBank; DB09088; Amylocaine.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB05541; Brivaracetam.
DR DrugBank; DB00564; Carbamazepine.
DR DrugBank; DB00907; Cocaine.
DR DrugBank; DB13269; Dichlorobenzyl alcohol.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB06218; Lacosamide.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB00776; Oxcarbazepine.
DR DrugBank; DB11186; Pentoxyverine.
DR DrugBank; DB00252; Phenytoin.
DR DrugBank; DB09345; Pramocaine.
DR DrugBank; DB01069; Promethazine.
DR DrugBank; DB09342; Propoxycaine.
DR DrugBank; DB00243; Ranolazine.
DR DrugBank; DB09085; Tetracaine.
DR DrugBank; DB05232; Tetrodotoxin.
DR DrugBank; DB00273; Topiramate.
DR DrugBank; DB00313; Valproic acid.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; Q9NY46; -.
DR GuidetoPHARMACOLOGY; 580; -.
DR GlyGen; Q9NY46; 8 sites.
DR iPTMnet; Q9NY46; -.
DR PhosphoSitePlus; Q9NY46; -.
DR BioMuta; SCN3A; -.
DR DMDM; 25014054; -.
DR jPOST; Q9NY46; -.
DR MassIVE; Q9NY46; -.
DR PaxDb; Q9NY46; -.
DR PeptideAtlas; Q9NY46; -.
DR PRIDE; Q9NY46; -.
DR ProteomicsDB; 83165; -. [Q9NY46-1]
DR ProteomicsDB; 83166; -. [Q9NY46-2]
DR ProteomicsDB; 83167; -. [Q9NY46-3]
DR ProteomicsDB; 83168; -. [Q9NY46-4]
DR Antibodypedia; 33767; 135 antibodies from 25 providers.
DR DNASU; 6328; -.
DR Ensembl; ENST00000283254.12; ENSP00000283254.7; ENSG00000153253.19. [Q9NY46-3]
DR Ensembl; ENST00000409101.7; ENSP00000386726.3; ENSG00000153253.19. [Q9NY46-2]
DR GeneID; 6328; -.
DR KEGG; hsa:6328; -.
DR MANE-Select; ENST00000283254.12; ENSP00000283254.7; NM_006922.4; NP_008853.3. [Q9NY46-3]
DR UCSC; uc002ucx.4; human. [Q9NY46-1]
DR CTD; 6328; -.
DR DisGeNET; 6328; -.
DR GeneCards; SCN3A; -.
DR GeneReviews; SCN3A; -.
DR HGNC; HGNC:10590; SCN3A.
DR HPA; ENSG00000153253; Group enriched (brain, lymphoid tissue).
DR MalaCards; SCN3A; -.
DR MIM; 182391; gene.
DR MIM; 617935; phenotype.
DR MIM; 617938; phenotype.
DR neXtProt; NX_Q9NY46; -.
DR OpenTargets; ENSG00000153253; -.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA35005; -.
DR VEuPathDB; HostDB:ENSG00000153253; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000157130; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR InParanoid; Q9NY46; -.
DR OMA; AFETNIT; -.
DR OrthoDB; 56920at2759; -.
DR PhylomeDB; Q9NY46; -.
DR TreeFam; TF323985; -.
DR PathwayCommons; Q9NY46; -.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-HSA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR SignaLink; Q9NY46; -.
DR SIGNOR; Q9NY46; -.
DR BioGRID-ORCS; 6328; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; SCN3A; human.
DR GeneWiki; SCN3A; -.
DR GenomeRNAi; 6328; -.
DR Pharos; Q9NY46; Tclin.
DR PRO; PR:Q9NY46; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NY46; protein.
DR Bgee; ENSG00000153253; Expressed in endothelial cell and 149 other tissues.
DR ExpressionAtlas; Q9NY46; baseline and differential.
DR Genevisible; Q9NY46; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Epilepsy; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Sodium;
KW Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..2000
FT /note="Sodium channel protein type 3 subunit alpha"
FT /id="PRO_0000048493"
FT TOPO_DOM 1..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..147
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 148..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 176..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..207
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 208..213
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 214..230
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 231..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 250..269
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 270..368
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 369..393
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 394..400
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 401..421
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 422..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 761..779
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 780..790
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 791..810
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 811..824
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 825..844
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 845..846
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 847..864
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 865..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 881..899
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 900..928
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 929..949
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 950..962
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 963..983
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 984..1207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1208..1225
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1226..1238
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1239..1257
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1258..1271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1272..1290
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1291..1298
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1299..1317
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1318..1334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1335..1354
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1355..1403
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1404..1425
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1426..1442
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1443..1464
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1465..1527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1528..1545
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1546..1556
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1557..1575
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1576..1587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1588..1605
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1606..1618
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1619..1635
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1636..1654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1655..1672
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1673..1694
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1695..1717
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1718..1747
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1748..1770
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1771..2000
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 110..455
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 742..1014
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1188..1499
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1508..1806
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1900..1929
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 28..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1949..2000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1949..1972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1973..2000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08104"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08104"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08104"
FT MOD_RES 1501
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..346
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 911
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 911
FT /note="Interchain; with the conotoxin GVIIJ (when the
FT channel is not linked to SCN2B or SCN4B; the bond to SCN2B
FT or SCN4B protects the channel from the inhibition by
FT toxin)"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 951..960
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT VAR_SEQ 208
FT /note="S -> D (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9589372, ECO:0000303|Ref.2"
FT /id="VSP_001033"
FT VAR_SEQ 625..673
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9589372, ECO:0000303|Ref.1"
FT /id="VSP_001034"
FT VARIANT 43
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:12610651"
FT /id="VAR_029743"
FT VARIANT 247
FT /note="L -> P (in FFEVF4; loss of localization at the cell
FT surface)"
FT /evidence="ECO:0000269|PubMed:28235671"
FT /id="VAR_080503"
FT VARIANT 357
FT /note="R -> Q (in FFEVF4; affects voltage-dependent sodium
FT channel activity; smaller current density and slower
FT activation compared to wild-type channels and increased
FT current activation in response to depolarizing voltage
FT ramps; dbSNP:rs774195502)"
FT /evidence="ECO:0000269|PubMed:24157691"
FT /id="VAR_080504"
FT VARIANT 606
FT /note="S -> T"
FT /evidence="ECO:0000269|PubMed:11245985"
FT /id="VAR_014275"
FT VARIANT 815
FT /note="D -> N (in FFEVF4; unknown pathological
FT significance; increased current activation in response to
FT depolarizing voltage ramps; dbSNP:rs755440336)"
FT /evidence="ECO:0000269|PubMed:24157691"
FT /id="VAR_080505"
FT VARIANT 875
FT /note="I -> T (in DEE62; prominent gain of channel
FT function, with markedly increased amplitude of the slowly
FT inactivating current component and a leftward shift in the
FT voltage dependence of activation to more hyperpolarized
FT potentials; dbSNP:rs1057518801)"
FT /evidence="ECO:0000269|PubMed:29466837"
FT /id="VAR_080506"
FT VARIANT 1084
FT /note="V -> I (in dbSNP:rs140990288)"
FT /evidence="ECO:0000269|PubMed:26566883"
FT /id="VAR_076435"
FT VARIANT 1107
FT /note="V -> A (in dbSNP:rs12474273)"
FT /id="VAR_029744"
FT VARIANT 1160
FT /note="E -> K (in FFEVF4; affects voltage-dependent sodium
FT channel activity; increased level of persistent sodium
FT current compared to wild-type channels and increased
FT current activation in response to depolarizing voltage
FT ramps; dbSNP:rs377632429)"
FT /evidence="ECO:0000269|PubMed:24157691"
FT /id="VAR_080507"
FT VARIANT 1333
FT /note="P -> L (in DEE62; prominent gain of channel
FT function, with markedly increased amplitude of the slowly
FT inactivating current component and a leftward shift in the
FT voltage dependence of activation to more hyperpolarized
FT potentials; dbSNP:rs1057520753)"
FT /evidence="ECO:0000269|PubMed:29466837"
FT /id="VAR_080508"
FT VARIANT 1372
FT /note="M -> V (in FFEVF4; unknown pathological
FT significance; increased current activation in response to
FT depolarizing voltage ramps; dbSNP:rs758906955)"
FT /evidence="ECO:0000269|PubMed:24157691"
FT /id="VAR_080509"
FT VARIANT 1642
FT /note="R -> C (in DEE62; unknown pathological significance;
FT no gain of function in channel activity; channel recovery
FT from inactivation is more rapid than that of wild-type
FT channel; dbSNP:rs1312429782)"
FT /evidence="ECO:0000269|PubMed:29466837"
FT /id="VAR_080510"
FT VARIANT 1769
FT /note="V -> A (in DEE62; prominent gain of channel
FT function, with markedly increased amplitude of the slowly
FT inactivating current component; dbSNP:rs1553517274)"
FT /evidence="ECO:0000269|PubMed:29466837"
FT /id="VAR_080511"
FT VARIANT 1799
FT /note="K -> Q (in DEE62; unknown pathological significance;
FT no gain of function in channel activity;
FT dbSNP:rs1170839078)"
FT /evidence="ECO:0000269|PubMed:29466837"
FT /id="VAR_080512"
FT VARIANT 1803
FT /note="D -> N (in dbSNP:rs3731762)"
FT /id="VAR_055640"
FT VARIANT 1813
FT /note="L -> S"
FT /evidence="ECO:0000269|PubMed:12610651"
FT /id="VAR_029745"
FT MUTAGEN 1970
FT /note="Y->A: Abolishes interaction with NEDD4L."
FT /evidence="ECO:0000269|PubMed:15548568"
FT CONFLICT 175
FT /note="A -> V (in Ref. 4; AAC29514/AAC29515)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="Y -> N (in Ref. 4; AAC29514/AAC29515)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="M -> T (in Ref. 4; AAC29514/AAC29515)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="I -> V (in Ref. 2; AAK00219)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="S -> G (in Ref. 2; AAK00219)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="S -> G (in Ref. 2; AAK00219)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="V -> E (in Ref. 4; AAC29514/AAC29515)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="E -> A (in Ref. 4; AAC29514/AAC29515)"
FT /evidence="ECO:0000305"
FT CONFLICT 1163
FT /note="L -> F (in Ref. 2; AAK00219)"
FT /evidence="ECO:0000305"
FT CONFLICT 1274
FT /note="W -> R (in Ref. 4; AAC29514/AAC29515)"
FT /evidence="ECO:0000305"
FT CONFLICT 1329
FT /note="V -> L (in Ref. 6; AAB30530)"
FT /evidence="ECO:0000305"
FT CONFLICT 1414..1415
FT /note="AT -> VS (in Ref. 4; AAC29514/AAC29515)"
FT /evidence="ECO:0000305"
FT CONFLICT 1614
FT /note="F -> S (in Ref. 2; AAK00219)"
FT /evidence="ECO:0000305"
FT CONFLICT 1741..1743
FT /note="CGN -> RGD (in Ref. 2; AAK00219)"
FT /evidence="ECO:0000305"
FT CONFLICT 1862
FT /note="G -> C (in Ref. 2; AAK00219)"
FT /evidence="ECO:0000305"
FT CONFLICT 1966
FT /note="S -> P (in Ref. 2; AAK00219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2000 AA; 226294 MW; F754A1C7D49ECB58 CRC64;
MAQALLVPPG PESFRLFTRE SLAAIEKRAA EEKAKKPKKE QDNDDENKPK PNSDLEAGKN
LPFIYGDIPP EMVSEPLEDL DPYYINKKTF IVMNKGKAIF RFSATSALYI LTPLNPVRKI
AIKILVHSLF SMLIMCTILT NCVFMTLSNP PDWTKNVEYT FTGIYTFESL IKILARGFCL
EDFTFLRDPW NWLDFSVIVM AYVTEFVSLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCLQW PPSDSAFETN TTSYFNGTMD
SNGTFVNVTM STFNWKDYIG DDSHFYVLDG QKDPLLCGNG SDAGQCPEGY ICVKAGRNPN
YGYTSFDTFS WAFLSLFRLM TQDYWENLYQ LTLRAAGKTY MIFFVLVIFL GSFYLVNLIL
AVVAMAYEEQ NQATLEEAEQ KEAEFQQMLE QLKKQQEEAQ AVAAASAASR DFSGIGGLGE
LLESSSEASK LSSKSAKEWR NRRKKRRQRE HLEGNNKGER DSFPKSESED SVKRSSFLFS
MDGNRLTSDK KFCSPHQSLL SIRGSLFSPR RNSKTSIFSF RGRAKDVGSE NDFADDEHST
FEDSESRRDS LFVPHRHGER RNSNVSQASM SSRMVPGLPA NGKMHSTVDC NGVVSLVGGP
SALTSPTGQL PPEGTTTETE VRKRRLSSYQ ISMEMLEDSS GRQRAVSIAS ILTNTMEELE
ESRQKCPPCW YRFANVFLIW DCCDAWLKVK HLVNLIVMDP FVDLAITICI VLNTLFMAME
HYPMTEQFSS VLTVGNLVFT GIFTAEMVLK IIAMDPYYYF QEGWNIFDGI IVSLSLMELG
LSNVEGLSVL RSFRLLRVFK LAKSWPTLNM LIKIIGNSVG ALGNLTLVLA IIVFIFAVVG
MQLFGKSYKE CVCKINDDCT LPRWHMNDFF HSFLIVFRVL CGEWIETMWD CMEVAGQTMC
LIVFMLVMVI GNLVVLNLFL ALLLSSFSSD NLAATDDDNE MNNLQIAVGR MQKGIDYVKN
KMRECFQKAF FRKPKVIEIH EGNKIDSCMS NNTGIEISKE LNYLRDGNGT TSGVGTGSSV
EKYVIDENDY MSFINNPSLT VTVPIAVGES DFENLNTEEF SSESELEESK EKLNATSSSE
GSTVDVVLPR EGEQAETEPE EDLKPEACFT EGCIKKFPFC QVSTEEGKGK IWWNLRKTCY
SIVEHNWFET FIVFMILLSS GALAFEDIYI EQRKTIKTML EYADKVFTYI FILEMLLKWV
AYGFQTYFTN AWCWLDFLIV DVSLVSLVAN ALGYSELGAI KSLRTLRALR PLRALSRFEG
MRVVVNALVG AIPSIMNVLL VCLIFWLIFS IMGVNLFAGK FYHCVNMTTG NMFDISDVNN
LSDCQALGKQ ARWKNVKVNF DNVGAGYLAL LQVATFKGWM DIMYAAVDSR DVKLQPVYEE
NLYMYLYFVI FIIFGSFFTL NLFIGVIIDN FNQQKKKFGG QDIFMTEEQK KYYNAMKKLG
SKKPQKPIPR PANKFQGMVF DFVTRQVFDI SIMILICLNM VTMMVETDDQ GKYMTLVLSR
INLVFIVLFT GEFVLKLVSL RHYYFTIGWN IFDFVVVILS IVGMFLAEMI EKYFVSPTLF
RVIRLARIGR ILRLIKGAKG IRTLLFALMM SLPALFNIGL LLFLVMFIYA IFGMSNFAYV
KKEAGIDDMF NFETFGNSMI CLFQITTSAG WDGLLAPILN SAPPDCDPDT IHPGSSVKGD
CGNPSVGIFF FVSYIIISFL VVVNMYIAVI LENFSVATEE SAEPLSEDDF EMFYEVWEKF
DPDATQFIEF SKLSDFAAAL DPPLLIAKPN KVQLIAMDLP MVSGDRIHCL DILFAFTKRV
LGESGEMDAL RIQMEDRFMA SNPSKVSYEP ITTTLKRKQE EVSAAIIQRN FRCYLLKQRL
KNISSNYNKE AIKGRIDLPI KQDMIIDKLN GNSTPEKTDG SSSTTSPPSY DSVTKPDKEK
FEKDKPEKES KGKEVRENQK
